Antimicrobial peptides for combating drug-resistant bacterial infections
The problem of drug resistance due to long-term use of antibiotics has been a concern for years. As this problem grows worse, infections caused by multiple bacteria are expanding rapidly and are extremely detrimental to human health. Antimicrobial peptides (AMPs) are a good alternative to current an...
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| Published in | Drug resistance updates Vol. 68; p. 100954 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Scotland
Elsevier Ltd
01.05.2023
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| Subjects | |
| Online Access | Get full text |
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| Abstract | The problem of drug resistance due to long-term use of antibiotics has been a concern for years. As this problem grows worse, infections caused by multiple bacteria are expanding rapidly and are extremely detrimental to human health. Antimicrobial peptides (AMPs) are a good alternative to current antimicrobials with potent antimicrobial activity and unique antimicrobial mechanisms, which have advantages over traditional antibiotics in fighting against drug-resistant bacterial infections. Currently, researchers have conducted clinical investigations on AMPs for drug-resistant bacterial infections while integrating new technologies in the development of AMPs, such as changing amino acid structure of AMPs and using different delivery methods for AMPs. This article introduces the basic properties of AMPs, deliberates the mechanism of drug resistance in bacteria and the therapeutic mechanism of AMPs. The current disadvantages and advances of AMPs in combating drug-resistant bacterial infections are also discussed. This article provides important insights into the research and clinical application of new AMPs for drug-resistant bacterial infections. |
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| AbstractList | The problem of drug resistance due to long-term use of antibiotics has been a concern for years. As this problem grows worse, infections caused by multiple bacteria are expanding rapidly and are extremely detrimental to human health. Antimicrobial peptides (AMPs) are a good alternative to current antimicrobials with potent antimicrobial activity and unique antimicrobial mechanisms, which have advantages over traditional antibiotics in fighting against drug-resistant bacterial infections. Currently, researchers have conducted clinical investigations on AMPs for drug-resistant bacterial infections while integrating new technologies in the development of AMPs, such as changing amino acid structure of AMPs and using different delivery methods for AMPs. This article introduces the basic properties of AMPs, deliberates the mechanism of drug resistance in bacteria and the therapeutic mechanism of AMPs. The current disadvantages and advances of AMPs in combating drug-resistant bacterial infections are also discussed. This article provides important insights into the research and clinical application of new AMPs for drug-resistant bacterial infections. The problem of drug resistance due to long-term use of antibiotics has been a concern for years. As this problem grows worse, infections caused by multiple bacteria are expanding rapidly and are extremely detrimental to human health. Antimicrobial peptides (AMPs) are a good alternative to current antimicrobials with potent antimicrobial activity and unique antimicrobial mechanisms, which have advantages over traditional antibiotics in fighting against drug-resistant bacterial infections. Currently, researchers have conducted clinical investigations on AMPs for drug-resistant bacterial infections while integrating new technologies in the development of AMPs, such as changing amino acid structure of AMPs and using different delivery methods for AMPs. This article introduces the basic properties of AMPs, deliberates the mechanism of drug resistance in bacteria and the therapeutic mechanism of AMPs. The current disadvantages and advances of AMPs in combating drug-resistant bacterial infections are also discussed. This article provides important insights into the research and clinical application of new AMPs for drug-resistant bacterial infections.The problem of drug resistance due to long-term use of antibiotics has been a concern for years. As this problem grows worse, infections caused by multiple bacteria are expanding rapidly and are extremely detrimental to human health. Antimicrobial peptides (AMPs) are a good alternative to current antimicrobials with potent antimicrobial activity and unique antimicrobial mechanisms, which have advantages over traditional antibiotics in fighting against drug-resistant bacterial infections. Currently, researchers have conducted clinical investigations on AMPs for drug-resistant bacterial infections while integrating new technologies in the development of AMPs, such as changing amino acid structure of AMPs and using different delivery methods for AMPs. This article introduces the basic properties of AMPs, deliberates the mechanism of drug resistance in bacteria and the therapeutic mechanism of AMPs. The current disadvantages and advances of AMPs in combating drug-resistant bacterial infections are also discussed. This article provides important insights into the research and clinical application of new AMPs for drug-resistant bacterial infections. |
| ArticleNumber | 100954 |
| Author | Wang, Ruichen Xuan, Jiaqi Sun, Leming Feng, Weiguo Chen, Zhe-Sheng Zhang, Bowen Wang, Jiaye Bo, Letao Yang, Hui |
| Author_xml | – sequence: 1 givenname: Jiaqi surname: Xuan fullname: Xuan, Jiaqi organization: School of Life Sciences, Engineering Research Center of Chinese Ministry of Education for Biological Diagnosis, Treatment and Protection Technology and Equipment in Special Environment, Northwestern Polytechnical University, Xi’an 710072, Shaanxi, China – sequence: 2 givenname: Weiguo surname: Feng fullname: Feng, Weiguo organization: School of Life Science and Technology, Weifang Medical University, Weifang 261053, Shandong, China – sequence: 3 givenname: Jiaye surname: Wang fullname: Wang, Jiaye organization: School of Life Sciences, Engineering Research Center of Chinese Ministry of Education for Biological Diagnosis, Treatment and Protection Technology and Equipment in Special Environment, Northwestern Polytechnical University, Xi’an 710072, Shaanxi, China – sequence: 4 givenname: Ruichen surname: Wang fullname: Wang, Ruichen organization: School of Life Sciences, Engineering Research Center of Chinese Ministry of Education for Biological Diagnosis, Treatment and Protection Technology and Equipment in Special Environment, Northwestern Polytechnical University, Xi’an 710072, Shaanxi, China – sequence: 5 givenname: Bowen surname: Zhang fullname: Zhang, Bowen organization: School of Life Sciences, Engineering Research Center of Chinese Ministry of Education for Biological Diagnosis, Treatment and Protection Technology and Equipment in Special Environment, Northwestern Polytechnical University, Xi’an 710072, Shaanxi, China – sequence: 6 givenname: Letao surname: Bo fullname: Bo, Letao organization: Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John’s University, Queens, NY 11439, USA – sequence: 7 givenname: Zhe-Sheng surname: Chen fullname: Chen, Zhe-Sheng email: chenz@stjohns.edu organization: Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John’s University, Queens, NY 11439, USA – sequence: 8 givenname: Hui surname: Yang fullname: Yang, Hui email: kittyyh@nwpu.edu.cn organization: School of Life Sciences, Engineering Research Center of Chinese Ministry of Education for Biological Diagnosis, Treatment and Protection Technology and Equipment in Special Environment, Northwestern Polytechnical University, Xi’an 710072, Shaanxi, China – sequence: 9 givenname: Leming orcidid: 0000-0002-3188-9557 surname: Sun fullname: Sun, Leming email: lmsun@nwpu.edu.cn organization: School of Life Sciences, Engineering Research Center of Chinese Ministry of Education for Biological Diagnosis, Treatment and Protection Technology and Equipment in Special Environment, Northwestern Polytechnical University, Xi’an 710072, Shaanxi, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36905712$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.3390/molecules23020414 10.3390/antibiotics11040520 10.1128/AAC.49.7.2845-2850.2005 10.1073/pnas.1909585117 10.4049/jimmunol.169.7.3883 10.1007/978-1-62703-583-5_9 10.1007/s002030050418 10.1016/S0167-0115(00)00107-5 10.1016/j.ijbiomac.2022.07.103 10.1007/s00249-015-1094-x 10.1016/j.jgar.2020.02.001 10.1039/C1CS15214A 10.3390/antibiotics9010024 10.7150/ijbs.23419 10.1039/b714132g 10.1146/annurev-biochem-061809-112742 10.1016/j.bbrc.2018.01.124 10.1128/CMR.00056-05 10.1080/07388551.2020.1796576 10.1007/s002329900201 10.1016/j.pharmthera.2021.107990 10.1128/AAC.00338-19 10.1038/s41598-018-34694-z 10.1039/C4RA02458C 10.3390/ma11122468 10.1096/fj.13-227942 10.1086/533452 10.1038/nsmb.3439 10.1099/mic.0.26265-0 10.1007/s00018-016-2344-5 10.1128/iai.65.7.2898-2903.1997 10.1074/jbc.M109.097204 10.1128/AAC.01436-08 10.4274/tjps.galenos.2020.43078 10.1016/j.ibmb.2019.04.017 10.1128/AAC.02434-15 10.1016/j.jaad.2020.08.132 10.1016/j.drudis.2019.08.004 10.1016/j.peptides.2018.05.011 10.3389/fmicb.2018.02723 10.1006/bbrc.2001.5884 10.1016/j.drudis.2009.10.009 10.1016/j.colsurfb.2017.02.003 10.1056/NEJM196204122661505 10.3390/pharmaceutics13111795 10.1016/j.tips.2019.04.012 10.1016/j.bbamem.2020.183282 10.1016/S0014-5793(99)01600-2 10.1128/AAC.00130-21 10.3390/ijms222111401 10.1016/S0140-6736(21)02724-0 10.1038/s41598-018-22409-3 10.12968/jowc.2010.19.8.77709 10.1016/j.toxicon.2007.06.023 10.1038/nbt1267 10.17264/stmarieng.11.133 10.1016/j.biochi.2010.02.023 10.1093/jac/dkm357 10.1128/AAC.01180-12 10.1016/j.tibtech.2011.05.001 10.1016/j.jhep.2016.08.006 10.1016/S1473-3099(13)70318-9 10.1016/S0002-9343(98)00351-9 10.1038/srep29707 10.1089/dna.2019.4874 10.1080/02713680590968637 10.1083/jcb.201709001 10.1086/518605 10.1093/nar/gkv1051 10.1016/j.drup.2020.100704 10.1038/nrmicro1441 10.1128/CMR.00064-16 10.4161/viru.2.5.17724 10.1016/j.actbio.2019.12.025 10.3389/fmicb.2017.01205 10.1128/AAC.01493-18 10.1098/rstb.2014.0086 10.1128/AAC.48.12.4673-4679.2004 10.1021/acs.biomac.8b00208 10.1016/j.peptides.2015.03.003 10.1186/s12866-019-1589-1 10.1038/35104690 10.1021/ja00897a025 10.1038/s41429-019-0186-8 10.1016/j.molimm.2009.05.019 10.1016/j.peptides.2012.07.005 10.1111/j.1742-4658.2009.07359.x 10.1016/j.cbpc.2005.11.022 10.1007/s13238-010-0004-3 10.1111/j.1365-2958.2006.05540.x 10.1039/D0CS00729C 10.4103/jisp.jisp_325_16 10.1074/jbc.271.45.28375 10.2147/IDR.S215084 10.1016/S0167-4838(01)00272-2 10.1126/scitranslmed.aan4044 10.1128/AAC.42.12.3320 10.1111/j.1742-4658.2009.07257.x 10.1371/journal.pone.0043514 10.3390/ph7050545 10.1007/978-1-4939-6737-7_4 10.3389/fchem.2021.691532 10.1038/s41579-018-0048-6 10.1016/j.intimp.2018.10.030 10.1016/j.peptides.2010.03.037 10.1007/s10068-018-0317-1 10.1073/pnas.84.15.5449 10.1016/j.ijantimicag.2012.02.003 10.1093/nar/gkv1278 10.1016/S0966-842X(00)01913-2 10.1016/j.bbagen.2019.02.013 10.1016/j.ijantimicag.2011.02.006 10.1007/978-1-4939-2285-7_3 10.1128/CMR.00006-08 10.1128/AAC.49.2.479-487.2005 10.3389/fmicb.2020.591426 10.1007/s10540-006-9030-z 10.1074/jbc.M111.248641 10.1034/j.1399-3011.2001.00947.x 10.1128/MMBR.67.4.593-656.2003 10.1016/j.bcp.2016.09.018 10.1007/s12272-016-0769-x 10.1002/cbdv.200790095 10.1016/j.regpep.2005.06.003 10.3390/toxins10110461 10.1016/j.bbapap.2010.01.015 10.1139/cjm-2020-0142 10.1038/srep40874 10.1016/j.bbamem.2019.05.008 |
