Combined effect of lasioglossin LL-III derivative with azoles against Candida albicans virulence factors: biofilm formation, phospholipases, proteases and hemolytic activity

Candida albicans has several virulence factors at its disposal, including yeast-hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglo...

Full description

Saved in:
Bibliographic Details
Published inFEMS yeast research Vol. 20; no. 3; pp. 1 - 16
Main Authors Vankova, Eva, Kasparova, Petra, Dulickova, Nikola, Cerovsky, Vaclav
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.05.2020
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Candida albicans has several virulence factors at its disposal, including yeast-hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglossin LL-III to enhance effect of azoles on attenuation of C. albicans virulence factors. LL-III/43 was able to inhibit initial adhesion or biofilm formation of C. albicans strains at 50 µM. Azoles, however, were ineffective at this concentration. Using fluorescently labeled LL-III/43, we observed that peptide covered C. albicans cells, partially penetrated through their membranes and then accumulated inside cells. LL-III/43 (25 µM) in combination with clotrimazole prevented biofilm formation already at 3.1 µM clotrimazole. Neither LL-III/43 nor azoles were able to significantly inhibit phospholipases, proteases, or hemolytic activity of C. albicans. LL-III/43 (25 µM) and clotrimazole (50 µM) in combination decreased production of these virulence factors, and it completely attenuated its hemolytic activity. Scanning electron microscopy showed that LL-III/43 (50 µM) prevented C. albicans biofilm formation on Ti-6Al-4 V alloy used in orthopedic surgeries and combination of LL-III/43 (25 µM) with clotrimazole (3.1 µM) prevented biofilm formation on urinary catheters. Therefore, mixture of LL-III/43 and clotrimazole is suitable candidate for future pharmaceutical research.
AbstractList Candida albicans has several virulence factors at its disposal, including yeast--hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglossin LL-III to enhance effect of azoles on attenuation of C. albicans virulence factors. LL-III/43 was able to inhibit initial adhesion or biofilm formation of C. albicans strains at 50 [micro]M. Azoles, however, were ineffective at this concentration. Using fluorescently labeled LL-III/43, we observed that peptide covered C. albicans cells, partially penetrated through their membranes and then accumulated inside cells. LL-III/43 (25 [micro]M) in combination with clotrimazole prevented biofilm formation already at 3.1 [micro]M clotrimazole. Neither LL-III/43 nor azoles were able to significantly inhibit phospholipases, proteases, or hemolytic activity of C. albicans. LL-III/43 (25 [micro]M) and clotrimazole (50 [micro]M) in combination decreased production of these virulence factors, and it completely attenuated its hemolytic activity. Scanning electron microscopy showed that LL-III/43 (50 [micro]M) prevented C. albicans biofilm formation on Ti-6Al-4 V alloy used in orthopedic surgeries and combination of LL-III/43 (25 [micro]M) with clotrimazole (3.1 [micro]M) prevented biofilm formation on urinary catheters. Therefore, mixture of LL-III/43 and clotrimazole is suitable candidate for future pharmaceutical research.
Candida albicans has several virulence factors at its disposal, including yeast–hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglossin LL-III to enhance effect of azoles on attenuation of C. albicans virulence factors. LL-III/43 was able to inhibit initial adhesion or biofilm formation of C. albicans strains at 50 µM. Azoles, however, were ineffective at this concentration. Using fluorescently labeled LL-III/43, we observed that peptide covered C. albicans cells, partially penetrated through their membranes and then accumulated inside cells. LL-III/43 (25 µM) in combination with clotrimazole prevented biofilm formation already at 3.1 µM clotrimazole. Neither LL-III/43 nor azoles were able to significantly inhibit phospholipases, proteases, or hemolytic activity of C. albicans. LL-III/43 (25 µM) and clotrimazole (50 µM) in combination decreased production of these virulence factors, and it completely attenuated its hemolytic activity. Scanning electron microscopy showed that LL-III/43 (50 µM) prevented C. albicans biofilm formation on Ti-6Al-4 V alloy used in orthopedic surgeries and combination of LL-III/43 (25 µM) with clotrimazole (3.1 µM) prevented biofilm formation on urinary catheters. Therefore, mixture of LL-III/43 and clotrimazole is suitable candidate for future pharmaceutical research.
Candida albicans has several virulence factors at its disposal, including yeast-hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglossin LL-III to enhance effect of azoles on attenuation of C. albicans virulence factors. LL-III/43 was able to inhibit initial adhesion or biofilm formation of C. albicans strains at 50 µM. Azoles, however, were ineffective at this concentration. Using fluorescently labeled LL-III/43, we observed that peptide covered C. albicans cells, partially penetrated through their membranes and then accumulated inside cells. LL-III/43 (25 µM) in combination with clotrimazole prevented biofilm formation already at 3.1 µM clotrimazole. Neither LL-III/43 nor azoles were able to significantly inhibit phospholipases, proteases, or hemolytic activity of C. albicans. LL-III/43 (25 µM) and clotrimazole (50 µM) in combination decreased production of these virulence factors, and it completely attenuated its hemolytic activity. Scanning electron microscopy showed that LL-III/43 (50 µM) prevented C. albicans biofilm formation on Ti-6Al-4 V alloy used in orthopedic surgeries and combination of LL-III/43 (25 µM) with clotrimazole (3.1 µM) prevented biofilm formation on urinary catheters. Therefore, mixture of LL-III/43 and clotrimazole is suitable candidate for future pharmaceutical research.
Candida albicans has several virulence factors at its disposal, including yeast--hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglossin LL-III to enhance effect of azoles on attenuation of C. albicans virulence factors. LL-III/43 was able to inhibit initial adhesion or biofilm formation of C. albicans strains at 50 [micro]M. Azoles, however, were ineffective at this concentration. Using fluorescently labeled LL-III/43, we observed that peptide covered C. albicans cells, partially penetrated through their membranes and then accumulated inside cells. LL-III/43 (25 [micro]M) in combination with clotrimazole prevented biofilm formation already at 3.1 [micro]M clotrimazole. Neither LL-III/43 nor azoles were able to significantly inhibit phospholipases, proteases, or hemolytic activity of C. albicans. LL-III/43 (25 [micro]M) and clotrimazole (50 [micro]M) in combination decreased production of these virulence factors, and it completely attenuated its hemolytic activity. Scanning electron microscopy showed that LL-III/43 (50 [micro]M) prevented C. albicans biofilm formation on Ti-6Al-4 V alloy used in orthopedic surgeries and combination of LL-III/43 (25 [micro]M) with clotrimazole (3.1 [micro]M) prevented biofilm formation on urinary catheters. Therefore, mixture of LL-III/43 and clotrimazole is suitable candidate for future pharmaceutical research. Keywords: antimicrobial peptides; azoles; biofilm formation; Candida albicans; LL-III derivative; virulence factors
ABSTRACT Candida albicans has several virulence factors at its disposal, including yeast–hyphal transition associated with biofilm formation, phospholipases, proteases and hemolytic activity, all of which contribute to its pathogenesis. We used synthetic derivative LL-III/43 of antimicrobial peptide lasioglossin LL-III to enhance effect of azoles on attenuation of C. albicans virulence factors. LL-III/43 was able to inhibit initial adhesion or biofilm formation of C. albicans strains at 50 µM. Azoles, however, were ineffective at this concentration. Using fluorescently labeled LL-III/43, we observed that peptide covered C. albicans cells, partially penetrated through their membranes and then accumulated inside cells. LL-III/43 (25 µM) in combination with clotrimazole prevented biofilm formation already at 3.1 µM clotrimazole. Neither LL-III/43 nor azoles were able to significantly inhibit phospholipases, proteases, or hemolytic activity of C. albicans. LL-III/43 (25 µM) and clotrimazole (50 µM) in combination decreased production of these virulence factors, and it completely attenuated its hemolytic activity. Scanning electron microscopy showed that LL-III/43 (50 µM) prevented C. albicans biofilm formation on Ti-6Al-4 V alloy used in orthopedic surgeries and combination of LL-III/43 (25 µM) with clotrimazole (3.1 µM) prevented biofilm formation on urinary catheters. Therefore, mixture of LL-III/43 and clotrimazole is suitable candidate for future pharmaceutical research.
