Methyl β-D-galactopyranoside esters as potential inhibitors for SARS-CoV-2 protease enzyme: synthesis, antimicrobial, PASS, molecular docking, molecular dynamics simulations and quantum computations
Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6- O -acyl MGP esters by direct acylation method with an exce...
Saved in:
| Published in | Glycoconjugate journal Vol. 39; no. 2; pp. 261 - 290 |
|---|---|
| Main Authors | , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
New York
Springer US
01.04.2022
Springer Nature B.V |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0282-0080 1573-4986 1573-4986 |
| DOI | 10.1007/s10719-021-10039-3 |
Cover
Loading…
| Abstract | Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6-
O
-acyl MGP esters by direct acylation method with an excellent yield. To obtain newer products for antimicrobial assessment studies, the 6-
O
-MGP esters were further modified into 2,3,4-tri-
O
-acyl MGP esters containing a wide variety of functionalities in a single molecular framework. The chemical structures of the newly synthesized compounds were elucidated by analyzing their physicochemical, elemental, and spectroscopic data. In vitro antimicrobial testing against five bacteria and two fungi and the prediction of activity spectra for substances (PASS) revealed that these MGP estes have promising antifungal functionality compared to their antibacterial activities. The antimicrobial tests demonstrated that the compounds 3 and 10 were the most potent against
Bacillus subtilis
and
Escherichia coli
strains, with the minimum inhibitory concentration (MIC) values ranging from 0.352 ± 0.02 to 0.703 ± 0.01 mg/ml and minimum bactericidal concentration (MBC) values ranging from 0.704 ± 0.02 to 1.408 ± 0.04 mg/ml. Density functional theory (DFT) at the B3LYP/3-21G level of theory was employed to enumerate, frontier orbital energy, enthalpy, free energy, electronic energy, MEP, dipole moment which evaluated the effect of certain groups (aliphatic and aromatic) on drug properties. They discovered that all esters were more thermodynamically stable than the parent molecule. Molecular docking is performed using AutoDock Vina to determine the binding affinities and interactions between the MGP esters and the SARS-CoV-2 main protease. The modified esters strongly interact with the prime Cys145, His41, MET165, GLY143, THR26, and ASN142 residues. The MGP esters’ shape and ability to form multiple electrostatic and hydrogen bonds with the active site match other minor-groove binders’ binding modes. The molecular dynamics simulation validates the molecular docking results. The pharmacokinetic characterization of the optimized inhibitor demonstrates that these MGP esters appear to be safer inhibitors and a combination of in silico ADMET (absorption, distribution, metabolism, excretion, and toxicity) prediction and drug-likeness had promising results due to their improved kinetic properties. Structure activity relationships (SAR) study including in vitro and
silico
results revealed that the acyl chain, palmitoyl (C16) and 4-chlorobenzoyl (4.ClC
6
H
4
CO-) in combination with sugar were found the most potential activates against human and fungal pathogens. After all, our comprehensive computational and statistical analysis shows that these selected MGP esters can be used as potential inhibitors against the SARS-CoV-2. |
|---|---|
| AbstractList | Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6-O-acyl MGP esters by direct acylation method with an excellent yield. To obtain newer products for antimicrobial assessment studies, the 6-O-MGP esters were further modified into 2,3,4-tri-O-acyl MGP esters containing a wide variety of functionalities in a single molecular framework. The chemical structures of the newly synthesized compounds were elucidated by analyzing their physicochemical, elemental, and spectroscopic data. In vitro antimicrobial testing against five bacteria and two fungi and the prediction of activity spectra for substances (PASS) revealed that these MGP estes have promising antifungal functionality compared to their antibacterial activities. The antimicrobial tests demonstrated that the compounds 3 and 10 were the most potent against Bacillus subtilis and Escherichia coli strains, with the minimum inhibitory concentration (MIC) values ranging from 0.352 ± 0.02 to 0.703 ± 0.01 mg/ml and minimum bactericidal concentration (MBC) values ranging from 0.704 ± 0.02 to 1.408 ± 0.04 mg/ml. Density functional theory (DFT) at the B3LYP/3-21G level of theory was employed to enumerate, frontier orbital energy, enthalpy, free energy, electronic energy, MEP, dipole moment which evaluated the effect of certain groups (aliphatic and aromatic) on drug properties. They discovered that all esters were more thermodynamically stable than the parent molecule. Molecular docking is performed using AutoDock Vina to determine the binding affinities and interactions between the MGP esters and the SARS-CoV-2 main protease. The modified esters strongly interact with the prime Cys145, His41, MET165, GLY143, THR26, and ASN142 residues. The MGP esters' shape and ability to form multiple electrostatic and hydrogen bonds with the active site match other minor-groove binders' binding modes. The molecular dynamics simulation validates the molecular docking results. The pharmacokinetic characterization of the optimized inhibitor demonstrates that these MGP esters appear to be safer inhibitors and a combination of in silico ADMET (absorption, distribution, metabolism, excretion, and toxicity) prediction and drug-likeness had promising results due to their improved kinetic properties. Structure activity relationships (SAR) study including in vitro and silico results revealed that the acyl chain, palmitoyl (C16) and 4-chlorobenzoyl (4.ClC6H4CO-) in combination with sugar were found the most potential activates against human and fungal pathogens. After all, our comprehensive computational and statistical analysis shows that these selected MGP esters can be used as potential inhibitors against the SARS-CoV-2.Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6-O-acyl MGP esters by direct acylation method with an excellent yield. To obtain newer products for antimicrobial assessment studies, the 6-O-MGP esters were further modified into 2,3,4-tri-O-acyl MGP esters containing a wide variety of functionalities in a single molecular framework. The chemical structures of the newly synthesized compounds were elucidated by analyzing their physicochemical, elemental, and spectroscopic data. In vitro antimicrobial testing against five bacteria and two fungi and the prediction of activity spectra for substances (PASS) revealed that these MGP estes have promising antifungal functionality compared to their antibacterial activities. The antimicrobial tests demonstrated that the compounds 3 and 10 were the most potent against Bacillus subtilis and Escherichia coli strains, with the minimum inhibitory concentration (MIC) values ranging from 0.352 ± 0.02 to 0.703 ± 0.01 mg/ml and minimum bactericidal concentration (MBC) values ranging from 0.704 ± 0.02 to 1.408 ± 0.04 mg/ml. Density functional theory (DFT) at the B3LYP/3-21G level of theory was employed to enumerate, frontier orbital energy, enthalpy, free energy, electronic energy, MEP, dipole moment which evaluated the effect of certain groups (aliphatic and aromatic) on drug properties. They discovered that all esters were more thermodynamically stable than the parent molecule. Molecular docking is performed using AutoDock Vina to determine the binding affinities and interactions between the MGP esters and the SARS-CoV-2 main protease. The modified esters strongly interact with the prime Cys145, His41, MET165, GLY143, THR26, and ASN142 residues. The MGP esters' shape and ability to form multiple electrostatic and hydrogen bonds with the active site match other minor-groove binders' binding modes. The molecular dynamics simulation validates the molecular docking results. The pharmacokinetic characterization of the optimized inhibitor demonstrates that these MGP esters appear to be safer inhibitors and a combination of in silico ADMET (absorption, distribution, metabolism, excretion, and toxicity) prediction and drug-likeness had promising results due to their improved kinetic properties. Structure activity relationships (SAR) study including in vitro and silico results revealed that the acyl chain, palmitoyl (C16) and 4-chlorobenzoyl (4.ClC6H4CO-) in combination with sugar were found the most potential activates against human and fungal pathogens. After all, our comprehensive computational and statistical analysis shows that these selected MGP esters can be used as potential inhibitors against the SARS-CoV-2. Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6-O-acyl MGP esters by direct acylation method with an excellent yield. To obtain newer products for antimicrobial assessment studies, the 6-O-MGP esters were further modified into 2,3,4-tri-O-acyl MGP esters containing a wide variety of functionalities in a single molecular framework. The chemical structures of the newly synthesized compounds were elucidated by analyzing their physicochemical, elemental, and spectroscopic data. In vitro antimicrobial testing against five bacteria and two fungi and the prediction of activity spectra for substances (PASS) revealed that these MGP estes have promising antifungal functionality compared to their antibacterial activities. The antimicrobial tests demonstrated that the compounds 3 and 10 were the most potent against Bacillus subtilis and Escherichia coli strains, with the minimum inhibitory concentration (MIC) values ranging from 0.352 ± 0.02 to 0.703 ± 0.01 mg/ml and minimum bactericidal concentration (MBC) values ranging from 0.704 ± 0.02 to 1.408 ± 0.04 mg/ml. Density functional theory (DFT) at the B3LYP/3-21G level of theory was employed to enumerate, frontier orbital energy, enthalpy, free energy, electronic energy, MEP, dipole moment which evaluated the effect of certain groups (aliphatic and aromatic) on drug properties. They discovered that all esters were more thermodynamically stable than the parent molecule. Molecular docking is performed using AutoDock Vina to determine the binding affinities and interactions between the MGP esters and the SARS-CoV-2 main protease. The modified esters strongly interact with the prime Cys145, His41, MET165, GLY143, THR26, and ASN142 residues. The MGP esters' shape and ability to form multiple electrostatic and hydrogen bonds with the active site match other minor-groove binders' binding modes. The molecular dynamics simulation validates the molecular docking results. The pharmacokinetic characterization of the optimized inhibitor demonstrates that these MGP esters appear to be safer inhibitors and a combination of in silico ADMET (absorption, distribution, metabolism, excretion, and toxicity) prediction and drug-likeness had promising results due to their improved kinetic properties. Structure activity relationships (SAR) study including in vitro and silico results revealed that the acyl chain, palmitoyl (C16) and 4-chlorobenzoyl (4.ClC H CO-) in combination with sugar were found the most potential activates against human and fungal pathogens. After all, our comprehensive computational and statistical analysis shows that these selected MGP esters can be used as potential inhibitors against the SARS-CoV-2. Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6- O -acyl MGP esters by direct acylation method with an excellent yield. To obtain newer products for antimicrobial assessment studies, the 6- O -MGP esters were further modified into 2,3,4-tri- O -acyl MGP esters containing a wide variety of functionalities in a single molecular framework. The chemical structures of the newly synthesized compounds were elucidated by analyzing their physicochemical, elemental, and spectroscopic data. In vitro antimicrobial testing against five bacteria and two fungi and the prediction of activity spectra for substances (PASS) revealed that these MGP estes have promising antifungal functionality compared to their antibacterial activities. The antimicrobial tests demonstrated that the compounds 3 and 10 were the most potent against Bacillus subtilis and Escherichia coli strains, with the minimum inhibitory concentration (MIC) values ranging from 0.352 ± 0.02 to 0.703 ± 0.01 mg/ml and minimum bactericidal concentration (MBC) values ranging from 0.704 ± 0.02 to 1.408 ± 0.04 mg/ml. Density functional theory (DFT) at the B3LYP/3-21G level of theory was employed to enumerate, frontier orbital energy, enthalpy, free energy, electronic energy, MEP, dipole moment which evaluated the effect of certain groups (aliphatic and aromatic) on drug properties. They discovered that all esters were more thermodynamically stable than the parent molecule. Molecular docking is performed using AutoDock Vina to determine the binding affinities and interactions between the MGP esters and the SARS-CoV-2 main protease. The modified esters strongly interact with the prime Cys145, His41, MET165, GLY143, THR26, and ASN142 residues. The MGP esters’ shape and ability to form multiple electrostatic and hydrogen bonds with the active site match other minor-groove binders’ binding modes. The molecular dynamics simulation validates the molecular docking results. The pharmacokinetic characterization of the optimized inhibitor demonstrates that these MGP esters appear to be safer inhibitors and a combination of in silico ADMET (absorption, distribution, metabolism, excretion, and toxicity) prediction and drug-likeness had promising results due to their improved kinetic properties. Structure activity relationships (SAR) study including in vitro and silico results revealed that the acyl chain, palmitoyl (C16) and 4-chlorobenzoyl (4.ClC 6 H 4 CO-) in combination with sugar were found the most potential activates against human and fungal pathogens. After all, our comprehensive computational and statistical analysis shows that these selected MGP esters can be used as potential inhibitors against the SARS-CoV-2. Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study, methyl β-D-galactopyranoside (MGP) was treated with various acyl halides to produce 6-O-acyl MGP esters by direct acylation method with an excellent yield. To obtain newer products for antimicrobial assessment studies, the 6-O-MGP esters were further modified into 2,3,4-tri-O-acyl MGP esters containing a wide variety of functionalities in a single molecular framework. The chemical structures of the newly synthesized compounds were elucidated by analyzing their physicochemical, elemental, and spectroscopic data. In vitro antimicrobial testing against five bacteria and two fungi and the prediction of activity spectra for substances (PASS) revealed that these MGP estes have promising antifungal functionality compared to their antibacterial activities. The antimicrobial tests demonstrated that the compounds 3 and 10 were the most potent against Bacillus subtilis and Escherichia coli strains, with the minimum inhibitory concentration (MIC) values ranging from 0.352 ± 0.02 to 0.703 ± 0.01 mg/ml and minimum bactericidal concentration (MBC) values ranging from 0.704 ± 0.02 to 1.408 ± 0.04 mg/ml. Density functional theory (DFT) at the B3LYP/3-21G level of theory was employed to enumerate, frontier orbital energy, enthalpy, free energy, electronic energy, MEP, dipole moment which evaluated the effect of certain groups (aliphatic and aromatic) on drug properties. They discovered that all esters were more thermodynamically stable than the parent molecule. Molecular docking is performed using AutoDock Vina to determine the binding affinities and interactions between the MGP esters and the SARS-CoV-2 main protease. The modified esters strongly interact with the prime Cys145, His41, MET165, GLY143, THR26, and ASN142 residues. The MGP esters’ shape and ability to form multiple electrostatic and hydrogen bonds with the active site match other minor-groove binders’ binding modes. The molecular dynamics simulation validates the molecular docking results. The pharmacokinetic characterization of the optimized inhibitor demonstrates that these MGP esters appear to be safer inhibitors and a combination of in silico ADMET (absorption, distribution, metabolism, excretion, and toxicity) prediction and drug-likeness had promising results due to their improved kinetic properties. Structure activity relationships (SAR) study including in vitro and silico results revealed that the acyl chain, palmitoyl (C16) and 4-chlorobenzoyl (4.ClC6H4CO-) in combination with sugar were found the most potential activates against human and fungal pathogens. After all, our comprehensive computational and statistical analysis shows that these selected MGP esters can be used as potential inhibitors against the SARS-CoV-2. |