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| References | Lee (bib60) 1997; 65 Coorens (bib17) 2017; 7 Kang (bib47) 2018; 62 Scott (bib105) 2002; 169 Lai (bib55) 2007; 63 Bechinger (bib6) 1997; 156 Du (bib23) 2018; 16 Payne (bib92) 2015; 370 Takahashi (bib120) 2018; 8 Conlon (bib14) 2006; 143 Li (bib63) 2016; 39 Luo, Song (bib67) 2021; 22 Zavascki (bib140) 2007; 60 Yu (bib137) 2016; 60 Bommineni (bib9) 2010; 31 Abbassi (bib1) 2010; 285 Leitgeb (bib61) 2007; 4 Yang, Donk (bib133) 2014; 44 T (bib118) 2017; 24 Kim (bib50) 2000; 90 Shiela (bib108) 2019; 19 Mahlapuu (bib69) 2020; 40 Lee (bib59) 2018; 217 Wang (bib128) 2015; 1268 Olson (bib90) 2001; 288 Zasloff (bib139) 1987; 84 Jangra (bib45) 2019; 63 Nguyen (bib87) 2011; 29 YJ (bib135) 2005; 30 Niemeyer-van der Kolk (bib89) 2022; 86 Mallapragada (bib70) 2017; 21 van Dijk (bib124) 2009; 46 Archer (bib5) 2011; 2 Stewart (bib113) 2021; 65 Skerlavaj (bib111) 1999; 463 Waghu (bib126) 2015; 44 Maturana (bib76) 2017; 153 Landman (bib56) 2008; 21 Hiroshi (bib39) 2003; 67 de Melo (bib18) 2015; 68 Shafee (bib106) 2017; 74 Nissen-Meyer, Nes (bib86) 1997; 167 Giacometti (bib32) 1998; 42 Wolinsky, Hines (bib131) 1962; 266 Mura (bib83) 2016; 45 Conlon (bib13) 2005; 131 Yuan (bib138) 2019; 1863 Marcellini (bib71) 2009; 276 Fadaka (bib27) 2021; 13 R (bib98) 2019; 72 J, DJ (bib43) 2019; 40 Ali (bib3) 2001; 1550 Menousek (bib78) 2012; 39 Skerlavaj (bib112) 1996; 271 Nicolas (bib88) 2009; 276 T, H (bib117) 2001; 21 Uddin, Ahn (bib123) 2018; 27 Ageitos (bib2) 2017; 133 Poirel (bib96) 2017; 30 Sun (bib115) 2018; 19 Zhao (bib143) 2009; 53 Conlon (bib16) 2012; 37 Rice (bib101) 2008; 197 Han (bib36) 2021; 40 Kim (bib51) 2001; 58 Harsh (bib38) 2017; 8 Mah, O'Toole (bib68) 2001; 9 Marks (bib73) 2012; 7 Deptuła (bib19) 2018; 23 Yasir (bib134) 2018; 11 Murray (bib84) 2022; 399 Ramesh (bib100) 2017; 1548 Kitano (bib52) 2020; 11 Raghuraman, Chattopadhyay (bib99) 2007; 27 Laxminarayan (bib57) 2013; 13 Takahashi (bib119) 2010; 92 Conlon (bib15) 2007; 50 Goldberg (bib33) 2013; 27 Wu (bib132) 2018; 10 Deshayes (bib20) 2021; 3 Mcintosh (bib77) 2009 Mwangi (bib85) 2019; 116 Huang (bib41) 2022; 11 Kwakman (bib54) 2011; 286 Diene (bib22) 2011; 37 Elsalem (bib25) 2022; 19 Martinez (bib74) 2019; 1861 Horna (bib40) 2018; 8 Perron (bib94) 2006; 273 Kumarasamy (bib53) 2010; 209 Sadelaji (bib103) 2022; 25 Sharma (bib107) 2021; 67 Gan (bib30) 2021; 50 Fca (bib28) 2019; 5 Deslouches, Di (bib21) 2017; 2 Porcelli (bib97) 2013; 1063 Zhang (bib142) 2018; 497 Mataraci, Dosler (bib75) 2012; 56 Peschel, Sahl (bib95) 2006; 4 Chen, Lu (bib10) 2020; 9 Jenssen (bib46) 2006; 19 Palomo (bib91) 2014; 62 Wang (bib127) 2014; 7 El Shazely (bib24) 2019; 110 Mishra (bib81) 2018; 106 Fernandez (bib29) 2016; 65 Pedersen (bib93) 2012; 41 Vlieghe (bib125) 2010; 15 Erica, C (bib26) 2006; 49 Jacobs (bib44) 1999; 106 Wang (bib129) 2015; 44 Lepeltier (bib62) 2020; 52 Sarkar (bib104) 2021; 9 Thapa (bib122) 2020; 103 Riool (bib102) 2020; 1862 Hamad (bib35) 2019; 24 Sieprawska-Lupa (bib109) 2004; 48 Thakur (bib121) 2022; 218 Mohamed (bib82) 2016; 6 Zhang (bib141) 2011; 31 Huang (bib42) 2010; 1 Gera (bib31) 2022; 232 Haisma (bib34) 2016; 4063–4072 Karen, A (bib48) 2020; 33 Lazzaro (bib58) 2020 Ciornei (bib12) 2005; 49 Bell, Gouyon (bib7) 2003; 149 Merrifield (bib80) 1963; 85 Chen (bib11) 2018; 14 Li (bib64) 2020; 11 Mermer (bib79) 2020; 22 Liu (bib65) 2018; 65 Hancock, Sahl (bib37) 2006; 24 Lovering (bib66) 2012; 81 Keith (bib49) 2005; 49 Maria (bib72) 2018; 9 BH (bib8) 2021; 50 Wolcott (bib130) 2010; 19 Swedan (bib116) 2019; 12 Subasinghage (bib114) 2010; 1804 Anna (bib4) 2018; 10 Yohei, Yoshichika (bib136) 2007; 45 Silphaduang, Noga (bib110) 2001; 414 Sun (10.1016/j.drup.2023.100954_bib115) 2018; 19 Leitgeb (10.1016/j.drup.2023.100954_bib61) 2007; 4 Kumarasamy (10.1016/j.drup.2023.100954_bib53) 2010; 209 Olson (10.1016/j.drup.2023.100954_bib90) 2001; 288 Lepeltier (10.1016/j.drup.2023.100954_bib62) 2020; 52 Sieprawska-Lupa (10.1016/j.drup.2023.100954_bib109) 2004; 48 Zhang (10.1016/j.drup.2023.100954_bib142) 2018; 497 Du (10.1016/j.drup.2023.100954_bib23) 2018; 16 Riool (10.1016/j.drup.2023.100954_bib102) 2020; 1862 Shiela (10.1016/j.drup.2023.100954_bib108) 2019; 19 Harsh (10.1016/j.drup.2023.100954_bib38) 2017; 8 Rice (10.1016/j.drup.2023.100954_bib101) 2008; 197 Menousek (10.1016/j.drup.2023.100954_bib78) 2012; 39 Horna (10.1016/j.drup.2023.100954_bib40) 2018; 8 Lai (10.1016/j.drup.2023.100954_bib55) 2007; 63 Deptuła (10.1016/j.drup.2023.100954_bib19) 2018; 23 Scott (10.1016/j.drup.2023.100954_bib105) 2002; 169 Hiroshi (10.1016/j.drup.2023.100954_bib39) 2003; 67 Pedersen (10.1016/j.drup.2023.100954_bib93) 2012; 41 Wu (10.1016/j.drup.2023.100954_bib132) 2018; 10 Sadelaji (10.1016/j.drup.2023.100954_bib103) 2022; 25 Coorens (10.1016/j.drup.2023.100954_bib17) 2017; 7 Erica (10.1016/j.drup.2023.100954_bib26) 2006; 49 BH (10.1016/j.drup.2023.100954_bib8) 2021; 50 Conlon (10.1016/j.drup.2023.100954_bib16) 2012; 37 Zhang (10.1016/j.drup.2023.100954_bib141) 2011; 31 Zasloff (10.1016/j.drup.2023.100954_bib139) 1987; 84 Mura (10.1016/j.drup.2023.100954_bib83) 2016; 45 Perron (10.1016/j.drup.2023.100954_bib94) 2006; 273 Waghu (10.1016/j.drup.2023.100954_bib126) 2015; 44 Swedan (10.1016/j.drup.2023.100954_bib116) 2019; 12 Huang (10.1016/j.drup.2023.100954_bib41) 2022; 11 Deshayes (10.1016/j.drup.2023.100954_bib20) 2021; 3 Marks (10.1016/j.drup.2023.100954_bib73) 2012; 7 Takahashi (10.1016/j.drup.2023.100954_bib119) 2010; 92 Ageitos (10.1016/j.drup.2023.100954_bib2) 2017; 133 Bechinger (10.1016/j.drup.2023.100954_bib6) 1997; 156 T (10.1016/j.drup.2023.100954_bib117) 2001; 21 Merrifield (10.1016/j.drup.2023.100954_bib80) 1963; 85 Mohamed (10.1016/j.drup.2023.100954_bib82) 2016; 6 Elsalem (10.1016/j.drup.2023.100954_bib25) 2022; 19 Ramesh (10.1016/j.drup.2023.100954_bib100) 2017; 1548 Yang (10.1016/j.drup.2023.100954_bib133) 2014; 44 Jacobs (10.1016/j.drup.2023.100954_bib44) 1999; 106 Yuan (10.1016/j.drup.2023.100954_bib138) 2019; 1863 Lazzaro (10.1016/j.drup.2023.100954_bib58) 2020 Nissen-Meyer (10.1016/j.drup.2023.100954_bib86) 1997; 167 Archer (10.1016/j.drup.2023.100954_bib5) 2011; 2 Porcelli (10.1016/j.drup.2023.100954_bib97) 2013; 1063 Stewart (10.1016/j.drup.2023.100954_bib113) 2021; 65 Lee (10.1016/j.drup.2023.100954_bib60) 1997; 65 T (10.1016/j.drup.2023.100954_bib118) 2017; 24 Liu (10.1016/j.drup.2023.100954_bib65) 2018; 65 Anna (10.1016/j.drup.2023.100954_bib4) 2018; 10 Thapa (10.1016/j.drup.2023.100954_bib122) 2020; 103 Bell (10.1016/j.drup.2023.100954_bib7) 2003; 149 Kang (10.1016/j.drup.2023.100954_bib47) 2018; 62 Raghuraman (10.1016/j.drup.2023.100954_bib99) 2007; 27 Fca (10.1016/j.drup.2023.100954_bib28) 2019; 5 Yasir (10.1016/j.drup.2023.100954_bib134) 2018; 11 Fernandez (10.1016/j.drup.2023.100954_bib29) 2016; 65 Bommineni (10.1016/j.drup.2023.100954_bib9) 2010; 31 Maria (10.1016/j.drup.2023.100954_bib72) 2018; 9 Skerlavaj (10.1016/j.drup.2023.100954_bib112) 1996; 271 Kwakman (10.1016/j.drup.2023.100954_bib54) 2011; 286 van Dijk (10.1016/j.drup.2023.100954_bib124) 2009; 46 de Melo (10.1016/j.drup.2023.100954_bib18) 2015; 68 Sharma (10.1016/j.drup.2023.100954_bib107) 2021; 67 Li (10.1016/j.drup.2023.100954_bib64) 2020; 11 Shafee (10.1016/j.drup.2023.100954_bib106) 2017; 74 Laxminarayan (10.1016/j.drup.2023.100954_bib57) 2013; 13 Conlon (10.1016/j.drup.2023.100954_bib13) 2005; 131 Nguyen (10.1016/j.drup.2023.100954_bib87) 2011; 29 Mermer (10.1016/j.drup.2023.100954_bib79) 2020; 22 Mishra (10.1016/j.drup.2023.100954_bib81) 2018; 106 Landman (10.1016/j.drup.2023.100954_bib56) 2008; 21 Hamad (10.1016/j.drup.2023.100954_bib35) 2019; 24 Jangra (10.1016/j.drup.2023.100954_bib45) 2019; 63 Palomo (10.1016/j.drup.2023.100954_bib91) 2014; 62 Wolcott (10.1016/j.drup.2023.100954_bib130) 2010; 19 Kitano (10.1016/j.drup.2023.100954_bib52) 2020; 11 YJ (10.1016/j.drup.2023.100954_bib135) 2005; 30 Peschel (10.1016/j.drup.2023.100954_bib95) 2006; 4 Poirel (10.1016/j.drup.2023.100954_bib96) 2017; 30 Mwangi (10.1016/j.drup.2023.100954_bib85) 2019; 116 Hancock (10.1016/j.drup.2023.100954_bib37) 2006; 24 Goldberg (10.1016/j.drup.2023.100954_bib33) 2013; 27 Huang (10.1016/j.drup.2023.100954_bib42) 2010; 1 Marcellini (10.1016/j.drup.2023.100954_bib71) 2009; 276 Han (10.1016/j.drup.2023.100954_bib36) 2021; 40 Kim (10.1016/j.drup.2023.100954_bib51) 2001; 58 Zhao (10.1016/j.drup.2023.100954_bib143) 2009; 53 Payne (10.1016/j.drup.2023.100954_bib92) 2015; 370 Chen (10.1016/j.drup.2023.100954_bib11) 2018; 14 Karen (10.1016/j.drup.2023.100954_bib48) 2020; 33 Vlieghe (10.1016/j.drup.2023.100954_bib125) 2010; 15 Sarkar (10.1016/j.drup.2023.100954_bib104) 2021; 9 Jenssen (10.1016/j.drup.2023.100954_bib46) 2006; 19 Takahashi (10.1016/j.drup.2023.100954_bib120) 2018; 8 Nicolas (10.1016/j.drup.2023.100954_bib88) 2009; 276 Conlon (10.1016/j.drup.2023.100954_bib15) 2007; 50 Giacometti (10.1016/j.drup.2023.100954_bib32) 1998; 42 Wang (10.1016/j.drup.2023.100954_bib127) 2014; 7 Maturana (10.1016/j.drup.2023.100954_bib76) 2017; 153 Abbassi (10.1016/j.drup.2023.100954_bib1) 2010; 285 Yohei (10.1016/j.drup.2023.100954_bib136) 2007; 45 Li (10.1016/j.drup.2023.100954_bib63) 2016; 39 Zavascki (10.1016/j.drup.2023.100954_bib140) 2007; 60 Deslouches (10.1016/j.drup.2023.100954_bib21) 2017; 2 Thakur (10.1016/j.drup.2023.100954_bib121) 2022; 218 Wang (10.1016/j.drup.2023.100954_bib129) 2015; 44 Gan (10.1016/j.drup.2023.100954_bib30) 2021; 50 Luo (10.1016/j.drup.2023.100954_bib67) 2021; 22 Skerlavaj (10.1016/j.drup.2023.100954_bib111) 1999; 463 Mcintosh (10.1016/j.drup.2023.100954_bib77) 2009 Silphaduang (10.1016/j.drup.2023.100954_bib110) 2001; 414 Keith (10.1016/j.drup.2023.100954_bib49) 2005; 49 Kim (10.1016/j.drup.2023.100954_bib50) 2000; 90 Conlon (10.1016/j.drup.2023.100954_bib14) 2006; 143 Lovering (10.1016/j.drup.2023.100954_bib66) 2012; 81 Diene (10.1016/j.drup.2023.100954_bib22) 2011; 37 Uddin (10.1016/j.drup.2023.100954_bib123) 2018; 27 Chen (10.1016/j.drup.2023.100954_bib10) 2020; 9 Niemeyer-van der Kolk (10.1016/j.drup.2023.100954_bib89) 2022; 86 Ciornei (10.1016/j.drup.2023.100954_bib12) 2005; 49 Subasinghage (10.1016/j.drup.2023.100954_bib114) 2010; 1804 Murray (10.1016/j.drup.2023.100954_bib84) 2022; 399 Wang (10.1016/j.drup.2023.100954_bib128) 2015; 1268 Martinez (10.1016/j.drup.2023.100954_bib74) 2019; 1861 Ali (10.1016/j.drup.2023.100954_bib3) 2001; 1550 El Shazely (10.1016/j.drup.2023.100954_bib24) 2019; 110 J (10.1016/j.drup.2023.100954_bib43) 2019; 40 Wolinsky (10.1016/j.drup.2023.100954_bib131) 1962; 266 Haisma (10.1016/j.drup.2023.100954_bib34) 2016; 4063–4072 Fadaka (10.1016/j.drup.2023.100954_bib27) 2021; 13 Mah (10.1016/j.drup.2023.100954_bib68) 2001; 9 Lee (10.1016/j.drup.2023.100954_bib59) 2018; 217 Mallapragada (10.1016/j.drup.2023.100954_bib70) 2017; 21 Mahlapuu (10.1016/j.drup.2023.100954_bib69) 2020; 40 Yu (10.1016/j.drup.2023.100954_bib137) 2016; 60 Mataraci (10.1016/j.drup.2023.100954_bib75) 2012; 56 R (10.1016/j.drup.2023.100954_bib98) 2019; 72 Gera (10.1016/j.drup.2023.100954_bib31) 2022; 232 |