Audience Academic
Author Vaňková, Eva
Čeřovský, Václav
Kašparová, Petra
Dulíčková, Nikola
Author_xml – sequence: 1
  fullname: Vankova, Eva
– sequence: 2
  fullname: Kasparova, Petra
– sequence: 3
  fullname: Dulickova, Nikola
– sequence: 4
  fullname: Cerovsky, Vaclav
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32324227$$D View this record in MEDLINE/PubMed
BookMark eNptktuKFDEQhhtZcQ9666UEvFFwdnPqnm7vlsHDwIDg4TpUpyszWdLJmKRHx3fyHc2w42FlCSEV8tVPpeo_r0588FhVTxm9ZLQTVwbHtI9XJgBQTh9UZ6xu5jMmGnnyT3xanad0QymbU9o-qk4FF1xyPj-rfi7C2FuPA0FjUGcSDHGQbFi7kJL1ZLWaLZdLMmC0O8h2h-SbzRsCP4LDRGAN1qdMFuAHOwAB11sNPpGdjZNDr5EY0DnE9Jr0NhjrRmJCHItS8K_IdhNS2c5uIWEq9xgyHkJS9MgGx-D22WpSJOzO5v3j6qEBl_DJ8byovrx983nxfrb68G65uF7NtORtnkk9QCcH0UtOZVuLuWwaZGbgSOt-aFltgPYMOtO1tIby2vLGsLqFWjAcQIuL6sWtbino64Qpq9Emjc6BxzAlxUUnuWw60RT0-X_oTZiiL9Wp0uK6kZwx-Zdag0NlvQk5gj6Iqus5ZbXsaMcKdXkPVdaAo9Vl8KV_eDfh5Z2EwmT8ntcwpaSWnz7eK65jmWxEo7bRjhD3ilF18JK69ZI6eqkkPDv-bOpHHP7gv80jfgE83Mnp
CitedBy_id crossref_primary_10_1371_journal_pone_0272844
crossref_primary_10_1016_j_micpath_2024_106613
crossref_primary_10_3390_pharmaceutics15030789
crossref_primary_10_1155_2023_5645500
crossref_primary_10_3389_fbioe_2022_815393
crossref_primary_10_1007_s10989_022_10401_5
crossref_primary_10_1134_S0006350922020178
crossref_primary_10_1007_s11274_020_02891_6
crossref_primary_10_1080_21655979_2021_1933824
crossref_primary_10_3390_ijms23169264
crossref_primary_10_1007_s12223_021_00898_6
crossref_primary_10_3389_fcimb_2022_993029
crossref_primary_10_1007_s00726_023_03326_w
crossref_primary_10_3390_ph15050534
Cites_doi 10.1128/CMR.15.2.167-193.2002
10.1016/j.tibtech.2011.05.001
10.1146/annurev-micro-091014-104330
10.1002/cbic.200900133
10.1016/j.micres.2018.08.012
10.1128/AAC.49.7.2583-2588.2005
10.1111/j.1348-0421.1996.tb01147.x
10.1016/j.drup.2004.09.002
10.1099/jmm.0.001000
10.1016/S0378-1097(00)00071-9
10.3390/molecules201017913
10.1016/j.bbamem.2009.06.008
10.1002/psc.2827
10.1007/s10856-012-4645-z
10.1016/j.archoralbio.2006.12.008
10.1371/journal.pone.0132701
10.1016/S0960-894X(98)00084-5
10.1002/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M
10.1093/jac/dkn393
10.1023/A:1026572128004
10.5114/pdia.2013.38358
10.1128/CMR.00056-05
10.1016/j.bbamem.2014.11.024
10.1128/mBio.01991-17
10.1016/j.mycmed.2017.12.011
10.1016/j.ijantimicag.2009.11.021
10.1046/j.1439-0507.2001.00685.x
10.1111/1348-0421.12538
10.1128/JB.183.18.5385-5394.2001
10.1128/JCM.39.8.2971-2974.2001
10.3389/fmicb.2017.02218
10.1023/B:BILE.0000015472.09542.6d
10.1016/S0966-842X(00)01913-2
10.1021/acs.jnatprod.5b01129
10.1128/AAC.01777-18
10.1002/ctpp.201800044
10.1016/j.bbrc.2012.11.015
10.1080/21505594.2015.1039885
10.3389/fmicb.2016.01844
10.2478/s11535-010-0111-4
10.1016/j.peptides.2014.09.021
10.1016/j.tips.2019.04.012
10.1016/j.peptides.2015.07.023
10.1016/j.phymed.2014.11.019
10.1590/0037-8682-0032-2017
10.1016/j.archoralbio.2005.11.007
10.1016/j.peptides.2015.11.001
10.1093/jac/44.5.641
10.1093/femsyr/foz013
10.1111/cmi.13093
10.3389/fmicb.2016.01783
10.1128/AAC.02381-14
10.1016/j.cbpa.2017.03.014
10.1128/AAC.43.11.2635
10.1128/AAC.03065-15
10.1038/nature17625
10.1016/S0006-291X(03)00755-1
10.1016/j.pdpdt.2018.04.016
10.1007/978-3-319-50409-4_5
10.1039/C5RA14862F
10.1007/s00294-013-0400-3
10.1039/c3ra40887f
10.3389/fped.2019.00375
10.3389/fmicb.2017.02051
10.1002/pola.29078
10.1093/cid/cis697
10.1016/0378-1119(93)90668-S
10.1179/1973947812Y.0000000007
10.1007/s00253-009-1879-x
10.3109/13693780902801242
10.1016/j.jbiotec.2016.06.023
10.1007/s00726-010-0519-1
ContentType Journal Article
Copyright FEMS 2020.
COPYRIGHT 2020 Oxford University Press
Copyright_xml – notice: FEMS 2020.