| Author | Amin, Md R. Mahmud, Shafi Emran, Talha B. Dey, Sujan Ozeki, Yasuhiro Yasmin, Farhana Saleh, Md A. Fujii, Yuki Yamada, Masao Hasan, Imtiaj Ogawa, Yukiko Kawsar, Sarkar M. A. Rajia, Sultana |
| Author_xml | – sequence: 1 givenname: Md R. surname: Amin fullname: Amin, Md R. organization: Laboratory of Carbohydrate and Nucleoside Chemistry, Department of Chemistry, Faculty of Science, University of Chittagong – sequence: 2 givenname: Farhana surname: Yasmin fullname: Yasmin, Farhana organization: Laboratory of Carbohydrate and Nucleoside Chemistry, Department of Chemistry, Faculty of Science, University of Chittagong – sequence: 3 givenname: Sujan surname: Dey fullname: Dey, Sujan organization: Department of Microbiology, Faculty of Biological Science, University of Chittagong – sequence: 4 givenname: Shafi surname: Mahmud fullname: Mahmud, Shafi organization: Microbiology Laboratory, Department of Genetic Engineering and Biotechnology, University of Rajshahi – sequence: 5 givenname: Md A. surname: Saleh fullname: Saleh, Md A. organization: Microbiology Laboratory, Department of Genetic Engineering and Biotechnology, University of Rajshahi – sequence: 6 givenname: Talha B. surname: Emran fullname: Emran, Talha B. organization: Department of Pharmacy, BGC Trust University Bangladesh – sequence: 7 givenname: Imtiaj surname: Hasan fullname: Hasan, Imtiaj organization: Department of Biochemistry and Molecular Biology, Faculty of Science, University of Rajshahi – sequence: 8 givenname: Sultana surname: Rajia fullname: Rajia, Sultana organization: Center for Interdisciplinary Research, Varendra University – sequence: 9 givenname: Yukiko surname: Ogawa fullname: Ogawa, Yukiko organization: School of Pharmaceutical Sciences, Nagasaki International University – sequence: 10 givenname: Yuki surname: Fujii fullname: Fujii, Yuki organization: School of Pharmaceutical Sciences, Nagasaki International University – sequence: 11 givenname: Masao surname: Yamada fullname: Yamada, Masao organization: School of Science, Yokohama City University – sequence: 12 givenname: Yasuhiro orcidid: 0000-0002-2782-6158 surname: Ozeki fullname: Ozeki, Yasuhiro email: ozeki@yokohama-cu.ac.jp organization: School of Science, Yokohama City University – sequence: 13 givenname: Sarkar M. A. surname: Kawsar fullname: Kawsar, Sarkar M. A. email: akawsarabe@yahoo.com organization: Laboratory of Carbohydrate and Nucleoside Chemistry, Department of Chemistry, Faculty of Science, University of Chittagong |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35037163$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9ks9u1DAQxi1URNuFF-CALHHhsAY7cWKHQ6XV8lcqArHA1XIc765LYqd2ghQei5fgxjMxJaXQHnqyPPP9Ps-M5xgd-OAtQg8ZfcooFc8So4JVhGaMwD2vSH4HHbFC5IRXsjxARzSTGaFU0kN0nNIZBYhn8h46zAuaC1bmR-jnOzvspxb_-kFekJ1utRlCP0XtQ3KNxTYNNiasE-7DYP3gdIud37vaDQHi2xDxZvVxQ9bhC8lwH0GkE2D--9TZ5zhNftjb5NISa4A7Z2KowWOJP6w2myXuQmvN2OqIm2C-Or-7Fpq8BiLh5DoIDC54qMQ3-HwEs7HDJnT9OMyJ--juVrfJPrg8F-jzq5ef1m_I6fvXb9erU2K44APhwlBmBDXbvORZXdusrE2jaSUkFU3FmqIoNC8LXjNaMl7ZqqaFNI2ttjk1QuQLdDL79mPd2cbATKJuVR9dp-Okgnbqesa7vdqFb0qKkklRgMGTS4MYzkeYr-pcMrZttbdhTCorMypkIeF3FujxDelZGKOH9kDFRVUUXFagevR_RVel_P1jEGSzAIafUrTbKwmj6mKR1LxIChZJ_VkkdQHJG5Bx86ihK9fejuYzmuAdv7PxX9m3UL8BTGfiKQ |
| CitedBy_id | crossref_primary_10_1016_j_jep_2024_118301 crossref_primary_10_1039_D2NJ05703D crossref_primary_10_3389_fmicb_2023_1206816 crossref_primary_10_1002_slct_202304774 crossref_primary_10_1016_j_jsps_2024_102093 crossref_primary_10_1371_journal_pone_0314422 crossref_primary_10_1007_s11030_024_10888_8 crossref_primary_10_1016_j_chphi_2024_100700 crossref_primary_10_3389_fonc_2023_1228865 crossref_primary_10_1080_00498254_2024_2361457 crossref_primary_10_1080_07391102_2023_2198606 crossref_primary_10_1080_15257770_2023_2215839 crossref_primary_10_1016_j_molstruc_2023_135999 crossref_primary_10_1515_psr_2022_0282 crossref_primary_10_1007_s10562_023_04337_8 crossref_primary_10_1080_16583655_2024_2327101 crossref_primary_10_1080_07391102_2022_2121761 crossref_primary_10_1016_j_ijbiomac_2024_134870 crossref_primary_10_1016_j_arabjc_2024_105798 crossref_primary_10_1016_j_chphi_2024_100615 crossref_primary_10_1124_pharmrev_123_000863 crossref_primary_10_1080_15257770_2024_2333495 crossref_primary_10_1016_j_molstruc_2024_137930 crossref_primary_10_1016_j_molstruc_2024_141206 crossref_primary_10_1080_10286020_2024_2343821 crossref_primary_10_1080_17425255_2024_2330666 crossref_primary_10_1080_15257770_2022_2096898 crossref_primary_10_3390_molecules28062613 |
| Cites_doi | 10.1016/j.jgg.2020.02.001 10.3389/fmolb.2021.628585 10.5582/bst.2020.01020 10.4137/DTI.S12519 10.1021/ct900275y 10.1103/PhysRevB.37.785 10.1016/S0076-6879(06)16024-3 10.1080/17512433.2021.1959318 10.1063/1.470117 10.1007/978-1-4684-7529-6_9 10.4236/ijoc.2015.54023 10.1016/s0169-409x(00)00129-0 10.1002/jcc.23899 10.4067/S0717-97072021000205206 10.1093/glycob/3.2.97 10.1103/PhysRevA.38.3098 10.1002/jcc.20035 10.1002/elps.1150181505 10.5267/j.ccl.2015.12.001 10.3797/scipharm.1308-03 10.1038/nature05819 10.1007/978-1-4939-7366-8_4 10.1021/ci300367a 10.1021/acs.jmedchem.5b00104 10.1016/j.jmgm.2006.02.009 10.1093/ajcp/45.4_ts.493 10.3390/biology10070589 10.3390/molecules25225433 10.1038/s41598-019-43828-w 10.1126/science.1059820 10.1021/cr00023a005 10.1002/jps.2600710611 10.1021/ja0047368 10.1063/1.4872239 10.1016/j.saa.2013.10.042 10.15671/hjbc.622038 10.1007/s40203-021-00102-0 10.23893/1307-2080.APS.05704 10.35812/CelluloseChemTechnol.2021.55.44 10.23893/1307-2080.APS.05622 10.29356/jmcs.v65i1.1464 10.33435/tcandtc.718807 10.1007/978-1-4939-2269-7 10.12692/ijb/12.6.211-219 10.22036/pcr.2021.264541.1869 10.22034/ijnc.2020.131337.1124 10.1093/nar/28.1.235 10.1002/9780470125793.ch7 10.17516/1998-2836-0226 10.3897/pharmacia.68.e56543 10.17516/1998-2836-0199 10.25177/JCCMM.4.4.RA.10663 10.2478/auoc-2021-0002 10.9734/bpi/cacb/v6/8670D |