| References_xml | – year: 2020 ident: bib58 article-title: Antimicrobial peptides: application informed by evolution publication-title: (6490), eaau5480 – volume: 86 start-page: 854 year: 2022 end-page: 862 ident: bib89 article-title: Topical antimicrobial peptide omiganan recovers cutaneous dysbiosis but does not improve clinical symptoms in patients with mild to moderate atopic dermatitis in a phase 2 randomized controlled trial publication-title: J. Am. Acad. Dermatol. – volume: 65 start-page: 2898 year: 1997 end-page: 2903 ident: bib60 article-title: Effects of pH and salinity on the antimicrobial properties of clavanins publication-title: Infect. Immun. – volume: 9 start-page: 34 year: 2001 end-page: 39 ident: bib68 article-title: Mechanisms of biofilm resistance to antimicrobial agents publication-title: Trends Microbiol. – volume: 288 start-page: 1001 year: 2001 end-page: 1005 ident: bib90 article-title: Pseudin-2: An Antimicrobial Peptide with Low Hemolytic Activity from the Skin of the Paradoxical Frog publication-title: Biochem. Biophys. Res. Commun. – volume: 50 start-page: 746 year: 2007 end-page: 756 ident: bib15 article-title: Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii publication-title: Toxicon – volume: 27 start-page: 3818 year: 2013 end-page: 3826 ident: bib33 article-title: Sensitization of gram-negative bacteria by targeting the membrane potential publication-title: Faseb J. – volume: 44 start-page: 7662 year: 2014 end-page: 7677 ident: bib133 article-title: Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis publication-title: Chemistry – volume: 13 start-page: 1795 year: 2021 ident: bib27 article-title: Nanotechnology-based delivery systems for antimicrobial peptides publication-title: Pharmaceutics – volume: 7 year: 2012 ident: bib73 article-title: The human milk protein-lipid complex HAMLET sensitizes bacterial pathogens to traditional antimicrobial agents publication-title: PLoS One – volume: 11 start-page: 2468 year: 2018 ident: bib134 article-title: Action of Antimicrobial Peptides against Bacterial Biofilms publication-title: Materials – volume: 72 start-page: 605 year: 2019 end-page: 616 ident: bib98 article-title: Synergistic combinations of anthelmintic salicylanilides oxyclozanide, rafoxanide, and closantel with colistin eradicates multidrug-resistant colistin-resistant Gram-negative bacilli publication-title: J. Antibiot. – volume: 4 start-page: 529 year: 2006 end-page: 536 ident: bib95 article-title: The co-evolution of host cationic antimicrobial peptides and microbial resistance publication-title: Nat. Rev. Microbiol. – volume: 44 start-page: D1094 year: 2015 end-page: D1097 ident: bib126 article-title: CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides publication-title: Nucleic Acids Res. – volume: 133 start-page: 117 year: 2017 end-page: 138 ident: bib2 article-title: Antimicrobial peptides (AMPs): ancient compounds that represent novel weapons in the fight against bacteria publication-title: Biochem Pharm. – volume: 19 start-page: 491 year: 2006 end-page: 511 ident: bib46 article-title: Peptide antimicrobial agents publication-title: Clin. Microbiol. Rev. – volume: 13 start-page: 1057 year: 2013 end-page: 1098 ident: bib57 article-title: Antibiotic resistance-the need for global solutions publication-title: Lancet Infect. Dis. – volume: 19 start-page: 210 year: 2019 ident: bib108 article-title: AcrAB-TolC efflux pump system plays a role in carbapenem non-susceptibility in Escherichia coli publication-title: BMC Microbiol. – volume: 53 start-page: 3472 year: 2009 end-page: 3477 ident: bib143 article-title: Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates publication-title: Antimicrob. Agents Chemother. – volume: 106 start-page: 9 year: 2018 end-page: 20 ident: bib81 article-title: Antibacterial, antifungal, anticancer activities and structural bioinformatics analysis of six naturally occurring temporins publication-title: Peptides – volume: 21 start-page: 224S year: 2001 end-page: 232S ident: bib117 article-title: Mechanism of action of and resistance to quinolones publication-title: Pharmacotherapy – volume: 4063–4072 year: 2016 ident: bib34 article-title: Antimicrobial peptide P60.4Ac-containing creams and gel for eradication of methicillin-resistant Staphylococcus aureus from cultured skin and airway epithelial surfaces publication-title: Antimicrob. Agents Chemother. – volume: 1548 start-page: 51 year: 2017 end-page: 59 ident: bib100 article-title: Microwave-Assisted Synthesis of Antimicrobial Peptides publication-title: Methods Mol. Biol. – volume: 48 start-page: 4673 year: 2004 end-page: 4679 ident: bib109 article-title: Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases publication-title: Antimicrob. Agents Chemother. – volume: 2 start-page: 445 year: 2011 end-page: 459 ident: bib5 article-title: Staphylococcus aureus biofilms publication-title: Virulence – volume: 52 year: 2020 ident: bib62 article-title: Nanomedicine to target multidrug resistant tumors publication-title: Drug Resist Updat – volume: 27 start-page: 921 year: 2018 end-page: 928 ident: bib123 article-title: Characterization of β-lactamase- and efflux pump-mediated multiple antibiotic resistance in Salmonella Typhimurium publication-title: Food Sci. Biotechnol. – volume: 5 year: 2019 ident: bib28 article-title: Biopolymeric pellets of polyvinyl alcohol and alginate for the encapsulation of Ib-M6 peptide and its antimicrobial activity against E.coli publication-title: Heliyon – volume: 31 start-page: 227 year: 2011 end-page: 232 ident: bib141 article-title: Activities of antimicrobial peptides and the reconstruction of the natural antimicrobial peptides publication-title: Chem. Life – volume: 8 start-page: 16463 year: 2018 ident: bib40 article-title: Interplay between MexAB-OprM and MexEF-OprN in clinical isolates of Pseudomonas aeruginosa publication-title: Sci. Rep. – volume: 45 start-page: 88 year: 2007 end-page: 94 ident: bib136 article-title: 16S ribosomal RNA methylation: emerging resistance mechanism against aminoglycosides publication-title: Clin. Infect. Dis. – volume: 143 start-page: 42 year: 2006 end-page: 49 ident: bib14 article-title: Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis publication-title: Comp. Biochem Physiol. C. Toxicol. Pharm. – volume: 3 year: 2021 ident: bib20 article-title: Drug delivery systems for the oral administration of antimicrobial peptides: promising tools to treat infectious diseases publication-title: Front Med Technol. – volume: 62 start-page: e01493 year: 2018 end-page: 18 ident: bib47 article-title: Pse-T2, an antimicrobial peptide with high-level, broad-spectrum antimicrobial potency and skin biocompatibility against multidrug-resistant pseudomonas aeruginosa infection publication-title: Antimicrob. Agents Chemother. – volume: 167 start-page: 67 year: 1997 end-page: 77 ident: bib86 article-title: Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action publication-title: Arch. Microbiol – volume: 85 start-page: 2149 year: 1963 end-page: 2154 ident: bib80 article-title: Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide publication-title: J. Am. Chem. Soc. – volume: 68 start-page: 3 year: 2015 end-page: 10 ident: bib18 article-title: Structural characterization of a novel peptide with antimicrobial activity from the venom gland of the scorpion Tityus stigmurus: Stigmurin publication-title: Peptides – volume: 22 start-page: 147 year: 2020 end-page: 151 ident: bib79 article-title: Ceftaroline versus vancomycin in the treatment of methicillin-resistant Staphylococcus aureus (MRSA) in an experimental MRSA meningitis model publication-title: J. Glob. Antimicrob. Resist. – volume: 1804 start-page: 1020 year: 2010 end-page: 1028 ident: bib114 article-title: Development of potent anti-infective agents from Silurana tropicalis: conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7 publication-title: Biochim Biophys. Acta – volume: 15 start-page: 40 year: 2010 end-page: 56 ident: bib125 article-title: Synthetic therapeutic peptides: science and market publication-title: Drug Discov. Today – volume: 63 start-page: 497 year: 2007 end-page: 506 ident: bib55 article-title: The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci publication-title: Mol. Microbiol – volume: 58 start-page: 349 year: 2001 end-page: 356 ident: bib51 article-title: Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris publication-title: J. Pept. Res – volume: 9 start-page: 2723 year: 2018 ident: bib72 article-title: Factors Contributing to the Evolution of mecA -Mediated β-lactam Resistance in Staphylococci: Update and New Insights From Whole Genome Sequencing (WGS) publication-title: Front. Microbiol. – volume: 81 start-page: 451 year: 2012 end-page: 478 ident: bib66 article-title: Structural perspective of peptidoglycan biosynthesis and assembly publication-title: Annu Rev. Biochem – volume: 153 start-page: 152 year: 2017 end-page: 159 ident: bib76 article-title: Lipid selectivity in novel antimicrobial peptides: Implication on antimicrobial and hemolytic activity publication-title: Colloids Surf. B Biointerfaces – volume: 149 start-page: 1367 year: 2003 end-page: 1375 ident: bib7 article-title: Arming the enemy: the evolution of resistance to self-proteins publication-title: Microbiol. (Read. ) – volume: 50 start-page: 7820 year: 2021 end-page: 7880 ident: bib30 article-title: The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions publication-title: Chem. Soc. Rev. – volume: 56 start-page: 6366 year: 2012 end-page: 6371 ident: bib75 article-title: In vitro activities of antibiotics and antimicrobial cationic peptides alone and in combination against methicillin-resistant Staphylococcus aureus biofilms publication-title: Antimicrob. Agents Chemother. – volume: 62 start-page: 32658 year: 2014 end-page: 32672 ident: bib91 article-title: Solid-phase peptide synthesis: an overview focused on the preparation of biologically relevant peptides publication-title: RSC Adv. 4 – volume: 37 start-page: 113 year: 2012 end-page: 119 ident: bib16 article-title: Host-defense peptides in skin secretions of the tetraploid frog Silurana epitropicalis with potent activity against methicillin-resistant