– notice: COPYRIGHT 2020 Oxford University Press
DBID NPM
AAYXX
CITATION
ISR
3V.
7X7
7XB
88E
8FE
8FH
8FI
8FJ
8FK
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
FYUFA
GHDGH
GNUQQ
HCIFZ
K9.
LK8
M0S
M1P
M7P
PQEST
PQQKQ
PQUKI
PRINS
7X8
DOI 10.1093/femsyr/foaa020
DatabaseName PubMed
CrossRef
Gale In Context: Science
ProQuest Central (Corporate)
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest SciTech Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest Central
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Natural Science Collection
ProQuest One Community College
ProQuest Central Korea
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
SciTech Premium Collection (Proquest) (PQ_SDU_P3)
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
Health & Medical Collection (Alumni Edition)
Medical Database
Biological Science Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
MEDLINE - Academic
DatabaseTitle PubMed
CrossRef
ProQuest Central Student
ProQuest Central Essentials
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Central China
ProQuest Central
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
Natural Science Collection
ProQuest Central Korea
Biological Science Collection
ProQuest Medical Library (Alumni)
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
Biological Science Database
ProQuest SciTech Collection
ProQuest Hospital Collection (Alumni)
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
ProQuest One Academic
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList

ProQuest Central Student
PubMed

CrossRef
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1567-1364
ExternalDocumentID A701549091
10_1093_femsyr_foaa020
32324227
Genre Journal Article
GeographicLocations Czech Republic
GeographicLocations_xml – name: Czech Republic
GroupedDBID ---
.3N
.GA
0R~
10A
1OC
29H
36B
4.4
48X
50Y
50Z
51W
51X
52M
52N
52O
52P
52S
52T
52W
52X
53G
5GY
5HH
5LA
5VS
66C
702
7PT
7X7
8-0
8-1
8-3
8-4
8-5
88E
8FI
8FJ
8UM
930
A03
AAHBH
AAIMJ
AAMDB
AAMVS
AAOGV
AAPQZ
AAPXW
AARHZ
AAUQX
AAVAP
ABCQN
ABEML
ABEUO
ABIXL
ABJNI
ABPTD
ABQLI
ABUWG
ABXVV
ACGFO
ACGFS
ACPRK
ACSCC
ACUFI
ADBBV
ADEZT
ADGZP
ADHKW
ADHZD
ADQBN
ADRIX
ADRTK
ADVEK
ADYVW
AEGPL
AEJOX
AEKSI
AELWJ
AEMDU
AENEX
AENZO
AEPUE
AETBJ
AEWNT
AFFZL
AFGWE
AFIYH
AFKRA
AFOFC
AFXEN
AGINJ
AGSYK
AJEEA
AKWXX
ALIPV
ALMA_UNASSIGNED_HOLDINGS
ALUQC
APIBT
APWMN
ARIXL
AVWKF
AXUDD
AYOIW
AZBYB
BAFTC
BAYMD
BBNVY
BCRHZ
BENPR
BEYMZ
BHONS
BHPHI
BPHCQ
BQDIO
BSWAC
CCPQU
CDBKE
CS3
D-E
D-F
DAKXR
DCZOG
DILTD
DR2
DU5
EBS
EMB
F00
F01
F04
F5P
FDB
FHSFR
FLUFQ
FOEOM
FYUFA
G-S
G.N
GAUVT
GJXCC
H13
HAR
HCIFZ
HMCUK
HZI
HZ~
IAO
IHR
ISR
ITC
IX1
J21
K48
KBUDW
KOP
KSI
KSN
LC2
LC3
LP6
LP7
M1P
M7P
MK4
N04
N05
N9A
NLBLG
NOMLY
NPM
O9-
OAWHX
ODMLO
OIG
OJQWA
P2P
P2X
P4D
PAFKI
PEELM
PROAC
PSQYO
Q.N
Q11
Q5Y
QB0
R.K
ROL
ROX
RPM
RUSNO
RX1
RXO
TLC
TOX
UB1
UKHRP
V8K
W8V
W99
WQJ
XG1
YAYTL
YKOAZ
YXANX
~IA
~KM
~WT
AASNB
AAYXX
CITATION
OVD
ABEJV
AABJS
AABMN
AAESY
AAIYJ
ADEIU
ADORX
ADQLU
AIKOY
AZQFJ
BY8
BYORX
CASEJ
DPPUQ
OJZSN
TEORI
3V.
7XB
8FE
8FH
8FK
AZQEC
DWQXO
GNUQQ
K9.
LK8
PQEST
PQQKQ
PQUKI
PRINS
7X8
ID FETCH-LOGICAL-c428t-4cda94d3b42048537466e1fd2e05bd815fa0b1a9f9805a746826f158a531edac3
IEDL.DBID 7X7
ISSN 1567-1364
1567-1356
IngestDate Fri Oct 25 07:58:50 EDT 2024
Thu Oct 10 18:41:29 EDT 2024
Thu Feb 22 23:47:26 EST 2024
Tue Nov 12 23:22:21 EST 2024
Thu Aug 01 19:19:01 EDT 2024
Thu Sep 26 17:00:01 EDT 2024
Wed Oct 16 00:46:19 EDT 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 3
Keywords Candida albicans
biofilm formation
azoles
antimicrobial peptides
virulence factors
LL-III derivative
Language English
License FEMS 2020.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c428t-4cda94d3b42048537466e1fd2e05bd815fa0b1a9f9805a746826f158a531edac3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000-0001-8863-0696
0000-0003-4184-2848
0000-0003-2182-0430
OpenAccessLink https://academic.oup.com/femsyr/article-pdf/20/3/foaa020/38875885/foaa020.pdf
PMID 32324227
PQID 2425642114
PQPubID 2044077
PageCount 16
ParticipantIDs proquest_miscellaneous_2394246936
proquest_journals_2425642114
gale_infotracmisc_A701549091
gale_infotracacademiconefile_A701549091
gale_incontextgauss_ISR_A701549091
crossref_primary_10_1093_femsyr_foaa020
pubmed_primary_32324227
PublicationCentury 2000
PublicationDate 2020-May-01
2020-05-01
20200501
PublicationDateYYYYMMDD 2020-05-01
PublicationDate_xml – month: 05
  year: 2020
  text: 2020-May-01
  day: 01
PublicationDecade 2020
PublicationPlace England
PublicationPlace_xml – name: England
– name: Hoboken
PublicationTitle FEMS yeast research
PublicationTitleAlternate FEMS Yeast Res
PublicationYear 2020
Publisher Oxford University Press
Publisher_xml – name: Oxford University Press
References Galan-Ladero (2021070701263330000_bib17) 2010; 48
Vriens (2021070701263330000_bib71) 2015; 10
Mishra (2021070701263330000_bib43) 2017; 38
Jiang (2021070701263330000_bib24) 2012; 23
Viejo-Díaz (2021070701263330000_bib68) 2005; 49
Bandyopadhyay (2021070701263330000_bib1) 2013; 430
Ma (2021070701263330000_bib37) 2015; 20
Mah (2021070701263330000_bib38) 2001; 9
Nguyen (2021070701263330000_bib50) 2011; 29
Slaninová (2021070701263330000_bib59) 2015; 11
Orlandi (2021070701263330000_bib53) 2018; 22
Kodedová (2021070701263330000_bib28) 2019; 21
Vriens (2021070701263330000_bib72) 2016; 75
Koehbach (2021070701263330000_bib29) 2019; 40
Čeřovský (2021070701263330000_bib11) 2009; 10
Luo (2021070701263330000_bib36) 2001; 39
Nett (2021070701263330000_bib49) 2014; 12
Park (2021070701263330000_bib54) 2009; 1788
Marcos-Zambrano (2021070701263330000_bib39) 2016; 60
Löffler (2021070701263330000_bib35) 2000; 185
Giacometti (2021070701263330000_bib18) 1999; 44
Clinical, Institute LS (2021070701263330000_bib8) 2017
Donlan (2021070701263330000_bib12) 2002; 15
Moyes (2021070701263330000_bib46) 2016; 532
Uppuluri (2021070701263330000_bib65) 2017
Basu (2021070701263330000_bib2) 2015; 5
Kovács (2021070701263330000_bib30) 2019; 63
Mariscal (2021070701263330000_bib40) 2009; 82
Dosler (2021070701263330000_bib13) 2012; 24
Monincová (2021070701263330000_bib44) 2010; 39
Issam (2021070701263330000_bib22) 2015; 22
Chandra (2021070701263330000_bib21) 2001; 183
Lee (2021070701263330000_bib32) 2004; 26
Paula-Mattiello (2021070701263330000_bib55) 2017; 50