| ContentType | Journal Article |
| Copyright | The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022. |
| Copyright_xml | – notice: The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 – notice: 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. – notice: The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022. |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7T5 7X7 7XB 88A 88E 88I 8AO 8FE 8FH 8FI 8FJ 8FK ABUWG AFKRA AZQEC BBNVY BENPR BHPHI CCPQU DWQXO FYUFA GHDGH GNUQQ H94 HCIFZ K9. LK8 M0S M1P M2P M7P PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS Q9U 7X8 5PM |
| DOI | 10.1007/s10719-021-10039-3 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Immunology Abstracts Health & Medical Collection (ProQuest) ProQuest Central (purchase pre-March 2016) Biology Database (Alumni Edition) Medical Database (Alumni Edition) Science Database (Alumni Edition) ProQuest Pharma Collection 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 UK/Ireland ProQuest Central Essentials Biological Science Collection ProQuest Central Database Suite (ProQuest) Natural Science Collection ProQuest One ProQuest Central Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student AIDS and Cancer Research Abstracts SciTech Collection (ProQuest) ProQuest Health & Medical Complete (Alumni) Biological Sciences ProQuest Health & Medical Collection Medical Database Science Database (ProQuest) Biological Science Database (ProQuest) ProQuest Central Premium ProQuest One Academic (New) ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China ProQuest Central Basic MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Central China ProQuest Biology Journals (Alumni Edition) ProQuest Central ProQuest One Applied & Life Sciences ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Health & Medical Research Collection Biological Science Collection AIDS and Cancer Research Abstracts ProQuest Central (New) ProQuest Medical Library (Alumni) ProQuest Science Journals (Alumni Edition) ProQuest Biological Science Collection ProQuest Central Basic ProQuest Science Journals 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 Immunology Abstracts ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE ProQuest Central Student |
| 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: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry Biology |
| EISSN | 1573-4986 |
| EndPage | 290 |
| ExternalDocumentID | PMC8761875 35037163 10_1007_s10719_021_10039_3 |
| Genre | Journal Article |
| GroupedDBID | --- -4W -56 -5G -BR -EM -Y2 -~C .86 .VR 06C 06D 0R~ 0VY 1N0 1SB 2.D 203 28- 29I 29~ 2J2 2JN 2JY 2KG 2KM 2LR 2P1 2VQ 2~H 30V 3O- 3SX 3V. 4.4 406 408 409 40D 40E 53G 5GY 5QI 5RE 5VS 67N 67Z 6NX 7X7 88A 88E 88I 8AO 8CJ 8FE 8FH 8FI 8FJ 8TC 8UJ 95- 95. 95~ 96X AAAVM AABHQ AACDK AAHNG AAIAL AAJBT AAJKR AANXM AANZL AARHV AARTL AASML AATNV AATVU AAUYE AAWCG AAYIU AAYQN AAYTO AAYZH ABAKF ABBBX ABBXA ABDZT ABECU ABFTV ABHLI ABHQN ABJNI ABJOX ABKCH ABKTR ABMNI ABMQK ABNWP ABPLI ABQBU ABQSL ABSXP ABTEG ABTHY ABTKH ABTMW ABULA ABUWG ABWNU ABXPI ACAOD ACBXY ACDTI ACGFS ACGOD ACHSB ACHXU ACKNC ACMDZ ACMLO ACNCT ACOKC ACOMO ACPIV ACPRK ACSNA ACZOJ ADBBV ADHHG ADHIR ADIMF ADINQ ADKNI ADKPE ADRFC ADTPH ADURQ ADYFF ADYPR ADZKW AEBTG AEFIE AEFQL AEGAL AEGNC AEJHL AEJRE AEKMD AEMSY AENEX AEOHA AEPYU AESKC AETLH AEVLU AEXYK AFBBN AFEXP AFGCZ AFKRA AFLOW AFQWF AFWTZ AFZKB AGAYW AGDGC AGGDS AGJBK AGMZJ AGQEE AGQMX AGRTI AGWIL AGWZB AGYKE AHAVH AHBYD AHKAY AHMBA AHSBF AHYZX AIAKS AIGIU AIIXL AILAN AITGF AJBLW AJRNO AJZVZ AKMHD ALIPV ALMA_UNASSIGNED_HOLDINGS ALWAN AMKLP AMXSW AMYLF AMYQR AOCGG ARMRJ ASPBG AVWKF AXYYD AZFZN AZQEC B-. BA0 BBNVY BBWZM BDATZ BENPR BGNMA BHPHI BPHCQ BSONS BVXVI CAG CCPQU COF CS3 CSCUP D1J DDRTE DL5 DNIVK DPUIP DU5 DWQXO EBD EBLON EBS EIOEI EJD EMOBN EN4 EPAXT ESBYG F5P FEDTE FERAY FFXSO FIGPU FINBP FNLPD FRRFC FSGXE FWDCC FYUFA G-Y G-Z GGCAI GGRSB GJIRD GNUQQ GNWQR GQ6 GQ7 GQ8 GXS H13 HCIFZ HF~ HG5 HG6 HMCUK HMJXF HQYDN HRMNR HVGLF HZ~ I09 IHE IJ- IKXTQ ITM IWAJR IXC IXE IZIGR IZQ I~X I~Z J-C J0Z JBSCW JCJTX JZLTJ KDC KOV KOW KPH LAK LK8 LLZTM M0L M1P M2P M4Y M7P MA- N2Q NB0 NDZJH NPVJJ NQJWS NU0 O9- O93 O9G O9I O9J OAM OVD P19 P2P PF0 PQQKQ PROAC PSQYO PT4 PT5 Q2X QOK QOR QOS R4E R89 R9I RHV RNI ROL RPX RRX RSV RZC RZE RZK S16 S1Z S26 S27 S28 S3A S3B SAP SBL SBY SCLPG SDH SDM SHX SISQX SJYHP SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW SSXJD STPWE SV3 SZN T13 T16 TEORI TSG TSK TSV TUC U2A U9L UG4 UKHRP UOJIU UTJUX UZXMN VC2 VFIZW W23 W48 W4F WJK WK6 WK8 Y6R YLTOR Z45 Z7U Z7V Z7W Z87 Z8O Z8P Z8Q Z91 Z92 ZMTXR ZOVNA ~EX ~KM AAPKM AAYXX ABBRH ABDBE ABFSG ACSTC ADHKG AEZWR AFDZB AFHIU AFOHR AGQPQ AHPBZ AHWEU AIXLP ATHPR AYFIA CITATION PHGZM PHGZT CGR CUY CVF ECM EIF NPM 7T5 7XB 8FK ABRTQ H94 K9. PJZUB PKEHL PPXIY PQEST PQGLB PQUKI PRINS Q9U 7X8 5PM |
| ID | FETCH-LOGICAL-c474t-47c01c70cf3642bbe26bcda097807d91d555a4654b106149e9b058cde9f30c773 |
| IEDL.DBID | U2A |
| ISSN | 0282-0080 1573-4986 |
| IngestDate | Thu Aug 21 14:07:04 EDT 2025 Fri Jul 11 03:28:48 EDT 2025 Fri Jul 25 18:53:00 EDT 2025 Wed Feb 19 02:25:32 EST 2025 Tue Jul 01 00:45:44 EDT 2025 Thu Apr 24 23:06:42 EDT 2025 Fri Feb 21 02:47:16 EST 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 2 |