Staphylococcus aureus (MRSA publication-title: Peptides – volume: 40 start-page: 414 year: 2021 end-page: 424 ident: bib36 article-title: Interactions of designed trp-containing antimicrobial peptides with DNA of multidrug-resistant pseudomonas aeruginosa publication-title: DNA Cell Biol. – volume: 9 start-page: 24 year: 2020 ident: bib10 article-title: Development and challenges of antimicrobial peptides for therapeutic applications publication-title: Antibiot. -Basel – volume: 276 start-page: 6483 year: 2009 end-page: 6496 ident: bib88 article-title: Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides publication-title: Febs J. – volume: 41 start-page: 1826 year: 2012 end-page: 1844 ident: bib93 article-title: Microwave heating in solid-phase peptide synthesis publication-title: Chem. Soc. Rev. – volume: 19 start-page: 1701 year: 2018 end-page: 1720 ident: bib115 article-title: Synthesis, Self-Assembly, and Biomedical Applications of Antimicrobial Peptide-Polymer Conjugates publication-title: Biomacromolecules – volume: 209 start-page: 597 year: 2010 end-page: 602 ident: bib53 article-title: Emergence of a new antibiotic resistance mechanism in India, Pakistan, and the UK: a molecular, biological, and epidemiological study publication-title: Br. Dent. J. – volume: 370 start-page: 20140086 year: 2015 ident: bib92 article-title: Time for a change: addressing R&D and commercialization challenges for antibacterials publication-title: Philos. Trans. R. Soc. B: Biol. Sci. – volume: 60 start-page: 1206 year: 2007 end-page: 1215 ident: bib140 article-title: Polymyxin B for the treatment of multidrug-resistant pathogens: a critical review publication-title: J. Antimicrob. Chemother. – volume: 31 start-page: 1225 year: 2010 end-page: 1230 ident: bib9 article-title: A fowlicidin-1 analog protects mice from lethal infections induced by methicillin-resistant Staphylococcus aureus publication-title: Peptides – volume: 42 start-page: 3320 year: 1998 end-page: 3324 ident: bib32 article-title: In vitro activities of membrane-active peptides against gram-positive and gram-negative aerobic bacteria publication-title: Antimicrob. Agents Chemother. – volume: 12 start-page: 2019 year: 2019 end-page: 2030 ident: bib116 article-title: Synergism of cationic antimicrobial peptide WLBU2 with antibacterial agents against biofilms of multi-drug resistant Acinetobacter baumannii and Klebsiella pneumoniae publication-title: Infect. Drug Resist. – volume: 10 start-page: eaan4044 year: 2018 ident: bib4 article-title: The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms publication-title: Sci. Transl. Med. – volume: 49 start-page: 479 year: 2005 end-page: 487 ident: bib49 article-title: Aminoglycoside resistance in Pseudomonas aeruginosa publication-title: Antimicrob. Agents Chemother. – volume: 218 start-page: 135 year: 2022 end-page: 156 ident: bib121 article-title: In pursuit of next-generation therapeutics: Antimicrobial peptides against superbugs, their sources, mechanism of action, nanotechnology-based delivery, and clinical applications publication-title: Int J. Biol. Macromol. – volume: 16 start-page: 523 year: 2018 end-page: 539 ident: bib23 article-title: Multidrug efflux pumps: structure, function and regulation publication-title: Nat. Rev. Microbiol. – volume: 1063 start-page: 159 year: 2013 end-page: 180 ident: bib97 article-title: On the role of NMR spectroscopy for characterization of antimicrobial peptides publication-title: Methods Mol. Biol. – volume: 217 start-page: 2059 year: 2018 end-page: 2071 ident: bib59 article-title: Romo1 is a mitochondrial nonselective cation channel with viroporin-like characteristics publication-title: J. Cell Biol. – volume: 24 start-page: 752 year: 2017 end-page: 757 ident: bib118 article-title: An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome publication-title: Nat. Struct. Mol. Biol. – volume: 1550 start-page: 81 year: 2001 end-page: 89 ident: bib3 article-title: Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae) publication-title: Biochim Biophys. Acta – volume: 63 start-page: e00338 year: 2019 end-page: 19 ident: bib45 article-title: Tridecaptin M, a new variant discovered in mud bacterium, shows activity against colistin- and extremely drug-resistant enterobacteriaceae publication-title: Antimicrob. Agents Chemother. – volume: 106 start-page: 19S year: 1999 end-page: 25S ident: bib44 article-title: Drug-resistant Streptococcus pneumoniae: rational antibiotic choices publication-title: Am. J. Med. – volume: 1268 start-page: 43 year: 2015 end-page: 66 ident: bib128 article-title: Improved methods for classification, prediction, and design of antimicrobial peptides publication-title: Methods Mol. Biol. – volume: 90 start-page: 53 year: 2000 end-page: 60 ident: bib50 article-title: Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio publication-title: Regul. Pept. – volume: 39 start-page: 402 year: 2012 end-page: 406 ident: bib78 article-title: Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300 publication-title: Int J. Antimicrob. Agents – volume: 67 start-page: 119 year: 2021 end-page: 137 ident: bib107 article-title: D-Amino acids in Antimicrobial Peptides: A Potential Approach to Treat and Combat Antimicrobial Resistance publication-title: Can. J. Microbiol – volume: 65 start-page: 382 year: 2018 end-page: 391 ident: bib65 article-title: Pretreatment with cathelicidin-BF ameliorates Pseudomonas aeruginosa pneumonia in mice by enhancing NETosis and the autophagy of recruited neutrophils and macrophages publication-title: Int. Immunopharmacol. – volume: 30 start-page: 557 year: 2017 end-page: 596 ident: bib96 article-title: Polymyxins: Antibacterial Activity, Susceptibility Testing, and Resistance Mechanisms Encoded by Plasmids or Chromosomes publication-title: Clin. Microbiol. Rev. – volume: 27 start-page: 189 year: 2007 end-page: 223 ident: bib99 article-title: Melittin: a Membrane-active Peptide with Diverse Functions publication-title: Biosci. Rep. – volume: 67 start-page: 593 year: 2003 end-page: 656 ident: bib39 article-title: Molecular basis of bacterial outer membrane permeability revisited publication-title: Microbiol. Mol. Biol. Rev.: MMBR – volume: 7 start-page: 40874 year: 2017 ident: bib17 article-title: Interspecies cathelicidin comparison reveals divergence in antimicrobial activity, TLR modulation, chemokine induction and regulation of phagocytosis publication-title: Sci. Rep. – volume: 40 start-page: 517 year: 2019 end-page: 528 ident: bib43 article-title: The vast structural diversity of antimicrobial peptides publication-title: Trends Pharmacol. Sci. – volume: 45 start-page: 195 year: 2016 end-page: 207 ident: bib83 article-title: The effect of amidation on the behaviour of antimicrobial peptides publication-title: Eur. Biophys. J. – volume: 169 start-page: 3883 year: 2002 end-page: 3891 ident: bib105 article-title: The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses publication-title: J. Immunol. – volume: 4 start-page: 1027 year: 2007 end-page: 1051 ident: bib61 article-title: The history of alamethicin: a review of the most extensively studied peptaibol publication-title: Chem. Biodivers. – volume: 8 start-page: 1205 year: 2017 ident: bib38 article-title: Bacteriocin-antimicrobial synergy: a medical and food perspective publication-title: Front. Microbiol. – volume: 21 start-page: 434 year: 2017 end-page: 438 ident: bib70 article-title: Antimicrobial peptides: The miraculous biological molecules publication-title: J. Indian Soc. Periodontol. – volume: 14 start-page: 599 year: 2018 end-page: 607 ident: bib11 article-title: Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering publication-title: Int J. Biol. Sci. – volume: 11 year: 2020 ident: bib64 article-title: High-Throughput Identification of Antibacterials Against Pseudomonas aeruginosa publication-title: Front. Microbiol. – volume: 65 start-page: 1043 year: 2016 end-page: 1054 ident: bib29 article-title: The challenges of multi-drug-resistance in hepatology publication-title: J. Hepatol. – volume: 29 start-page: 464 year: 2011 end-page: 472 ident: bib87 article-title: The expanding scope of antimicrobial peptide structures and their modes of action publication-title: Trends Biotechnol. – volume: 197 start-page: 1079 year: 2008 end-page: 1081 ident: bib101 article-title: Federal Funding for the Study of Antimicrobial Resistance in Nosocomial Pathogens: No ESKAPE publication-title: J. Infect. Dis. – volume: 1862 year: 2020 ident: bib102 article-title: Thrombocidin-1-derived antimicrobial peptide TC19 combats superficial multi-drug resistant bacterial wound infections publication-title: Biochim Biophys. Acta Biomembr. – start-page: 537 year: 2009 end-page: 559 ident: bib77 article-title: Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds publication-title: Nat. Prod. Rep. – volume: 131 start-page: 38 year: 2005 end-page: 45 ident: bib13 article-title: Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana) publication-title: Regul. Pept. – volume: 30 start-page: 505 year: 2005 end-page: 515 ident: bib135 article-title: A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs publication-title: Curr. eye Res. – volume: 8 start-page: 4032 year: 2018 ident: bib120 article-title: Cathelicidin promotes inflammation by enabling binding of self-RNA to cell surface scavenger receptors publication-title: Sci. Rep. – volume: 50 start-page: 7820 year: 2021 end-page: 7880 ident: bib8 article-title: The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions publication-title: Chem. Soc. Rev. – volume: 37 start-page: 544 year: 2011 end-page: 546 ident: bib22 article-title: Real-time PCR assay allows detection of the New Delhi metallo-β-lactamase (NDM-1)-encoding gene in France publication-title: Int. J. Antimicrob. Agents – volume: 10 start-page: 461 year: 2018 ident: bib132 article-title: Insect Antimicrobial Peptides, a Mini Review publication-title: Toxins – volume: 84 start-page: 5449 year: 1987 end-page: 5453 ident: bib139 article-title: Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor publication-title: Proc. Natl. Acad. Sci. USA – volume: 40 start-page: 978 year: 2020 end-page: 992 ident: bib69 article-title: Antimicrobial peptides as therapeutic agents: opportunities and challenges publication-title: Crit. Rev. Biotechnol. – volume: 273 start-page: 251 year: 2006 end-page: 256 ident: bib94 article-title: Experimental evolution of resistance to an antimicrobial peptide publication-title: Proc. Biol. Sci. – volume: 6 start-page: 29707 year: 2016 ident: bib82 article-title: Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus publication-title: Sci. Rep. – volume: 414 start-page: 268 year: 2001 end-page: 269 ident: bib110 article-title: Peptide antibiotics in mast cells of fish publication-title: Nature – volume: 103 start-page: 52 year: 2020 end-page: 67 ident: bib122 article-title: Topical antimicrobial peptide formulations for wound healing: Current developments