Niewerth (2021070701263330000_bib51) 2001; 44
Cirioni (2021070701263330000_bib6) 2008; 62
Guilhelmelli (2021070701263330000_bib19) 2016; 7
Cleveland (2021070701263330000_bib7) 2012; 55
Wakabayashi (2021070701263330000_bib73) 1996; 40
Cools (2021070701263330000_bib9) 2017; 8
Tan (2021070701263330000_bib62) 2018; 216
Troskie (2021070701263330000_bib64) 2014; 58
Mishra (2021070701263330000_bib42) 2013; 3
Scarsini (2021070701263330000_bib58) 2015; 71
Vráblíková (2021070701263330000_bib70) 2017; 61
Cui (2021070701263330000_bib10) 2015; 6
Lee (2021070701263330000_bib34) 2015; 1848
Jenssen (2021070701263330000_bib23) 2006; 19
Bondaryk (2021070701263330000_bib4) 2013; 30
Mukherjee (2021070701263330000_bib47) 2004; 7
Polaquini (2021070701263330000_bib56) 2006; 51
Slaninová (2021070701263330000_bib60) 2011; 6
Van't Hof (2021070701263330000_bib67) 2000; 78
Volejníková (2021070701263330000_bib69) 2019; 68
Zuza-Alves (2021070701263330000_bib77) 2016; 7
Mathé (2021070701263330000_bib41) 2013; 59
Romo (2021070701263330000_bib57) 2017; 8
Tossi (2021070701263330000_bib63) 2000; 55
Harris (2021070701263330000_bib20) 2010; 35
Vaňková (2021070701263330000_bib66) 2019; 59
Weber (2021070701263330000_bib74) 1998; 8
Kodedová (2021070701263330000_bib27) 2016; 233
Zaccaria (2021070701263330000_bib76) 2018; 56
Kuipers (2021070701263330000_bib31) 1999; 43
Mora-Navarro (2021070701263330000_bib45) 2015; 21
Bersani (2021070701263330000_bib3) 2019; 7
Yang (2021070701263330000_bib75) 2018; 28
Srikantha (2021070701263330000_bib61) 1993; 131
Dosler (2021070701263330000_bib14) 2014; 62
Kadir (2021070701263330000_bib25) 2007; 52
Nešuta (2021070701263330000_bib48) 2016; 79
Lee (2021070701263330000_bib33) 2003; 305
Fais (2021070701263330000_bib16) 2017; 8
Nobile (2021070701263330000_bib52) 2015; 69
Brogden (2021070701263330000_bib5) 2011; 38
Douglas (2021070701263330000_bib15) 2002; 19
Kočendová (2021070701263330000_bib26) 2019; 19
References_xml – volume: 15
  start-page: 167
  year: 2002
  ident: 2021070701263330000_bib12
  article-title: Biofilms: survival mechanisms of clinically relevant microorganisms
  publication-title: Clin Microbiol Rev
  doi: 10.1128/CMR.15.2.167-193.2002
  contributor:
    fullname: Donlan
– volume: 29
  start-page: 464
  year: 2011
  ident: 2021070701263330000_bib50
  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
  contributor:
    fullname: Nguyen
– volume: 69
  start-page: 71
  year: 2015
  ident: 2021070701263330000_bib52
  article-title: Candida albicans biofilms and human disease
  publication-title: Annu Rev Microbiol
  doi: 10.1146/annurev-micro-091014-104330
  contributor:
    fullname: Nobile
– volume: 10
  start-page: 2089
  year: 2009
  ident: 2021070701263330000_bib11
  article-title: Lasioglossins: three novel antimicrobial peptides from the venom of the eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)
  publication-title: ChemBioChem
  doi: 10.1002/cbic.200900133
  contributor:
    fullname: Čeřovský
– volume: 11
  start-page: 113
  year: 2015
  ident: 2021070701263330000_bib59
  article-title: Candida species and antimicrobial peptides from the venom of different wild bees
  publication-title: Collect Czech Chem C
  contributor:
    fullname: Slaninová
– volume: 216
  start-page: 120
  year: 2018
  ident: 2021070701263330000_bib62
  article-title: Antifungal activity of spider venom-derived peptide lycosin-I against Candida tropicalis
  publication-title: Microbiol Res
  doi: 10.1016/j.micres.2018.08.012
  contributor:
    fullname: Tan
– volume: 49
  start-page: 2583
  year: 2005
  ident: 2021070701263330000_bib68
  article-title: Different anti-Candida activities of two human lactoferrin-derived peptides, Lfpep and kaliocin-1
  publication-title: Antimicrob Agents Ch
  doi: 10.1128/AAC.49.7.2583-2588.2005
  contributor:
    fullname: Viejo-Díaz
– volume: 40
  start-page: 821
  year: 1996
  ident: 2021070701263330000_bib73
  article-title: Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents
  publication-title: Microbiol Immunol
  doi: 10.1111/j.1348-0421.1996.tb01147.x
  contributor:
    fullname: Wakabayashi
– volume: 7
  start-page: 301
  year: 2004
  ident: 2021070701263330000_bib47
  article-title: Candida biofilm resistance
  publication-title: Drug Resist Updat
  doi: 10.1016/j.drup.2004.09.002
  contributor:
    fullname: Mukherjee
– volume: 68
  start-page: 961
  year: 2019
  ident: 2021070701263330000_bib69
  article-title: Antimicrobial peptides prevent bacterial biofilm formation on the surface of polymethylmethacrylate bone cement
  publication-title: J Med Microbiol
  doi: 10.1099/jmm.0.001000
  contributor:
    fullname: Volejníková
– volume: 185
  start-page: 59
  year: 2000
  ident: 2021070701263330000_bib35
  article-title: Phospholipid and sterol analysis of plasma membranes of azole-resistant Candida albicans strains
  publication-title: FEMS Microbiol Lett
  doi: 10.1016/S0378-1097(00)00071-9
  contributor:
    fullname: Löffler
– volume: 20
  start-page: 17913
  year: 2015
  ident: 2021070701263330000_bib37
  article-title: Potent activities of roemerine against Candida albicans and the underlying mechanisms
  publication-title: Molecules
  doi: 10.3390/molecules201017913
  contributor:
    fullname: Ma
– volume: 1788
  start-page: 1790
  year: 2009
  ident: 2021070701263330000_bib54
  article-title: Fungicidal effect of antimicrobial peptide arenicin-1
  publication-title: BBA-Rev Biomembranes
  doi: 10.1016/j.bbamem.2009.06.008
  contributor:
    fullname: Park
– volume: 21
  start-page: 853
  year: 2015
  ident: 2021070701263330000_bib45
  article-title: Synthetic antimicrobial β-peptide in dual-treatment with fluconazole or ketoconazole enhances the in vitro inhibition of planktonic and biofilm Candida albicans
  publication-title: J Pept Sci
  doi: 10.1002/psc.2827
  contributor:
    fullname: Mora-Navarro
– volume: 23
  start-page: 1723
  year: 2012
  ident: 2021070701263330000_bib24
  article-title: Antimicrobial activities of recombinant mouse β-defensin 3 and its synergy with antibiotics
  publication-title: J Mater Sci-Mater M
  doi: 10.1007/s10856-012-4645-z
  contributor:
    fullname: Jiang
– volume: 52
  start-page: 691
  year: 2007
  ident: 2021070701263330000_bib25