| Keywords | Antimicrobial Molecular dynamics SARS-CoV-2 protease Methyl β-D-galactopyranoside Molecular docking Pharmacokinetic |
| Language | English |
| License | 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c474t-47c01c70cf3642bbe26bcda097807d91d555a4654b106149e9b058cde9f30c773 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| ORCID | 0000-0002-2782-6158 |
| OpenAccessLink | https://pubmed.ncbi.nlm.nih.gov/PMC8761875 |
| PMID | 35037163 |
| PQID | 2647955489 |
| PQPubID | 55359 |
| PageCount | 30 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_8761875 proquest_miscellaneous_2620785816 proquest_journals_2647955489 pubmed_primary_35037163 crossref_primary_10_1007_s10719_021_10039_3 crossref_citationtrail_10_1007_s10719_021_10039_3 springer_journals_10_1007_s10719_021_10039_3 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2022-04-01 |
| PublicationDateYYYYMMDD | 2022-04-01 |
| PublicationDate_xml | – month: 04 year: 2022 text: 2022-04-01 day: 01 |
| PublicationDecade | 2020 |
| PublicationPlace | New York |
| PublicationPlace_xml | – name: New York – name: United States |
| PublicationSubtitle | Official Journal of the International Glycoconjugate Organization |
| PublicationTitle | Glycoconjugate journal |
| PublicationTitleAbbrev | Glycoconj J |
| PublicationTitleAlternate | Glycoconj J |
| PublicationYear | 2022 |
| Publisher | Springer US Springer Nature B.V |
| Publisher_xml | – name: Springer US – name: Springer Nature B.V |
| References | Varki (CR3) 1993; 3 Cheng, Li, Zhou, Shen, Wu, Liu (CR53) 2012; 52 Harvey, De Fabritiis (CR47) 2009; 5 Politzer, Murray (CR60) 1991; 2 CR39 CR38 CR37 Bauer, Kirby, Sherris, Truck (CR32) 1966; 45 CR33 CR30 Kawsar, Kumar (CR17) 2021; 66 Lipinski, Lombardo, Dominy, Feeney (CR54) 2021; 46 Guex, Peitsch (CR40) 1997; 18 Chen, Fukuda (CR2) 2006; 416 Essmann, Perera, Berkowitz, Darden, Lee, Pedersen (CR46) 1995; 103 Mahmud, Biswas, Paul, Mita, Promi, Afrose, Hasan, Zaman, Uddin, Dhama (CR50) 2021; 10 Kawsar, Kabir, Manik, Hossain, Anwar (CR28) 2012; 2 Seeberger, Werz (CR4) 2007; 446 CR5 CR8 Krieger, Vriend (CR49) 2015; 36 CR9 Harrach, Drossel (CR45) 2014; 140 Pearson (CR36) 1986; 83 CR42 CR41 Grzywacz, Liberek, Myszka (CR21) 2020; 25 Shagir, Bhuiyan, Ozeki, Kawsar (CR7) 2016; 5 Perlstein (CR62) 2001; 123 Pires, Blundell, Ascher (CR64) 2015; 58 Kawsar, Faruk, Rahman, Fujii, Ozeki (CR19) 2014; 82 Lu (CR22) 2020; 14 (CR34) 1998; 38 CR18 Agamennone, Le, Straalen, Brouwer, Roelofs (CR20) 2019; 9 Land, Humble (CR43) 2018; 1685 Mahmud, Mita, Biswas, Paul, Promi, Afrose, Hasan, Shimu, Zaman, Uddin, Tallei, Emran, Saleh (CR51) 2021; 00 CR16 Bertozzi, Kiessling (CR1) 2001; 291 CR15 Hunt (CR55) 1975; 56 CR14 CR58 CR13 CR12 CR11 CR10 Lee, Yang, Parr (CR35) 1988; 37 Mahmud, Paul, Biswas, Afrose, Mita, Hasan, Shimu, Hossain, Promi, Ema, Chidambaram, Chandrasekaran, Alqahtani, Emran, Saleh (CR52) 2021; 8 Amin (CR59) 2013; 7 Kabir, Matin, Kawsar (CR29) 1998; 22 Grover, Moore (CR31) 1962; 52 Krieger, Nielsen, Spronk, Vriend (CR48) 2006; 25 Lien, Guo, Li, Su (CR57) 1982; 71 CR27 CR26 CR25 CR24 Cohen, Benson (CR56) 1993; 93 Kawsar, Hamida, Sheikh, Hossain, Shagir, Sanaullah, Manchur, Imtiaj, Ogawa, Fujii, Koide, Ozeki (CR6) 2015; 5 CR23 CR61 Wang, Wolf, Caldwell, Kollman, Case (CR44) 2004; 25 Liu, Wang (CR63) 2020; 7 10039_CR23 10039_CR24 CA Lipinski (10039_CR54) 2021; 46 10039_CR25 S Mahmud (10039_CR50) 2021; 10 10039_CR26 WA Hunt (10039_CR55) 1975; 56 J Perlstein (10039_CR62) 2001; 123 10039_CR27 10039_CR61 SMA Kawsar (10039_CR17) 2021; 66 H Lu (10039_CR22) 2020; 14 N Guex (10039_CR40) 1997; 18 P Politzer (10039_CR60) 1991; 2 H Land (10039_CR43) 2018; 1685 PH Seeberger (10039_CR4) 2007; 446 N Cohen (10039_CR56) 1993; 93 DEV Pires (10039_CR64) 2015; 58 A Varki (10039_CR3) 1993; 3 10039_CR37 10039_CR38 10039_CR39 RK Grover (10039_CR31) 1962; 52 SMA Kawsar (10039_CR19) 2014; 82 10039_CR30 X Liu (10039_CR63) 2020; 7 10039_CR5 V Agamennone (10039_CR20) 2019; 9 AKMS Kabir (10039_CR29) 1998; 22 10039_CR33 S Chen (10039_CR2) 2006; 416 S Mahmud (10039_CR52) 2021; 8 CR Bertozzi (10039_CR1) 2001; 291 SMA Kawsar (10039_CR28) 2012; 2 MJ Harvey (10039_CR47) 2009; 5 EJ Lien (10039_CR57) 1982; 71 C Lee (10039_CR35) 1988; 37 S Mahmud (10039_CR51) 2021; 00 E Krieger (10039_CR49) 2015; 36 SMA Kawsar (10039_CR6) 2015; 5 10039_CR41 10039_CR42 MF Harrach (10039_CR45) 2014; 140 10039_CR9 10039_CR8 AC Shagir (10039_CR7) 2016; 5 E Krieger (10039_CR48) 2006; 25 10039_CR12 10039_CR13 U Essmann (10039_CR46) 1995; 103 10039_CR14 F Cheng (10039_CR53) 2012; 52 10039_CR58 10039_CR15 10039_CR16 10039_CR18 D Grzywacz (10039_CR21) 2020; 25 J Wang (10039_CR44) 2004; 25 Density-functional exchange-energy approximation with correct asymptotic behaviour (10039_CR34) 1998; 38 10039_CR10 10039_CR11 RG Pearson (10039_CR36) 1986; 83 ML Amin (10039_CR59) 2013; 7 AW Bauer (10039_CR32) 1966; 45 |