and future prospects publication-title: Acta Biomater. – volume: 286 start-page: 43506 year: 2011 end-page: 43514 ident: bib54 article-title: Native thrombocidin-1 and unfolded thrombocidin-1 exert antimicrobial activity via distinct structural elements publication-title: J. Biol. Chem. – volume: 19 start-page: 110 year: 2022 end-page: 116 ident: bib25 article-title: WLBU2 antimicrobial peptide as a potential therapeutic for treatment of resistant bacterial publication-title: Turk. J. Pharm. Sci. – volume: 116 start-page: 26516 year: 2019 end-page: 26522 ident: bib85 article-title: The antimicrobial peptide ZY4 combats multidrug-resistant Pseudomonas aeruginosa and Acinetobacter baumannii infection publication-title: Proc. Natl. Acad. Sci. USA – volume: 1863 start-page: 849 year: 2019 end-page: 856 ident: bib138 article-title: A novel membrane-disruptive antimicrobial peptide from frog skin secretion against cystic fibrosis isolates and evaluation of anti-MRSA effect using Galleria mellonella model publication-title: Biochim Biophys. Acta Gen. Subj. – volume: 24 start-page: 2225 year: 2019 end-page: 2228 ident: bib35 article-title: Superbugs but no drugs: steps in averting a post-antibiotic era publication-title: Drug Disco Today – volume: 285 start-page: 16880 year: 2010 end-page: 16892 ident: bib1 article-title: Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide publication-title: J. Biol. Chem. – volume: 11 start-page: 133 year: 2020 end-page: 141 ident: bib52 article-title: CTX-M group distribution and positivity of extended-spectrum β-lactamase (ESBL)-Producing Enterobacteriaceae in Urinary Tract Infections in a Tertiary Metropolitan Hospital in Japan publication-title: J. St. Marian. Univ. – volume: 399 start-page: 629 year: 2022 end-page: 655 ident: bib84 article-title: Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis publication-title: Lancet – volume: 21 start-page: 449 year: 2008 end-page: 465 ident: bib56 article-title: Polymyxins Revisited publication-title: Clin. Microbiol. Rev. – volume: 65 start-page: e00130 year: 2021 end-page: 21 ident: bib113 article-title: Molecular Epidemiology of Third-Generation-Cephalosporin-Resistant Enterobacteriaceae in Southeast Queensland, Australia publication-title: Antimicrob. Agents Chemother. – volume: 44 start-page: D1087 year: 2015 end-page: D1093 ident: bib129 article-title: APD3: the antimicrobial peptide database as a tool for research and education publication-title: Nucleic Acids Res. – volume: 23 start-page: 414 year: 2018 ident: bib19 article-title: Antibacterial peptides in dermatology–strategies for evaluation of allergic potential publication-title: Molecules – volume: 232 year: 2022 ident: bib31 article-title: Antimicrobial peptides - Unleashing their therapeutic potential using nanotechnology publication-title: Pharm. Ther. – volume: 463 start-page: 58 year: 1999 end-page: 62 ident: bib111 article-title: SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes publication-title: Febs Lett. – volume: 25 start-page: 232 year: 2022 end-page: 238 ident: bib103 article-title: Ib-AMP4 antimicrobial peptide as a treatment for skin and systematic infection of methicillin-resistant Staphylococcus aureus (MRSA) publication-title: Iran. J. Basic Med. Sci. – volume: 46 start-page: 2465 year: 2009 end-page: 2473 ident: bib124 article-title: Identification of chicken cathelicidin-2 core elements involved in antibacterial and immunomodulatory activities publication-title: Mol. Immunol. – volume: 276 start-page: 5647 year: 2009 end-page: 5664 ident: bib71 article-title: Esculentin-1b(1-18)--a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli publication-title: Febs J. – volume: 9 year: 2021 ident: bib104 article-title: Antimicrobial Peptides and Proteins: From Nature's Reservoir to the Laboratory and Beyond publication-title: Front. Chem. – volume: 49 start-page: 2845 year: 2005 end-page: 2850 ident: bib12 article-title: Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37 publication-title: Antimicrob. Agents Chemother. – volume: 266 start-page: 759 year: 1962 end-page: 762 ident: bib131 article-title: Neurotoxic and Nephrotoxic Effects of Colistin in Patients with Renal Disease publication-title: N. Engl. J. Med. – volume: 1861 start-page: 1329 year: 2019 end-page: 1337 ident: bib74 article-title: Synergistic and antibiofilm activity of the antimicrobial peptide P5 against carbapenem-resistant Pseudomonas aeruginosa publication-title: Biochim. Et. Biophys. Acta (BBA) - Biomembr. – volume: 49 start-page: 6561 year: 2006 end-page: 6568 ident: bib26 article-title: Cyclic MrIA: a stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter publication-title: Am. Chem. Soc. – volume: 497 start-page: 943 year: 2018 end-page: 949 ident: bib142 article-title: Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues publication-title: Biochem Biophys. Res Commun. – volume: 7 start-page: 545 year: 2014 end-page: 594 ident: bib127 article-title: Human Antimicrobial Peptides and Proteins publication-title: Pharmaceuticals – volume: 110 start-page: 60 year: 2019 end-page: 68 ident: bib24 article-title: In vivo exposure of insect AMP resistant Staphylococcus aureus to an insect immune system publication-title: Insect Biochem Mol. Biol. – volume: 156 start-page: 197 year: 1997 end-page: 211 ident: bib6 article-title: Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin publication-title: J. Membr. Biol. – volume: 74 start-page: 663 year: 2017 end-page: 682 ident: bib106 article-title: Convergent evolution of defensin sequence, structure and function publication-title: Cell Mol. Life Sci. – volume: 11 start-page: 520 year: 2022 ident: bib41 article-title: Bacterial multidrug efflux pumps at the frontline of antimicrobial resistance: an overview publication-title: Antibiot. -Basel – volume: 1 start-page: 143 year: 2010 end-page: 152 ident: bib42 article-title: Alpha-helical cationic antimicrobial peptides: relationships of structure and function publication-title: Protein Cell – volume: 2 start-page: 1740 year: 2017 ident: bib21 article-title: Antimicrobial peptides: a potential therapeutic option for surgical site infections publication-title: Clin. Surg. – volume: 19 start-page: 320 year: 2010 end-page: 328 ident: bib130 article-title: Biofilm maturity studies indicate sharp debridement opens a time-dependent therapeutic window publication-title: J. Wound Care – volume: 24 start-page: 1551 year: 2006 end-page: 1557 ident: bib37 article-title: Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies publication-title: Nat. Biotechnol. – volume: 39 start-page: 978 year: 2016 end-page: 988 ident: bib63 article-title: The antimicrobial activity of Cbf-K16 against MRSA was enhanced by β-lactamantibiotics through cell wall non-integrity publication-title: Arch. Pharmacol. Res. – volume: 22 start-page: 11401 year: 2021 ident: bib67 article-title: Mechanism of Antimicrobial Peptides: Antimicrobial, Anti-Inflammatory and Antibiofilm Activities publication-title: Int. J. Mol. Sci. – volume: 92 start-page: 1236 year: 2010 end-page: 1241 ident: bib119 article-title: Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity publication-title: Biochimie – volume: 33 start-page: e00047 year: 2020 end-page: 19 ident: bib48 article-title: Epidemiology of β-lactamase-producing pathogens publication-title: Clin. Microbiol. Rev. – volume: 271 start-page: 28375 year: 1996 end-page: 28381 ident: bib112 article-title: Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities publication-title: J. Biol. Chem. – volume: 60 start-page: 1717 year: 2016 end-page: 1724 ident: bib137 article-title: Combination Effects of Antimicrobial Peptides publication-title: Antimicrob. Agents Chemother. – volume: 23 start-page: 414 issue: 2 year: 2018 ident: 10.1016/j.drup.2023.100954_bib19 article-title: Antibacterial peptides in dermatology–strategies for evaluation of allergic potential publication-title: Molecules doi: 10.3390/molecules23020414 – volume: 11 start-page: 520 issue: 4 year: 2022 ident: 10.1016/j.drup.2023.100954_bib41 article-title: Bacterial multidrug efflux pumps at the frontline of antimicrobial resistance: an overview publication-title: Antibiot. -Basel doi: 10.3390/antibiotics11040520 – volume: 49 start-page: 2845 issue: 7 year: 2005 ident: 10.1016/j.drup.2023.100954_bib12 article-title: Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37 publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.49.7.2845-2850.2005 – volume: 116 start-page: 26516 issue: 52 year: 2019 ident: 10.1016/j.drup.2023.100954_bib85 article-title: The antimicrobial peptide ZY4 combats multidrug-resistant Pseudomonas aeruginosa and Acinetobacter baumannii infection publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1909585117 – volume: 169 start-page: 3883 issue: 7 year: 2002 ident: 10.1016/j.drup.2023.100954_bib105 article-title: The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses publication-title: J. Immunol. doi: 10.4049/jimmunol.169.7.3883 – volume: 1063 start-page: 159 year: 2013 ident: 10.1016/j.drup.2023.100954_bib97 article-title: On the role of NMR spectroscopy for characterization of antimicrobial peptides publication-title: Methods Mol. Biol. doi: 10.1007/978-1-62703-583-5_9 – volume: 167 start-page: 67 issue: 2–3 year: 1997 ident: 10.1016/j.drup.2023.100954_bib86 article-title: Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action publication-title: Arch. Microbiol doi: 10.1007/s002030050418 – volume: 90 start-page: 53 issue: 1–3 year: 2000 ident: 10.1016/j.drup.2023.100954_bib50 article-title: Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio publication-title: Regul. Pept. doi: 10.1016/S0167-0115(00)00107-5 – volume: 218 start-page: 135 year: 2022 ident: 10.1016/j.drup.2023.100954_bib121 article-title: In pursuit of next-generation therapeutics: Antimicrobial peptides against superbugs, their sources, mechanism of action, nanotechnology-based delivery, and clinical applications publication-title: Int J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2022.07.103 – volume: 45 start-page: 195 issue: 3 year: 2016 ident: 10.1016/j.drup.2023.100954_bib83 article-title: The effect of amidation on the behaviour of antimicrobial peptides publication-title: Eur. Biophys. J. doi: 10.1007/s00249-015-1094-x – volume: 44 start-page: 7662 issue: 40 year: 2014 ident: 10.1016/j.drup.2023.100954_bib133 article-title: Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis publication-title: Chemistry – volume: 22 start-page: 147 year: 2020 ident: 10.1016/j.drup.2023.100954_bib79 article-title: Ceftaroline versus vancomycin in the treatment of methicillin-resistant Staphylococcus aureus (MRSA) in an experimental MRSA meningitis model publication-title: J. Glob. Antimicrob. Resist. doi: 10.1016/j.jgar.2020.02.001 – volume: 41 start-page: 1826 issue: 5 year: 2012 ident: 10.1016/j.drup.2023.100954_bib93 article-title: Microwave heating in solid-phase peptide synthesis publication-title: Chem. Soc. Rev. doi: 10.1039/C1CS15214A – volume: 9 start-page: 24 issue: 1 year: 2020 ident: 10.1016/j.drup.2023.100954_bib10 article-title: Development and challenges of antimicrobial peptides for therapeutic applications publication-title: Antibiot. -Basel doi: 10.3390/antibiotics9010024 – volume: 14 start-page: 599 issue: 6 year: 2018 ident: 10.1016/j.drup.2023.100954_bib11 article-title: Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering publication-title: Int J. Biol. Sci. doi: 10.7150/ijbs.23419 – start-page: 537 year: 2009 ident: 10.1016/j.drup.2023.100954_bib77 article-title: Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds publication-title: Nat. Prod. Rep. doi: 10.1039/b714132g – volume: 81 start-page: 451 year: 2012 ident: 10.1016/j.drup.2023.100954_bib66 article-title: Structural perspective of peptidoglycan biosynthesis and assembly publication-title: Annu Rev. Biochem doi: 10.1146/annurev-biochem-061809-112742 – volume: 497 start-page: 943 issue: 4 year: 2018 ident: 10.1016/j.drup.2023.100954_bib142 article-title: Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues publication-title: Biochem Biophys. Res Commun. doi: 10.1016/j.bbrc.2018.01.124 – volume: 19 start-page: 491 issue: 3 year: 2006 ident: 10.1016/j.drup.2023.100954_bib46 article-title: Peptide antimicrobial agents publication-title: Clin. Microbiol. Rev. doi: 10.1128/CMR.00056-05 – volume: 40 start-page: 978 issue: 7 year: 2020 ident: 10.1016/j.drup.2023.100954_bib69 article-title: Antimicrobial peptides as therapeutic agents: opportunities and challenges publication-title: Crit. Rev. Biotechnol. doi: 10.1080/07388551.2020.1796576 – volume: 156 start-page: 197 issue: 3 year: 1997 ident: 10.1016/j.drup.2023.100954_bib6 article-title: Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin publication-title: J. Membr. Biol. doi: 10.1007/s002329900201 – volume: 232 year: 2022 ident: 10.1016/j.drup.2023.100954_bib31 article-title: Antimicrobial peptides - Unleashing their therapeutic potential using nanotechnology publication-title: Pharm. Ther. doi: 10.1016/j.pharmthera.2021.107990 – volume: 63 start-page: e00338 issue: 6 year: 2019 ident: 10.1016/j.drup.2023.100954_bib45 article-title: Tridecaptin M, a new variant discovered in mud bacterium, shows activity against colistin- and extremely drug-resistant enterobacteriaceae publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.00338-19 – volume: 8 start-page: 16463 issue: 1 year: 2018 ident: 10.1016/j.drup.2023.100954_bib40 article-title: Interplay between MexAB-OprM and MexEF-OprN in clinical isolates of Pseudomonas aeruginosa publication-title: Sci. Rep. doi: 10.1038/s41598-018-34694-z – volume: 62 start-page: 32658 year: 2014 ident: 10.1016/j.drup.2023.100954_bib91 article-title: Solid-phase peptide synthesis: an overview focused on the preparation of biologically relevant peptides publication-title: RSC Adv. 4 doi: 10.1039/C4RA02458C – volume: 11 start-page: 2468 issue: 12 year: 2018 ident: 10.1016/j.drup.2023.100954_bib134 article-title: Action of Antimicrobial Peptides against Bacterial Biofilms publication-title: Materials doi: 10.3390/ma11122468 – volume: 27 start-page: 3818 issue: 9 year: 2013 ident: 10.1016/j.drup.2023.100954_bib33 article-title: Sensitization of gram-negative bacteria by targeting the membrane potential publication-title: Faseb J. doi: 10.1096/fj.13-227942 – volume: 197 start-page: 1079 issue: 8 year: 2008 ident: 10.1016/j.drup.2023.100954_bib101 article-title: Federal Funding for the Study of Antimicrobial Resistance in Nosocomial Pathogens: No ESKAPE publication-title: J. Infect. Dis. doi: 10.1086/533452 – volume: 24 start-page: 752 issue: 9 year: 2017 ident: 10.1016/j.drup.2023.100954_bib118 article-title: An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.3439 – volume: 149 start-page: 1367 issue: Pt 6 year: 2003 ident: 10.1016/j.drup.2023.100954_bib7 article-title: Arming the enemy: the evolution of resistance to self-proteins publication-title: Microbiol. (Read. ) doi: 10.1099/mic.0.26265-0 – volume: 74 start-page: 663 issue: 4 year: 2017 ident: 10.1016/j.drup.2023.100954_bib106 article-title: Convergent evolution of defensin sequence, structure and function publication-title: Cell Mol. Life Sci. doi: 10.1007/s00018-016-2344-5 – volume: 65 start-page: 2898 issue: 7 year: 1997 ident: 10.1016/j.drup.2023.100954_bib60 article-title: Effects of pH and salinity on the antimicrobial properties of clavanins publication-title: Infect. Immun. doi: 10.1128/iai.65.7.2898-2903.1997 – volume: 285 start-page: 16880 issue: 22 year: 2010 ident: 10.1016/j.drup.2023.100954_bib1 article-title: Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.097204 – volume: 53 start-page: 3472 issue: 8 year: 2009 ident: 10.1016/j.drup.2023.100954_bib143 article-title: Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01436-08 – volume: 19 start-page: 110 issue: 1 year: 2022 ident: 10.1016/j.drup.2023.100954_bib25 article-title: WLBU2 antimicrobial peptide as a potential therapeutic for treatment of resistant bacterial publication-title: Turk. J. Pharm. Sci. doi: 10.4274/tjps.galenos.2020.43078 – volume: 110 start-page: 60 year: 2019 ident: 10.1016/j.drup.2023.100954_bib24 article-title: In vivo exposure of insect AMP resistant Staphylococcus aureus to an insect immune system publication-title: Insect Biochem Mol. Biol. doi: 10.1016/j.ibmb.2019.04.017 – volume: 60 start-page: 1717 issue: 3 year: 2016 ident: 10.1016/j.drup.2023.100954_bib137 article-title: Combination Effects of Antimicrobial Peptides publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.02434-15 – volume: 86 start-page: 854 issue: 4 year: 2022 ident: 10.1016/j.drup.2023.100954_bib89 article-title: Topical antimicrobial peptide omiganan recovers cutaneous dysbiosis but does not improve clinical symptoms in patients with mild to moderate atopic dermatitis in a phase 2 randomized controlled trial publication-title: J. Am. Acad. Dermatol. doi: 10.1016/j.jaad.2020.08.132 – volume: 24 start-page: 2225 issue: 12 year: 2019 ident: 10.1016/j.drup.2023.100954_bib35 article-title: Superbugs but no drugs: steps in averting a post-antibiotic era publication-title: Drug Disco Today doi: 10.1016/j.drudis.2019.08.004 – volume: 5 issue: 6 year: 2019 ident: 10.1016/j.drup.2023.100954_bib28 article-title: Biopolymeric pellets of polyvinyl alcohol and alginate for the encapsulation of Ib-M6 peptide and its antimicrobial activity against E.coli publication-title: Heliyon – volume: 106 start-page: 9 year: 2018 ident: 10.1016/j.drup.2023.100954_bib81 article-title: Antibacterial, antifungal, anticancer activities and structural bioinformatics analysis of six naturally occurring temporins publication-title: Peptides doi: 10.1016/j.peptides.2018.05.011 – volume: 9 start-page: 2723 year: 2018 ident: 10.1016/j.drup.2023.100954_bib72 article-title: Factors Contributing to the Evolution of mecA -Mediated β-lactam Resistance in Staphylococci: Update and New Insights From Whole Genome Sequencing (WGS) publication-title: Front. Microbiol. doi: 10.3389/fmicb.2018.02723 – volume: 2 start-page: 1740 year: 2017 ident: 10.1016/j.drup.2023.100954_bib21 article-title: Antimicrobial peptides: a potential therapeutic option for surgical site infections publication-title: Clin. Surg. – volume: 33 start-page: e00047 issue: 2 year: 2020 ident: 10.1016/j.drup.2023.100954_bib48 article-title: Epidemiology of β-lactamase-producing pathogens publication-title: Clin. Microbiol. Rev. – volume: 288 start-page: 1001 issue: 4 year: 2001 ident: 10.1016/j.drup.2023.100954_bib90 article-title: Pseudin-2: An Antimicrobial Peptide with Low Hemolytic Activity from the Skin of the Paradoxical Frog publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.2001.5884 – volume: 15 start-page: 40 issue: 1 year: 2010 ident: 10.1016/j.drup.2023.100954_bib125 article-title: Synthetic therapeutic peptides: science and market publication-title: Drug Discov. Today doi: 10.1016/j.drudis.2009.10.009 – volume: 4063–4072 year: 2016 ident: 10.1016/j.drup.2023.100954_bib34 article-title: Antimicrobial peptide P60.4Ac-containing creams and gel for eradication of methicillin-resistant Staphylococcus aureus from cultured skin and airway epithelial surfaces publication-title: Antimicrob. Agents Chemother. – volume: 153 start-page: 152 year: 2017 ident: 10.1016/j.drup.2023.100954_bib76 article-title: Lipid selectivity in novel antimicrobial peptides: Implication on antimicrobial and hemolytic activity publication-title: Colloids Surf. B Biointerfaces doi: 10.1016/j.colsurfb.2017.02.003 – volume: 266 start-page: 759 issue: 15 year: 1962 ident: 10.1016/j.drup.2023.100954_bib131 article-title: Neurotoxic and Nephrotoxic Effects of Colistin in Patients with Renal Disease publication-title: N. Engl. J. Med. doi: 10.1056/NEJM196204122661505 – volume: 13 start-page: 1795 issue: 11 year: 2021 ident: 10.1016/j.drup.2023.100954_bib27 article-title: Nanotechnology-based delivery systems for antimicrobial peptides publication-title: Pharmaceutics doi: 10.3390/pharmaceutics13111795 – volume: 21 start-page: 224S issue: 10 Pt 2 year: 2001 ident: 10.1016/j.drup.2023.100954_bib117 article-title: Mechanism of action of and resistance to quinolones publication-title: Pharmacotherapy – volume: 40 start-page: 517 issue: 7 year: 2019 ident: 10.1016/j.drup.2023.100954_bib43 article-title: The vast structural diversity of antimicrobial peptides publication-title: Trends Pharmacol. Sci. doi: 10.1016/j.tips.2019.04.012 – volume: 1862 issue: 8 year: 2020 ident: 10.1016/j.drup.2023.100954_bib102 article-title: Thrombocidin-1-derived antimicrobial peptide TC19 combats superficial multi-drug resistant bacterial wound infections publication-title: Biochim Biophys. Acta Biomembr. doi: 10.1016/j.bbamem.2020.183282 – volume: 463 start-page: 58 issue: 1–2 year: 1999 ident: 10.1016/j.drup.2023.100954_bib111 article-title: SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes publication-title: Febs Lett. doi: 10.1016/S0014-5793(99)01600-2 – volume: 65 start-page: e00130 issue: 6 year: 2021 ident: 10.1016/j.drup.2023.100954_bib113 article-title: Molecular Epidemiology of Third-Generation-Cephalosporin-Resistant Enterobacteriaceae in Southeast Queensland, Australia publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.00130-21 – volume: 22 start-page: 11401 issue: 21 year: 2021 ident: 10.1016/j.drup.2023.100954_bib67 article-title: Mechanism of Antimicrobial Peptides: Antimicrobial, Anti-Inflammatory and Antibiofilm Activities publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms222111401 – volume: 399 start-page: 629 issue: 10325 year: 2022 ident: 10.1016/j.drup.2023.100954_bib84 article-title: Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis publication-title: Lancet doi: 10.1016/S0140-6736(21)02724-0 – volume: 8 start-page: 4032 issue: 1 year: 2018 ident: 10.1016/j.drup.2023.100954_bib120 article-title: Cathelicidin promotes inflammation by enabling binding of self-RNA to cell