  article-title: Phospholipase activity of Candida albicans isolates from patients with denture stomatitis: the influence of chlorhexidine gluconate on phospholipase production
  publication-title: Arch Oral Biol
  doi: 10.1016/j.archoralbio.2006.12.008
  contributor:
    fullname: Kadir
– volume: 10
  start-page: 1
  year: 2015
  ident: 2021070701263330000_bib71
  article-title: Synergistic activity of the plant defensin HsAFP1 and caspofungin against Candida albicans biofilms and planktonic cultures
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0132701
  contributor:
    fullname: Vriens
– volume: 8
  start-page: 597
  year: 1998
  ident: 2021070701263330000_bib74
  article-title: A fast and inexpensive method for N-terminal fluorescein-labeling of peptides
  publication-title: Bioorg Med Chem Lett
  doi: 10.1016/S0960-894X(98)00084-5
  contributor:
    fullname: Weber
– volume: 12
  start-page: 375
  year: 2014
  ident: 2021070701263330000_bib49
  article-title: Future directions for anti-biofilm therapeutics targeting Candida. Expert Rev
  publication-title: Anti-Infe
  contributor:
    fullname: Nett
– volume: 55
  start-page: 4
  year: 2000
  ident: 2021070701263330000_bib63
  article-title: Amphipathic, α-helical antimicrobial peptides
  publication-title: Pept Sci
  doi: 10.1002/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M
  contributor:
    fullname: Tossi
– volume: 62
  start-page: 1332
  year: 2008
  ident: 2021070701263330000_bib6
  article-title: Protective effects of the combination of α-helical antimicrobial peptides and rifampicin in three rat models of Pseudomonas aeruginosa infection
  publication-title: J Antimicrobiol Chemoth
  doi: 10.1093/jac/dkn393
  contributor:
    fullname: Cirioni
– volume: 78
  start-page: 163
  year: 2000
  ident: 2021070701263330000_bib67
  article-title: Synergistic effects of low doses of histatin 5 and its analogues on amphotericin B anti-mycotic activity
  publication-title: Antonie Van Leeuwenhoek
  doi: 10.1023/A:1026572128004
  contributor:
    fullname: Van't Hof
– volume: 30
  start-page: 293
  year: 2013
  ident: 2021070701263330000_bib4
  article-title: Antifungal agents commonly used in the superficial and mucosal candidiasis treatment: mode of action and resistance development
  publication-title: Adv Dermatol Allergol
  doi: 10.5114/pdia.2013.38358
  contributor:
    fullname: Bondaryk
– volume: 19
  start-page: 491
  year: 2006
  ident: 2021070701263330000_bib23
  article-title: Peptide antimicrobial agents
  publication-title: Clin Microbiol Rev
  doi: 10.1128/CMR.00056-05
  contributor:
    fullname: Jenssen
– volume: 1848
  start-page: 673
  year: 2015
  ident: 2021070701263330000_bib34
  article-title: Fungicidal mechanisms of the antimicrobial peptide Bac8c
  publication-title: BBA-Rev Biomembranes
  doi: 10.1016/j.bbamem.2014.11.024
  contributor:
    fullname: Lee
– volume: 8
  start-page: 1
  year: 2017
  ident: 2021070701263330000_bib57
  article-title: Development of anti-virulence approaches for candidiasis via a novel series of small-molecule inhibitors of Candida albicans filamentation
  publication-title: mBio
  doi: 10.1128/mBio.01991-17
  contributor:
    fullname: Romo
– volume: 28
  start-page: 36
  year: 2018
  ident: 2021070701263330000_bib75
  article-title: Dracorhodin perchlorate inhibits biofilm formation and virulence factors of Candida albicans
  publication-title: J Mycol Med
  doi: 10.1016/j.mycmed.2017.12.011
  contributor:
    fullname: Yang
– volume: 35
  start-page: 347
  year: 2010
  ident: 2021070701263330000_bib20
  article-title: Combination of caspofungin or anidulafungin with antimicrobial peptides results in potent synergistic killing of Candida albicans and Candida glabrata in vitro
  publication-title: Int J Antimicrob Ag
  doi: 10.1016/j.ijantimicag.2009.11.021
  contributor:
    fullname: Harris
– volume: 44
  start-page: 361
  year: 2001
  ident: 2021070701263330000_bib51
  article-title: Phospholipases of Candida albicans
  publication-title: Mycoses
  doi: 10.1046/j.1439-0507.2001.00685.x
  contributor:
    fullname: Niewerth
– volume: 61
  start-page: 474
  year: 2017
  ident: 2021070701263330000_bib70
  article-title: Lasioglossins LLIII affect the morphogenesis of Candida albicans and reduces the duration of experimental vaginal candidiasis in mice
  publication-title: Microbiol Immunol
  doi: 10.1111/1348-0421.12538
  contributor:
    fullname: Vráblíková
– volume: 183
  start-page: 5385
  year: 2001
  ident: 2021070701263330000_bib21
  article-title: Biofilm formation by the fungal pathogen Candida albicans: development, architecture, and drug resistance
  publication-title: J Bacteriol
  doi: 10.1128/JB.183.18.5385-5394.2001
  contributor:
    fullname: Chandra
– volume: 39
  start-page: 2971
  year: 2001
  ident: 2021070701263330000_bib36
  article-title: Candida species exhibit differential in vitro hemolytic activities
  publication-title: J Clin Microbiol
  doi: 10.1128/JCM.39.8.2971-2974.2001
  contributor:
    fullname: Luo
– volume: 8
  start-page: 1
  year: 2017
  ident: 2021070701263330000_bib16
  article-title: The N-terminus of human lactoferrin displays anti-biofilm activity on Candida parapsilosis in lumen catheters
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2017.02218
  contributor:
    fullname: Fais
– volume: 26
  start-page: 337
  year: 2004
  ident: 2021070701263330000_bib32
  article-title: Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides
  publication-title: Biotechnol Lett
  doi: 10.1023/B:BILE.0000015472.09542.6d
  contributor:
    fullname: Lee
– volume: 9
  start-page: 34
  year: 2001
  ident: 2021070701263330000_bib38
  article-title: Mechanisms of biofilm resistance to antimicrobial agents
  publication-title: Trends Microbiol
  doi: 10.1016/S0966-842X(00)01913-2
  contributor:
    fullname: Mah
– volume: 79
  start-page: 1073
  year: 2016
  ident: 2021070701263330000_bib48
  article-title: Antimicrobial peptide from the wild Bee Hylaeus signatus venom and its analogues: structure–activity study and synergistic effect with antibiotics
  publication-title: J Nat Prod
  doi: 10.1021/acs.jnatprod.5b01129
  contributor:
    fullname: Nešuta
– volume: 63
  start-page: e01777
  year: 2019
  ident: 2021070701263330000_bib30