| References_xml | – volume: 7 start-page: 119 year: 2020 end-page: 121 ident: CR63 article-title: Potential inhibitors against 2019-nCoV coronavirus M protease from clinically approved medicines publication-title: J. Genet. Genom. doi: 10.1016/j.jgg.2020.02.001 – volume: 8 year: 2021 ident: CR52 article-title: Prospective role of peptide-based antiviral therapy against the main protease of SARS-CoV-2 publication-title: Front. Mol. Biosci. doi: 10.3389/fmolb.2021.628585 – ident: CR39 – ident: CR16 – ident: CR12 – volume: 14 start-page: 69 year: 2020 end-page: 71 ident: CR22 article-title: Drug treatment options for the 2019-new coronavirus (2019-nCoV) publication-title: Biosci. Trends. doi: 10.5582/bst.2020.01020 – volume: 7 start-page: 27 year: 2013 end-page: 34 ident: CR59 article-title: P-glycoprotein inhibition for optimal drug delivery publication-title: Drug Target Insight. doi: 10.4137/DTI.S12519 – ident: CR61 – volume: 5 start-page: 2371 year: 2009 end-page: 2377 ident: CR47 article-title: An implementation of the smooth particle mesh Ewald method on GPU hardware publication-title: J. Chem. Theory Comput. doi: 10.1021/ct900275y – ident: CR8 – ident: CR58 – volume: 37 start-page: 785 year: 1988 end-page: 789 ident: CR35 article-title: Development of the colle-Salvetti correlation-energy formula into a functional of the electron density publication-title: Phys. Rev. B. doi: 10.1103/PhysRevB.37.785 – volume: 416 start-page: 371 year: 2006 end-page: 380 ident: CR2 article-title: Cell type-specific roles of carbohydrates in tumor metastasis publication-title: Meth. Enzymol. doi: 10.1016/S0076-6879(06)16024-3 – ident: CR25 – ident: CR42 – volume: 00 start-page: 1 year: 2021 end-page: 11 ident: CR51 article-title: Molecular docking and dynamics study to explore phytochemical ligand molecules against the main protease of SARS-CoV-2 from extensive phytochemical datasets publication-title: Expert Rev. Clin. Pharmacol. doi: 10.1080/17512433.2021.1959318 – volume: 103 start-page: 8577 year: 1995 end-page: 8593 ident: CR46 article-title: A smooth particle mesh Ewald method publication-title: J. Chem. Phys. doi: 10.1063/1.470117 – volume: 56 start-page: 195 year: 1975 end-page: 210 ident: CR55 article-title: The effects of aliphatic alcohols on the biophysical and biochemical correlates of membrane function publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-1-4684-7529-6_9 – volume: 5 start-page: 232 year: 2015 end-page: 245 ident: CR6 article-title: Chemically modified uridine molecules incorporating acyl residues to enhance antibacterial and cytotoxic activities publication-title: Int. J. Org. Chem. doi: 10.4236/ijoc.2015.54023 – ident: CR15 – volume: 2 start-page: 66 year: 2012 end-page: 73 ident: CR28 article-title: Antibacterial and mycelial growth inhibition of some acylated derivatives of D-glucopyranoside publication-title: Int. J. Biosci. – volume: 46 start-page: 3 year: 2021 end-page: 25 ident: CR54 article-title: Experimental and computational approaches to estimate solubility and permeability in drug discovery and development publication-title: Adv. Drug Deliv. Rev. doi: 10.1016/s0169-409x(00)00129-0 – ident: CR11 – ident: CR9 – volume: 36 start-page: 996 year: 2015 end-page: 1007 ident: CR49 article-title: New ways to boost molecular dynamics simulations publication-title: J. Comput. Chem. doi: 10.1002/jcc.23899 – volume: 66 start-page: 5206 year: 2021 end-page: 5214 ident: CR17 article-title: Computational investigation of methyl α-D-glucopyranoside derivatives as inhibitor against bacteria, fungi and COVID-19 (SARS-2) publication-title: J. Chil. Chem. Soci. doi: 10.4067/S0717-97072021000205206 – ident: CR5 – volume: 3 start-page: 97 year: 1993 end-page: 112 ident: CR3 publication-title: Glycobiology doi: 10.1093/glycob/3.2.97 – volume: 2 start-page: 273 year: 1991 end-page: 312 ident: CR60 article-title: Molecular electrostatic potentials and chemical reactivity publication-title: Rev. Comput. Chem. – ident: CR26 – volume: 38 start-page: 3098 year: 1998 end-page: 3100 ident: CR34 article-title: Becke, A.D publication-title: Phys. Rev. A. doi: 10.1103/PhysRevA.38.3098 – volume: 25 start-page: 1157 year: 2004 end-page: 1174 ident: CR44 article-title: Development and testing of a general Amber force field publication-title: J. Comput. Chem. doi: 10.1002/jcc.20035 – ident: CR18 – volume: 52 start-page: 876 year: 1962 end-page: 879 ident: CR31 article-title: In-vitro efficacy of certain essential oils and plant extracts against three major pathogens of Jatropha curcas L publication-title: Phytopathology – ident: CR14 – ident: CR37 – volume: 18 start-page: 2714 year: 1997 end-page: 2723 ident: CR40 article-title: SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling publication-title: Electrophoresis doi: 10.1002/elps.1150181505 – volume: 5 start-page: 83 year: 2016 end-page: 92 ident: CR7 article-title: Simple and rapid synthesis of some nucleoside derivatives: structural and spectral characterization publication-title: Curr. Chem. Lett. doi: 10.5267/j.ccl.2015.12.001 – volume: 82 start-page: 1 year: 2014 end-page: 20 ident: CR19 article-title: Regioselective synthesis, characterization and antimicrobial activities of some new monosaccharide derivatives publication-title: Sci. Pharm. doi: 10.3797/scipharm.1308-03 – ident: CR30 – volume: 22 start-page: 13 year: 1998 end-page: 18 ident: CR29 article-title: Synthesis and antibacterial activities of some uridine derivatives publication-title: Chittagong Univ. J. Sci. – ident: CR10 – ident: CR33 – volume: 446 start-page: 1046 year: 2007 end-page: 1051 ident: CR4 article-title: Synthesis and medical applications of oligosaccharides publication-title: Nature doi: 10.1038/nature05819 – volume: 1685 start-page: 43 year: 2018 end-page: 67 ident: CR43 article-title: YASARA: A tool to obtain structural guidance in biocatalytic investigations publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-7366-8_4 – volume: 52 start-page: 3099 year: 2012 end-page: 3105 ident: CR53 article-title: admetSAR: A comprehensive source and free tool for assessment of chemical ADMET properties publication-title: J. Chem. Inf. Mod. doi: 10.1021/ci300367a – volume: 58 start-page: 4066 year: 2015 end-page: 4072 ident: CR64 article-title: pkCSM: Predicting small-molecule pharmacokinetic