surface scavenger receptors publication-title: Sci. Rep. doi: 10.1038/s41598-018-22409-3 – volume: 19 start-page: 320 issue: 8 year: 2010 ident: 10.1016/j.drup.2023.100954_bib130 article-title: Biofilm maturity studies indicate sharp debridement opens a time-dependent therapeutic window publication-title: J. Wound Care doi: 10.12968/jowc.2010.19.8.77709 – volume: 50 start-page: 746 issue: 6 year: 2007 ident: 10.1016/j.drup.2023.100954_bib15 article-title: Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii publication-title: Toxicon doi: 10.1016/j.toxicon.2007.06.023 – volume: 24 start-page: 1551 issue: 12 year: 2006 ident: 10.1016/j.drup.2023.100954_bib37 article-title: Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies publication-title: Nat. Biotechnol. doi: 10.1038/nbt1267 – volume: 11 start-page: 133 issue: 2 year: 2020 ident: 10.1016/j.drup.2023.100954_bib52 article-title: CTX-M group distribution and positivity of extended-spectrum β-lactamase (ESBL)-Producing Enterobacteriaceae in Urinary Tract Infections in a Tertiary Metropolitan Hospital in Japan publication-title: J. St. Marian. Univ. doi: 10.17264/stmarieng.11.133 – volume: 92 start-page: 1236 issue: 9 year: 2010 ident: 10.1016/j.drup.2023.100954_bib119 article-title: Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity publication-title: Biochimie doi: 10.1016/j.biochi.2010.02.023 – volume: 60 start-page: 1206 issue: 6 year: 2007 ident: 10.1016/j.drup.2023.100954_bib140 article-title: Polymyxin B for the treatment of multidrug-resistant pathogens: a critical review publication-title: J. Antimicrob. Chemother. doi: 10.1093/jac/dkm357 – volume: 56 start-page: 6366 issue: 12 year: 2012 ident: 10.1016/j.drup.2023.100954_bib75 article-title: In vitro activities of antibiotics and antimicrobial cationic peptides alone and in combination against methicillin-resistant Staphylococcus aureus biofilms publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01180-12 – volume: 29 start-page: 464 issue: 9 year: 2011 ident: 10.1016/j.drup.2023.100954_bib87 article-title: The expanding scope of antimicrobial peptide structures and their modes of action publication-title: Trends Biotechnol. doi: 10.1016/j.tibtech.2011.05.001 – volume: 65 start-page: 1043 issue: 5 year: 2016 ident: 10.1016/j.drup.2023.100954_bib29 article-title: The challenges of multi-drug-resistance in hepatology publication-title: J. Hepatol. doi: 10.1016/j.jhep.2016.08.006 – volume: 13 start-page: 1057 issue: 12 year: 2013 ident: 10.1016/j.drup.2023.100954_bib57 article-title: Antibiotic resistance-the need for global solutions publication-title: Lancet Infect. Dis. doi: 10.1016/S1473-3099(13)70318-9 – volume: 106 start-page: 19S issue: 5A year: 1999 ident: 10.1016/j.drup.2023.100954_bib44 article-title: Drug-resistant Streptococcus pneumoniae: rational antibiotic choices publication-title: Am. J. Med. doi: 10.1016/S0002-9343(98)00351-9 – volume: 6 start-page: 29707 year: 2016 ident: 10.1016/j.drup.2023.100954_bib82 article-title: Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus publication-title: Sci. Rep. doi: 10.1038/srep29707 – volume: 40 start-page: 414 issue: 2 year: 2021 ident: 10.1016/j.drup.2023.100954_bib36 article-title: Interactions of designed trp-containing antimicrobial peptides with DNA of multidrug-resistant pseudomonas aeruginosa publication-title: DNA Cell Biol. doi: 10.1089/dna.2019.4874 – volume: 30 start-page: 505 issue: 7 year: 2005 ident: 10.1016/j.drup.2023.100954_bib135 article-title: A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs publication-title: Curr. eye Res. doi: 10.1080/02713680590968637 – volume: 49 start-page: 6561 year: 2006 ident: 10.1016/j.drup.2023.100954_bib26 article-title: Cyclic MrIA: a stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter publication-title: Am. Chem. Soc. – volume: 217 start-page: 2059 issue: 6 year: 2018 ident: 10.1016/j.drup.2023.100954_bib59 article-title: Romo1 is a mitochondrial nonselective cation channel with viroporin-like characteristics publication-title: J. Cell Biol. doi: 10.1083/jcb.201709001 – volume: 45 start-page: 88 issue: 1 year: 2007 ident: 10.1016/j.drup.2023.100954_bib136 article-title: 16S ribosomal RNA methylation: emerging resistance mechanism against aminoglycosides publication-title: Clin. Infect. Dis. doi: 10.1086/518605 – volume: 44 start-page: D1094 issue: D1 year: 2015 ident: 10.1016/j.drup.2023.100954_bib126 article-title: CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1051 – volume: 52 year: 2020 ident: 10.1016/j.drup.2023.100954_bib62 article-title: Nanomedicine to target multidrug resistant tumors publication-title: Drug Resist Updat doi: 10.1016/j.drup.2020.100704 – volume: 4 start-page: 529 issue: 7 year: 2006 ident: 10.1016/j.drup.2023.100954_bib95 article-title: The co-evolution of host cationic antimicrobial peptides and microbial resistance publication-title: Nat. Rev. Microbiol. doi: 10.1038/nrmicro1441 – volume: 30 start-page: 557 issue: 2 year: 2017 ident: 10.1016/j.drup.2023.100954_bib96 article-title: Polymyxins: Antibacterial Activity, Susceptibility Testing, and Resistance Mechanisms Encoded by Plasmids or Chromosomes publication-title: Clin. Microbiol. Rev. doi: 10.1128/CMR.00064-16 – volume: 2 start-page: 445 issue: 5 year: 2011 ident: 10.1016/j.drup.2023.100954_bib5 article-title: Staphylococcus aureus biofilms publication-title: Virulence doi: 10.4161/viru.2.5.17724 – volume: 103 start-page: 52 year: 2020 ident: 10.1016/j.drup.2023.100954_bib122 article-title: Topical antimicrobial peptide formulations for wound healing: Current developments and future prospects publication-title: Acta Biomater. doi: 10.1016/j.actbio.2019.12.025 – volume: 8 start-page: 1205 year: 2017 ident: 10.1016/j.drup.2023.100954_bib38 article-title: Bacteriocin-antimicrobial synergy: a medical and food perspective publication-title: Front. Microbiol. doi: 10.3389/fmicb.2017.01205 – volume: 62 start-page: e01493 issue: 12 year: 2018 ident: 10.1016/j.drup.2023.100954_bib47 article-title: Pse-T2, an antimicrobial peptide with high-level, broad-spectrum antimicrobial potency and skin biocompatibility against multidrug-resistant pseudomonas aeruginosa infection publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01493-18 – volume: 370 start-page: 20140086 issue: 1670 year: 2015 ident: 10.1016/j.drup.2023.100954_bib92 article-title: Time for a change: addressing R&D and commercialization challenges for antibacterials publication-title: Philos. Trans. R. Soc. B: Biol. Sci. doi: 10.1098/rstb.2014.0086 – volume: 48 start-page: 4673 issue: 12 year: 2004 ident: 10.1016/j.drup.2023.100954_bib109 article-title: Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.48.12.4673-4679.2004 – volume: 19 start-page: 1701 issue: 6 year: 2018 ident: 10.1016/j.drup.2023.100954_bib115 article-title: Synthesis, Self-Assembly, and Biomedical Applications of Antimicrobial Peptide-Polymer Conjugates publication-title: Biomacromolecules doi: 10.1021/acs.biomac.8b00208 – volume: 68 start-page: 3 year: 2015 ident: 10.1016/j.drup.2023.100954_bib18 article-title: Structural characterization of a novel peptide with antimicrobial activity from the venom gland of the scorpion Tityus stigmurus: Stigmurin publication-title: Peptides doi: 10.1016/j.peptides.2015.03.003 – volume: 19 start-page: 210 issue: 1 year: 2019 ident: 10.1016/j.drup.2023.100954_bib108 article-title: AcrAB-TolC efflux pump system plays a role in carbapenem non-susceptibility in Escherichia coli publication-title: BMC Microbiol. doi: 10.1186/s12866-019-1589-1 – volume: 414 start-page: 268 issue: 6861 year: 2001 ident: 10.1016/j.drup.2023.100954_bib110 article-title: Peptide antibiotics in mast cells of fish publication-title: Nature doi: 10.1038/35104690 – volume: 273 start-page: 251 issue: 1583 year: 2006 ident: 10.1016/j.drup.2023.100954_bib94 article-title: Experimental evolution of resistance to an antimicrobial peptide publication-title: Proc. Biol. Sci. – volume: 85 start-page: 2149 issue: 14 year: 1963 ident: 10.1016/j.drup.2023.100954_bib80 article-title: Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00897a025 – volume: 72 start-page: 605 issue: 8 year: 2019 ident: 10.1016/j.drup.2023.100954_bib98 article-title: Synergistic combinations of anthelmintic salicylanilides oxyclozanide, rafoxanide, and closantel with colistin eradicates multidrug-resistant colistin-resistant Gram-negative bacilli publication-title: J. Antibiot. doi: 10.1038/s41429-019-0186-8 – volume: 25 start-page: 232 issue: 2 year: 2022 ident: 10.1016/j.drup.2023.100954_bib103 article-title: Ib-AMP4 antimicrobial peptide as a treatment for skin and systematic infection of methicillin-resistant Staphylococcus aureus (MRSA) publication-title: Iran. J. Basic Med. Sci. – volume: 46 start-page: 2465 issue: 13 year: 2009 ident: 10.1016/j.drup.2023.100954_bib124 article-title: Identification of chicken cathelicidin-2 core elements involved in antibacterial and immunomodulatory activities publication-title: Mol. Immunol. doi: 10.1016/j.molimm.2009.05.019 – volume: 37 start-page: 113 issue: 1 year: 2012 ident: 10.1016/j.drup.2023.100954_bib16 article-title: Host-defense peptides in skin secretions of the tetraploid frog Silurana epitropicalis with potent activity against methicillin-resistant Staphylococcus aureus (MRSA publication-title: Peptides doi: 10.1016/j.peptides.2012.07.005 – volume: 276 start-page: 6483 issue: 22 year: 2009 ident: 10.1016/j.drup.2023.100954_bib88 article-title: Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides publication-title: Febs J. doi: 10.1111/j.1742-4658.2009.07359.x – volume: 143 start-page: 42 issue: 1 year: 2006 ident: 10.1016/j.drup.2023.100954_bib14 article-title: Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis publication-title: Comp. Biochem Physiol. C. Toxicol. Pharm. doi: 10.1016/j.cbpc.2005.11.022 – volume: 1 start-page: 143 issue: 2 year: 2010 ident: 10.1016/j.drup.2023.100954_bib42 article-title: Alpha-helical cationic antimicrobial peptides: relationships of structure and function publication-title: Protein Cell doi: 10.1007/s13238-010-0004-3 – volume: 63 start-page: 497 issue: 2 year: 2007 ident: 10.1016/j.drup.2023.100954_bib55 article-title: The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci publication-title: Mol. Microbiol doi: 10.1111/j.1365-2958.2006.05540.x – volume: 50 start-page: 7820 issue: 13 year: 2021 ident: 10.1016/j.drup.2023.100954_bib8 article-title: The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions publication-title: Chem. Soc. Rev. doi: 10.1039/D0CS00729C – volume: 21 start-page: 434 issue: 6 year: 2017 ident: 10.1016/j.drup.2023.100954_bib70 article-title: Antimicrobial peptides: The miraculous biological molecules publication-title: J. Indian Soc. Periodontol. doi: 10.4103/jisp.jisp_325_16 – volume: 271 start-page: 28375 issue: 45 year: 1996 ident: 10.1016/j.drup.2023.100954_bib112 article-title: Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.45.28375 – volume: 12 