  article-title: In vivo applicability of Neosartorya fischeri antifungal protein 2 (NFAP2) in treatment of vulvovaginal candidiasis
  publication-title: Antimicrob Agents Ch
  doi: 10.1128/AAC.01777-18
  contributor:
    fullname: Kovács
– volume: 59
  start-page: 166
  year: 2019
  ident: 2021070701263330000_bib66
  article-title: Prevention of biofilm re-development on Ti-6Al-4 V alloy by cometary discharge with a metallic grid
  publication-title: Contrib Plasm Phys
  doi: 10.1002/ctpp.201800044
  contributor:
    fullname: Vaňková
– volume: 430
  start-page: 1
  year: 2013
  ident: 2021070701263330000_bib1
  article-title: Model membrane interaction and DNA-binding of antimicrobial peptide Lasioglossin II derived from bee venom
  publication-title: Biochem Bioph Res Co
  doi: 10.1016/j.bbrc.2012.11.015
  contributor:
    fullname: Bandyopadhyay
– volume: 6
  start-page: 362
  year: 2015
  ident: 2021070701263330000_bib10
  article-title: Synergistic combinations of antifungals and anti-virulence agents to fight against Candida albicans
  publication-title: Virulence
  doi: 10.1080/21505594.2015.1039885
  contributor:
    fullname: Cui
– volume: 7
  start-page: 1
  year: 2016
  ident: 2021070701263330000_bib19
  article-title: Activity of scorpion venom-derived antifungal peptides against planktonic cells of Candida spp. and Cryptococcus neoformans and Candida albicans biofilms
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2016.01844
  contributor:
    fullname: Guilhelmelli
– volume: 6
  start-page: 150
  year: 2011
  ident: 2021070701263330000_bib60
  article-title: The antifungal effect of peptides from hymenoptera venom and their analogs
  publication-title: Open Life Sci
  doi: 10.2478/s11535-010-0111-4
  contributor:
    fullname: Slaninová
– volume: 62
  start-page: 32
  year: 2014
  ident: 2021070701263330000_bib14
  article-title: Inhibition and destruction of Pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides
  publication-title: Peptides
  doi: 10.1016/j.peptides.2014.09.021
  contributor:
    fullname: Dosler
– volume: 40
  start-page: 517
  year: 2019
  ident: 2021070701263330000_bib29
  article-title: The vast structural diversity of antimicrobial peptides
  publication-title: Trends Pharmacol Sci
  doi: 10.1016/j.tips.2019.04.012
  contributor:
    fullname: Koehbach
– volume: 71
  start-page: 211
  year: 2015
  ident: 2021070701263330000_bib58
  article-title: Antifungal activity of cathelicidin peptides against planktonic and biofilm cultures of Candida species isolated from vaginal infections
  publication-title: Peptides
  doi: 10.1016/j.peptides.2015.07.023
  contributor:
    fullname: Scarsini
– volume: 22
  start-page: 245
  year: 2015
  ident: 2021070701263330000_bib22
  article-title: Pharmacological synergism of bee venom and melittin with antibiotics and plant secondary metabolites against multi-drug resistant microbial pathogens
  publication-title: Phytomedicine
  doi: 10.1016/j.phymed.2014.11.019
  contributor:
    fullname: Issam
– volume-title: Performance Standards for Antifungal Susceptibility Testing of Yeasts
  year: 2017
  ident: 2021070701263330000_bib8
  contributor:
    fullname: Clinical, Institute LS
– volume: 50
  start-page: 558
  year: 2017
  ident: 2021070701263330000_bib55
  article-title: In vitro evaluation of hydrolytic enzyme activity and biofilm formation of Candida parapsilosis species complex from a nosocomial environment
  publication-title: Rev Soc Bras Med Tro
  doi: 10.1590/0037-8682-0032-2017
  contributor:
    fullname: Paula-Mattiello
– volume: 51
  start-page: 482
  year: 2006
  ident: 2021070701263330000_bib56
  article-title: Effect of aqueous extract from Neem (Azadirachta indica A. Juss) on hydrophobicity, biofilm formation and adhesion in composite resin by Candida albicans. Arch
  publication-title: Oral Biol
  doi: 10.1016/j.archoralbio.2005.11.007
  contributor:
    fullname: Polaquini
– volume: 75
  start-page: 71
  year: 2016
  ident: 2021070701263330000_bib72
  article-title: The radish defensins RsAFP1 and RsAFP2 act synergistically with caspofungin against Candida albicans biofilms
  publication-title: Peptides
  doi: 10.1016/j.peptides.2015.11.001
  contributor:
    fullname: Vriens
– volume: 44
  start-page: 641
  year: 1999
  ident: 2021070701263330000_bib18
  article-title: In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa
  publication-title: J Antimicrobiol Chemoth
  doi: 10.1093/jac/44.5.641
  contributor:
    fullname: Giacometti
– volume: 19
  start-page: 1
  year: 2019
  ident: 2021070701263330000_bib26
  article-title: Antifungal activity of analogues of antimicrobial peptides isolated from bee venoms against vulvovaginal Candida spp
  publication-title: FEMS Yeast Res
  doi: 10.1093/femsyr/foz013
  contributor:
    fullname: Kočendová
– volume: 21
  start-page: 1
  year: 2019
  ident: 2021070701263330000_bib28
  article-title: Variations in yeast plasma-membrane lipid composition affect killing activity of three families of insect antifungal peptides
  publication-title: Cell Microbiol
  doi: 10.1111/cmi.13093
  contributor:
    fullname: Kodedová
– volume: 7
  start-page: 1
  year: 2016
  ident: 2021070701263330000_bib77
  article-title: Evaluation of virulence factors in vitro, resistance to osmotic stress and antifungal susceptibility of Candida tropicalis isolated from the coastal environment of Northeast Brazil
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2016.01783
  contributor:
    fullname: Zuza-Alves
– volume: 58
  start-page: 3697
  year: 2014
  ident: 2021070701263330000_bib64
  article-title: Synergistic activity of the tyrocidines, antimicrobial cyclodecapeptides from Bacillus aneurinolyticus, with amphotericin B and caspofungin against Candida albicans biofilms
  publication-title: Antimicrob Agents Ch
  doi: 10.1128/AAC.02381-14
  contributor:
    fullname: Troskie
– volume: 38
  start-page: 87
  year: 2017
  ident: 2021070701263330000_bib43
  article-title: Host defense antimicrobial peptides as antibiotics: design and application strategies
  publication-title: Curr Opin Chem Biol
  doi: 10.1016/j.cbpa.2017.03.014
  contributor:
    fullname: Mishra
– volume: 43
  start-page: 2635
  year: 1999
  ident: 2021070701263330000_bib31
  article-title: Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against clinical Candida isolates
  publication-title: Antimicrob Agents Ch
  doi: 10.1128/AAC.43.11.2635
  contributor:
    fullname: Kuipers
– volume: 60
  start-page: 3579
  year: 2016
  ident: 2021070701263330000_bib39
  article-title: Biofilm production and antibiofilm activity of echinocandins and liposomal amphotericin B in echinocandin-resistant yeast species
  publication-title: Antimicrob Agents Ch
  doi: 10.1128/AAC.03065-15
  contributor:
    fullname: Marcos-Zambrano
– volume: 532
  start-page: 64
  year: 2016
  ident: 2021070701263330000_bib46
  article-title: Candidalysin is a fungal peptide toxin critical for mucosal infection
  publication-title: Nature
  doi: 10.1038/nature17625
  contributor:
    fullname: Moyes
– volume: 305
  start-page: 305
  year: 2003
  ident: 2021070701263330000_bib33
  article-title: Fungicidal effect of indolicidin and its interaction with phospholipid membranes
  publication-title: Biochem Bioph Res Co
  doi: 10.1016/S0006-291X(03)00755-1
  contributor:
    fullname: Lee
– volume: 38
  start-page: 217
  year: 2011
  ident: 2021070701263330000_bib5
  article-title: Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?
  publication-title: Int J Antimicrob Ag
  contributor:
    fullname: Brogden
– volume: 19
  start-page: 139
  year: 2002
  ident: 2021070701263330000_bib15
  article-title: Medical importance of biofilms in Candida infections
  publication-title: Rev Iberoam Micol
  contributor:
    fullname: Douglas
– volume: 22
  start-page: 233
  year: 2018
  ident: 2021070701263330000_bib53
  article-title: Catalase A is involved in the response to photooxidative stress in Pseudomonas aeruginosa. Photodiagn
  publication-title: Photodyn
  doi: 10.1016/j.pdpdt.2018.04.016
  contributor:
    fullname: Orlandi
– start-page: 63
  volume-title: Candida albicans: Cellular and Molecular Biology
  year: 2017
  ident: 2021070701263330000_bib65
  article-title: Candida albicans Biofilms
  doi: 10.1007/978-3-319-50409-4_5
  contributor:
    fullname: Uppuluri
– volume: 5
  start-page: 78712
  year: 2015
  ident: 2021070701263330000_bib2
  article-title: Global transcriptome analysis reveals distinct bacterial response towards soluble and surface-immobilized antimicrobial peptide (Lasioglossin-III)
  publication-title: RSC Adv
  doi: 10.1039/C5RA14862F
  contributor:
    fullname: Basu
– volume: 59
  start-page: 251
  year: 2013
  ident: 2021070701263330000_bib41
  article-title: Recent insights into Candida albicans biofilm resistance mechanisms
  publication-title: Curr Genet
  doi: 10.1007/s00294-013-0400-3
  contributor:
    fullname: Mathé
– volume: 3
  start-page: 9534
  year: 2013
  ident: 2021070701263330000_bib42
  article-title: Lasioglossin-III: antimicrobial characterization and feasibility study for immobilization applications
  publication-title: RSC Adv
  doi: 10.1039/c3ra40887f
  contributor:
    fullname: Mishra
– volume: 7
  start-page: 375
  year: 2019
  ident: 2021070701263330000_bib3
  article-title: Antifungal drugs for invasive Candida infections (ICI) in neonates: future perspectives
  publication-title: Front Pediatr
  doi: 10.3389/fped.2019.00375
  contributor:
    fullname: Bersani
– volume: 8
  start-page: 1
  year: 2017
  ident: 2021070701263330000_bib9
  article-title: A linear 19-mer plant defensin-derived peptide acts synergistically with caspofungin against Candida albicans biofilms
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2017.02051
  contributor:
    fullname: Cools
– volume: 56
  start-page: 1926
  year: 2018
  ident: 2021070701263330000_bib76
  article-title: Antimicrobial peptide modification of biomaterials using supramolecular additives
  publication-title: J Polym Sci A1
  doi: 10.1002/pola.29078
  contributor:
    fullname: Zaccaria
– volume: 55
  start-page: 1352
  year: 2012
  ident: 2021070701263330000_bib7
  article-title: Changes in incidence and antifungal drug resistance in candidemia: results from population-based laboratory surveillance in Atlanta and Baltimore, 2008–2011
  publication-title: Clin Infect Dis
  doi: 10.1093/cid/cis697
  contributor:
    fullname: Cleveland
– volume: 131
  start-page: 53
  year: 1993
  ident: 2021070701263330000_bib61
  article-title: A white-specific gene in the white-opaque switching system of Candida albicans
  publication-title: Gene
  doi: 10.1016/0378-1119(93)90668-S
  contributor:
    fullname: Srikantha
– volume: 24
  start-page: 137
  year: 2012
  ident: 2021070701263330000_bib13
  article-title: In vitro activities of antimicrobial cationic peptides; melittin and nisin, alone or in combination with antibiotics against Gram-positive bacteria
  publication-title: J Chemotherapy
  doi: 10.1179/1973947812Y.0000000007
  contributor:
    fullname: Dosler
– volume: 82
  start-page: 773
  year: 2009
  ident: 2021070701263330000_bib40
  article-title: Fluorescent assay based on resazurin for detection of activity of disinfectants against bacterial biofilm
  publication-title: Appl Microbiol Biotechnol
  doi: 10.1007/s00253-009-1879-x
  contributor:
    fullname: Mariscal
– volume: 48
  start-page: 207
  year: 2010
  ident: 2021070701263330000_bib17
  article-title: Enzymatic activities of Candida tropicalis isolated from hospitalized patients
  publication-title: Med Mycol
  doi: 10.3109/13693780902801242
  contributor:
    fullname: Galan-Ladero
– volume: 233
  start-page: 26
  year: 2016
  ident: 2021070701263330000_bib27
  article-title: High-throughput fluorescence screening assay for the identification and comparison of antimicrobial peptides’ activity on various yeast species
  publication-title: J Biotechnol
  doi: 10.1016/j.jbiotec.2016.06.023
  contributor:
    fullname: Kodedová
– volume: 39
  start-page: 763
  year: 2010
  ident: 2021070701263330000_bib44
  article-title: Novel antimicrobial peptides from the venom of the eusocial bee Halictus sexcinctus (Hymenoptera: Halictidae) and their analogs
  publication-title: Amino Acids
  doi: 10.1007/s00726-010-0519-1
  contributor:
    fullname: Monincová
SSID ssj0017008
Score 2.3883286
Snippet Candida albicans has several virulence factors at its disposal, including yeast-hyphal transition associated with biofilm formation, phospholipases, proteases...