start-page: 2019 year: 2019 ident: 10.1016/j.drup.2023.100954_bib116 article-title: Synergism of cationic antimicrobial peptide WLBU2 with antibacterial agents against biofilms of multi-drug resistant Acinetobacter baumannii and Klebsiella pneumoniae publication-title: Infect. Drug Resist. doi: 10.2147/IDR.S215084 – volume: 31 start-page: 227 issue: 2 year: 2011 ident: 10.1016/j.drup.2023.100954_bib141 article-title: Activities of antimicrobial peptides and the reconstruction of the natural antimicrobial peptides publication-title: Chem. Life – volume: 1550 start-page: 81 issue: 1 year: 2001 ident: 10.1016/j.drup.2023.100954_bib3 article-title: Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae) publication-title: Biochim Biophys. Acta doi: 10.1016/S0167-4838(01)00272-2 – volume: 10 start-page: eaan4044 issue: 423 year: 2018 ident: 10.1016/j.drup.2023.100954_bib4 article-title: The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms publication-title: Sci. Transl. Med. doi: 10.1126/scitranslmed.aan4044 – volume: 42 start-page: 3320 issue: 12 year: 1998 ident: 10.1016/j.drup.2023.100954_bib32 article-title: In vitro activities of membrane-active peptides against gram-positive and gram-negative aerobic bacteria publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.42.12.3320 – volume: 276 start-page: 5647 issue: 19 year: 2009 ident: 10.1016/j.drup.2023.100954_bib71 article-title: Esculentin-1b(1-18)--a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli publication-title: Febs J. doi: 10.1111/j.1742-4658.2009.07257.x – volume: 7 issue: 8 year: 2012 ident: 10.1016/j.drup.2023.100954_bib73 article-title: The human milk protein-lipid complex HAMLET sensitizes bacterial pathogens to traditional antimicrobial agents publication-title: PLoS One doi: 10.1371/journal.pone.0043514 – volume: 7 start-page: 545 issue: 5 year: 2014 ident: 10.1016/j.drup.2023.100954_bib127 article-title: Human Antimicrobial Peptides and Proteins publication-title: Pharmaceuticals doi: 10.3390/ph7050545 – volume: 1548 start-page: 51 year: 2017 ident: 10.1016/j.drup.2023.100954_bib100 article-title: Microwave-Assisted Synthesis of Antimicrobial Peptides publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-6737-7_4 – volume: 9 year: 2021 ident: 10.1016/j.drup.2023.100954_bib104 article-title: Antimicrobial Peptides and Proteins: From Nature's Reservoir to the Laboratory and Beyond publication-title: Front. Chem. doi: 10.3389/fchem.2021.691532 – volume: 50 start-page: 7820 issue: 13 year: 2021 ident: 10.1016/j.drup.2023.100954_bib30 article-title: The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions publication-title: Chem. Soc. Rev. doi: 10.1039/D0CS00729C – volume: 16 start-page: 523 issue: 9 year: 2018 ident: 10.1016/j.drup.2023.100954_bib23 article-title: Multidrug efflux pumps: structure, function and regulation publication-title: Nat. Rev. Microbiol. doi: 10.1038/s41579-018-0048-6 – volume: 65 start-page: 382 year: 2018 ident: 10.1016/j.drup.2023.100954_bib65 article-title: Pretreatment with cathelicidin-BF ameliorates Pseudomonas aeruginosa pneumonia in mice by enhancing NETosis and the autophagy of recruited neutrophils and macrophages publication-title: Int. Immunopharmacol. doi: 10.1016/j.intimp.2018.10.030 – volume: 31 start-page: 1225 issue: 7 year: 2010 ident: 10.1016/j.drup.2023.100954_bib9 article-title: A fowlicidin-1 analog protects mice from lethal infections induced by methicillin-resistant Staphylococcus aureus publication-title: Peptides doi: 10.1016/j.peptides.2010.03.037 – volume: 27 start-page: 921 issue: 3 year: 2018 ident: 10.1016/j.drup.2023.100954_bib123 article-title: Characterization of β-lactamase- and efflux pump-mediated multiple antibiotic resistance in Salmonella Typhimurium publication-title: Food Sci. Biotechnol. doi: 10.1007/s10068-018-0317-1 – volume: 84 start-page: 5449 issue: 15 year: 1987 ident: 10.1016/j.drup.2023.100954_bib139 article-title: Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.84.15.5449 – volume: 39 start-page: 402 issue: 5 year: 2012 ident: 10.1016/j.drup.2023.100954_bib78 article-title: Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300 publication-title: Int J. Antimicrob. Agents doi: 10.1016/j.ijantimicag.2012.02.003 – volume: 44 start-page: D1087 issue: D1 year: 2015 ident: 10.1016/j.drup.2023.100954_bib129 article-title: APD3: the antimicrobial peptide database as a tool for research and education publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1278 – volume: 9 start-page: 34 issue: 1 year: 2001 ident: 10.1016/j.drup.2023.100954_bib68 article-title: Mechanisms of biofilm resistance to antimicrobial agents publication-title: Trends Microbiol. doi: 10.1016/S0966-842X(00)01913-2 – volume: 1863 start-page: 849 issue: 5 year: 2019 ident: 10.1016/j.drup.2023.100954_bib138 article-title: A novel membrane-disruptive antimicrobial peptide from frog skin secretion against cystic fibrosis isolates and evaluation of anti-MRSA effect using Galleria mellonella model publication-title: Biochim Biophys. Acta Gen. Subj. doi: 10.1016/j.bbagen.2019.02.013 – volume: 37 start-page: 544 issue: 6 year: 2011 ident: 10.1016/j.drup.2023.100954_bib22 article-title: Real-time PCR assay allows detection of the New Delhi metallo-β-lactamase (NDM-1)-encoding gene in France publication-title: Int. J. Antimicrob. Agents doi: 10.1016/j.ijantimicag.2011.02.006 – volume: 1268 start-page: 43 issue: 1268 year: 2015 ident: 10.1016/j.drup.2023.100954_bib128 article-title: Improved methods for classification, prediction, and design of antimicrobial peptides publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-2285-7_3 – volume: 21 start-page: 449 issue: 3 year: 2008 ident: 10.1016/j.drup.2023.100954_bib56 article-title: Polymyxins Revisited publication-title: Clin. Microbiol. Rev. doi: 10.1128/CMR.00006-08 – volume: 49 start-page: 479 issue: 2 year: 2005 ident: 10.1016/j.drup.2023.100954_bib49 article-title: Aminoglycoside resistance in Pseudomonas aeruginosa publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.49.2.479-487.2005 – volume: 11 year: 2020 ident: 10.1016/j.drup.2023.100954_bib64 article-title: High-Throughput Identification of Antibacterials Against Pseudomonas aeruginosa publication-title: Front. Microbiol. doi: 10.3389/fmicb.2020.591426 – volume: 27 start-page: 189 issue: 4–5 year: 2007 ident: 10.1016/j.drup.2023.100954_bib99 article-title: Melittin: a Membrane-active Peptide with Diverse Functions publication-title: Biosci. Rep. doi: 10.1007/s10540-006-9030-z – volume: 3 year: 2021 ident: 10.1016/j.drup.2023.100954_bib20 article-title: Drug delivery systems for the oral administration of antimicrobial peptides: promising tools to treat infectious diseases publication-title: Front Med Technol. – volume: 286 start-page: 43506 issue: 50 year: 2011 ident: 10.1016/j.drup.2023.100954_bib54 article-title: Native thrombocidin-1 and unfolded thrombocidin-1 exert antimicrobial activity via distinct structural elements publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.248641 – volume: 58 start-page: 349 issue: 5 year: 2001 ident: 10.1016/j.drup.2023.100954_bib51 article-title: Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris publication-title: J. Pept. Res doi: 10.1034/j.1399-3011.2001.00947.x – volume: 67 start-page: 593 issue: 4 year: 2003 ident: 10.1016/j.drup.2023.100954_bib39 article-title: Molecular basis of bacterial outer membrane permeability revisited publication-title: Microbiol. Mol. Biol. Rev.: MMBR doi: 10.1128/MMBR.67.4.593-656.2003 – volume: 133 start-page: 117 year: 2017 ident: 10.1016/j.drup.2023.100954_bib2 article-title: Antimicrobial peptides (AMPs): ancient compounds that represent novel weapons in the fight against bacteria publication-title: Biochem Pharm. doi: 10.1016/j.bcp.2016.09.018 – volume: 209 start-page: 597 issue: 7 year: 2010 ident: 10.1016/j.drup.2023.100954_bib53 article-title: Emergence of a new antibiotic resistance mechanism in India, Pakistan, and the UK: a molecular, biological, and epidemiological study publication-title: Br. Dent. J. – volume: 39 start-page: 978 issue: 7 year: 2016 ident: 10.1016/j.drup.2023.100954_bib63 article-title: The antimicrobial activity of Cbf-K16 against MRSA was enhanced by β-lactamantibiotics through cell wall non-integrity publication-title: Arch. Pharmacol. Res. doi: 10.1007/s12272-016-0769-x – volume: 4 start-page: 1027 issue: 6 year: 2007 ident: 10.1016/j.drup.2023.100954_bib61 article-title: The history of alamethicin: a review of the most extensively studied peptaibol publication-title: Chem. Biodivers. doi: 10.1002/cbdv.200790095 – volume: 131 start-page: 38 issue: 1–3 year: 2005 ident: 10.1016/j.drup.2023.100954_bib13 article-title: Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana) publication-title: Regul. Pept. doi: 10.1016/j.regpep.2005.06.003 – volume: 10 start-page: 461 issue: 11 year: 2018 ident: 10.1016/j.drup.2023.100954_bib132 article-title: Insect Antimicrobial Peptides, a Mini Review publication-title: Toxins doi: 10.3390/toxins10110461 – volume: 1804 start-page: 1020 issue: 4 year: 2010 ident: 10.1016/j.drup.2023.100954_bib114 article-title: Development of potent anti-infective agents from Silurana tropicalis: conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7 publication-title: Biochim Biophys. Acta doi: 10.1016/j.bbapap.2010.01.015 – volume: 67 start-page: 119 issue: 2 year: 2021 ident: 10.1016/j.drup.2023.100954_bib107 article-title: D-Amino acids in Antimicrobial Peptides: A Potential Approach to Treat and Combat Antimicrobial Resistance publication-title: Can. J. Microbiol doi: 10.1139/cjm-2020-0142 – year: 2020 ident: 10.1016/j.drup.2023.100954_bib58 article-title: Antimicrobial peptides: application informed by evolution publication-title: Sci. 368 (6490), eaau5480 – volume: 7 start-page: 40874 issue: 1 year: 2017 ident: 10.1016/j.drup.2023.100954_bib17 article-title: Interspecies cathelicidin comparison reveals divergence in antimicrobial activity, TLR modulation, chemokine induction and regulation of phagocytosis publication-title: Sci. Rep. doi: 10.1038/srep40874 – volume: 1861 start-page: 1329 issue: 7 year: 2019 ident: 10.1016/j.drup.2023.100954_bib74 article-title: Synergistic and antibiofilm activity of the antimicrobial peptide P5 against carbapenem-resistant Pseudomonas aeruginosa publication-title: Biochim. Et. Biophys. Acta (BBA) - Biomembr. doi: 10.1016/j.bbamem.2019.05.008 |
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| SubjectTerms | Anti-Bacterial Agents - pharmacology Anti-Bacterial Agents - therapeutic use Anti-Infective Agents - therapeutic use Antibiotics Antimicrobial Cationic Peptides - pharmacology Antimicrobial Cationic Peptides - therapeutic use Antimicrobial Peptides Bacteria - metabolism Bacterial infection Bacterial Infections - drug therapy Drug resistance Humans |
| Title | Antimicrobial peptides for combating drug-resistant bacterial infections |
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