ABSTRACT Candida albicans has several virulence factors at its disposal, including yeast–hyphal transition associated with biofilm formation, phospholipases,...
Candida albicans has several virulence factors at its disposal, including yeast--hyphal transition associated with biofilm formation, phospholipases, proteases...
Candida albicans has several virulence factors at its disposal, including yeast–hyphal transition associated with biofilm formation, phospholipases, proteases...
SourceID proquest
gale
crossref
pubmed
SourceType Aggregation Database
Index Database
StartPage 1
SubjectTerms Antimicrobial agents
Antimicrobial peptides
Azoles
Biofilms
Bone surgery
Candida albicans
Catheters
Clotrimazole
Mushrooms
Peptides
Phospholipases
Proteases
Scanning electron microscopy
Surgery
Virulence factors
Title Combined effect of lasioglossin LL-III derivative with azoles against Candida albicans virulence factors: biofilm formation, phospholipases, proteases and hemolytic activity
URI https://www.ncbi.nlm.nih.gov/pubmed/32324227
https://www.proquest.com/docview/2425642114
https://search.proquest.com/docview/2394246936
Volume 20
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3db9MwELdgExIviO8VxnQgJF6ImsR2PnhBY2xa0ZhQYVLfIjuxu0htUpp2Uvmf-B-5c9JA98BDpKR23ER3Pt85d78fY2_jlICqQutZkXBPaJRFaqTvGWEjFQcmjxx929fL6PxKfJnISbfh1nRplVub6Ax1Uee0Rz4k15iKMgPxcfHTI9Yo-rraUWjcZftB6EeU0hVP-oCLoOdcKZxEYxBwGfWgjXxozbzZLIe2Vsonru9_FqXbpvmWw-kWnrOH7EHnMcJxK-JH7I6pHrN7LYfk5gn7jTMao1tTQJuaAbUFKo2spzP8q7KCiwtvNBpBgap241C-gfZeQf0iKCdQU1WihwgnVN5SKFAzTYaxgZtyuXYFSdBR8nwAXRK_9xz6gsf3sLiuGzxm5QJXwwavCfaBTgHHg2szr2cbfG6g8gliqXjKrs5Of5ycex0Hg5djYLLyRF6oVBRcC0L4lTwWUWQCW4TGl7pIAmmVrwOV2jTxpcJWDFdsIBOFc9sUKufP2F5VV-aAgdRpmkvUGGu18LVQ2hc5LqH4c6K5Hw7Yu60QskULtZG1n8h51oor68Q1YG9IRhnhV1SUIDNV66bJRt_H2XHsQOfQC8Lhuk62Xi1Vrrp6A3wYgrza6Xm40xMnWL7bvFWFrJvgTfZXHQfsdd9Md1LSWmXqNfbhqQhFlPJowJ63KtS_GHeebBi_-P_gL9n9kAJ8l2F5yPZWy7V5hV7QSh85VT9i-59OL7-N8erzOPwDg_0MBg
link.rule.ids 315,783,787,12068,21400,27936,27937,31731,31732,33756,33757,43322,43817
linkProvider ProQuest
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lj9MwELZgEYIL4rkUFjAIiQtRk9jOgwtarVg10N0D7Eq9WXZidyu1SWnalcp_4j8y47iB7oFDpTR2nEQzHs84M99HyPs0R6Cq2AaWZyzgGmSRGxEGhttEpZEpE0ffdnaejC7514mY-A231qdV7myiM9RVU-Ie-RBdYyzKjPjn5c8AWaPw66qn0LhN7iAOFzIYpJM-4ELoOVcKJ8AYREwkPWgjG1qzaLeroW2UCpHr-59F6aZpvuFwuoXn9CF54D1GetyJ-BG5ZerH5G7HIbl9Qn7DjIbo1lS0S82gjaVYGtlM53CrWU3H46AoClqBql07lG-Ke69U_UIoJ6qmagYeIj3B8pZKUTXXaBhbej1bbVxBEvWUPJ-oniG_94L2BY8f6fKqaeE3ny1hNWzhP8I-4CGF8eiVWTTzLTw3xfIJZKl4Si5Pv1ycjALPwRCUEJisA15WKucV0xwRfgVLeZKYyFaxCYWuskhYFepI5TbPQqGgFcIVG4lMwdw2lSrZM3JQN7V5TqjQeV4K0BhrNQ81VzrkJSyhcDrTLIwH5MNOCHLZQW3I7hM5k524pBfXgLxDGUnEr6gxQWaqNm0rix_f5XHqQOfAC4LhfCfbrFeqVL7eAB4GIa_2eh7t9YQJVu4371RB-gneyr_qOCBv-2a8EpPWatNsoA_LecyTnCUDctipUP9izHmycfri_4O_IfdGF2djOS7Ov70k92MM9l225RE5WK825hV4RGv92qn9H3jqDGo
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Combined+effect+of+lasioglossin+LL-III+derivative+with+azoles+against+Candida+albicans+virulence+factors%3A+biofilm+formation%2C+phospholipases%2C+proteases+and+hemolytic+activity&rft.jtitle=FEMS+yeast+research&rft.au=Va%C5%88kov%C3%A1%2C+Eva&rft.au=Ka%C5%A1parov%C3%A1%2C+Petra&rft.au=Dul%C3%AD%C4%8Dkov%C3%A1%2C+Nikola&rft.au=%C4%8Ce%C5%99ovsk%C3%BD%2C+V%C3%A1clav&rft.date=2020-05-01&rft.issn=1567-1364&rft.eissn=1567-1364&rft.volume=20&rft.issue=3&rft_id=info:doi/10.1093%2Ffemsyr%2Ffoaa020&rft.externalDBID=n%2Fa&rft.externalDocID=10_1093_femsyr_foaa020
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1567-1364&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1567-1364&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1567-1364&client=summon