and toxicity properties using graph-based signatures publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.5b00104 – ident: CR27 – ident: CR23 – volume: 83 start-page: 8440 year: 1986 end-page: 8441 ident: CR36 article-title: Absolute electronegativity and hardness correlated with molecular orbital theory publication-title: Proc. Nat. Acad. Sci. doi: 10.1103/PhysRevB.37.785 – volume: 25 start-page: 481 year: 2006 end-page: 486 ident: CR48 article-title: Fast empirical pKa prediction by Ewald summation publication-title: J. Mol. Graph. Model. doi: 10.1016/j.jmgm.2006.02.009 – volume: 45 start-page: 493 year: 1966 end-page: 496 ident: CR32 article-title: Antibiotic susceptibility testing by a standardized single disk method publication-title: Am. J. Clin. Pathol. doi: 10.1093/ajcp/45.4_ts.493 – volume: 10 start-page: 589 year: 2021 ident: CR50 article-title: Plant-based phytochemical screening by targeting main protease of SARS-CoV-2 to design effective potent inhibitors publication-title: Biology. doi: 10.3390/biology10070589 – ident: CR38 – ident: CR13 – volume: 25 start-page: 5433 year: 2020 ident: CR21 article-title: Synthesis, modification and biological activity of diosgenyl β-d-glycosaminosides: An overview publication-title: Molecules doi: 10.3390/molecules25225433 – volume: 9 start-page: 7308 year: 2019 ident: CR20 article-title: Antimicrobial activity and carbohydrate metabolism in the bacterial metagenome of the soil-living invertebrate Folsomia candida publication-title: Sci. Rep. doi: 10.1038/s41598-019-43828-w – volume: 291 start-page: 2357 year: 2001 end-page: 2364 ident: CR1 article-title: Chemical glycobiology publication-title: Science doi: 10.1126/science.1059820 – volume: 93 start-page: 2419 year: 1993 end-page: 2438 ident: CR56 article-title: Estimation of heats of formation of organic compounds by additivity methods publication-title: Chem. Rev. doi: 10.1021/cr00023a005 – volume: 71 start-page: 641 year: 1982 end-page: 655 ident: CR57 article-title: Use of dipole moment as a parameter in drug-receptor interaction and quantitative structure-activity relationship studies publication-title: J. Pharm. Sci. doi: 10.1002/jps.2600710611 – volume: 123 start-page: 191 year: 2001 end-page: 192 ident: CR62 article-title: The weak hydrogen bond in structural chemistry and biology publication-title: J. American Chem. Soc. doi: 10.1021/ja0047368 – ident: CR41 – ident: CR24 – volume: 140 year: 2014 ident: CR45 article-title: Structure and dynamics of TIP3P, TIP4P, and TIP5P water near smooth and atomistic walls of different hydroaffinity publication-title: J. Chem. Phys. doi: 10.1063/1.4872239 – volume: 18 start-page: 2714 year: 1997 ident: 10039_CR40 publication-title: Electrophoresis doi: 10.1002/elps.1150181505 – volume: 25 start-page: 481 year: 2006 ident: 10039_CR48 publication-title: J. Mol. Graph. Model. doi: 10.1016/j.jmgm.2006.02.009 – volume: 71 start-page: 641 year: 1982 ident: 10039_CR57 publication-title: J. Pharm. Sci. doi: 10.1002/jps.2600710611 – volume: 10 start-page: 589 year: 2021 ident: 10039_CR50 publication-title: Biology. doi: 10.3390/biology10070589 – ident: 10039_CR58 doi: 10.1016/j.saa.2013.10.042 – volume: 66 start-page: 5206 year: 2021 ident: 10039_CR17 publication-title: J. Chil. Chem. Soci. doi: 10.4067/S0717-97072021000205206 – volume: 5 start-page: 83 year: 2016 ident: 10039_CR7 publication-title: Curr. Chem. Lett. doi: 10.5267/j.ccl.2015.12.001 – volume: 36 start-page: 996 year: 2015 ident: 10039_CR49 publication-title: J. Comput. Chem. doi: 10.1002/jcc.23899 – volume: 5 start-page: 232 year: 2015 ident: 10039_CR6 publication-title: Int. J. Org. Chem. doi: 10.4236/ijoc.2015.54023 – ident: 10039_CR18 doi: 10.15671/hjbc.622038 – volume: 22 start-page: 13 year: 1998 ident: 10039_CR29 publication-title: Chittagong Univ. J. Sci. – ident: 10039_CR13 doi: 10.1007/s40203-021-00102-0 – ident: 10039_CR15 doi: 10.23893/1307-2080.APS.05704 – volume: 38 start-page: 3098 year: 1998 ident: 10039_CR34 publication-title: Phys. Rev. A. doi: 10.1103/PhysRevA.38.3098 – ident: 10039_CR25 doi: 10.35812/CelluloseChemTechnol.2021.55.44 – ident: 10039_CR10 doi: 10.23893/1307-2080.APS.05622 – ident: 10039_CR30 – volume: 93 start-page: 2419 year: 1993 ident: 10039_CR56 publication-title: Chem. Rev. doi: 10.1021/cr00023a005 – volume: 123 start-page: 191 year: 2001 ident: 10039_CR62 publication-title: J. American Chem. Soc. doi: 10.1021/ja0047368 – volume: 140 year: 2014 ident: 10039_CR45 publication-title: J. Chem. Phys. doi: 10.1063/1.4872239 – volume: 3 start-page: 97 year: 1993 ident: 10039_CR3 publication-title: Glycobiology doi: 10.1093/glycob/3.2.97 – volume: 5 start-page: 2371 year: 2009 ident: 10039_CR47 publication-title: J. Chem. Theory Comput. doi: 10.1021/ct900275y – ident: 10039_CR12 doi: 10.29356/jmcs.v65i1.1464 – ident: 10039_CR27 doi: 10.33435/tcandtc.718807 – ident: 10039_CR39 – volume: 82 start-page: 1 year: 2014 ident: 10039_CR19 publication-title: Sci. Pharm. doi: 10.3797/scipharm.1308-03 – ident: 10039_CR41 doi: 10.1007/978-1-4939-2269-7 – volume: 83 start-page: 8440 year: 1986 ident: 10039_CR36 publication-title: Proc. Nat. Acad. Sci. doi: 10.1103/PhysRevB.37.785 – volume: 25 start-page: 1157 year: 2004 ident: 10039_CR44 publication-title: J. Comput. Chem. doi: 10.1002/jcc.20035 – volume: 46 start-page: 3 year: 2021 ident: 10039_CR54 publication-title: Adv. Drug Deliv. Rev. doi: 10.1016/s0169-409x(00)00129-0 – ident: 10039_CR5 doi: 10.12692/ijb/12.6.211-219 – ident: 10039_CR24 doi: 10.22036/pcr.2021.264541.1869 – ident: 10039_CR42 – volume: 7 start-page: 27 year: 2013 ident: 10039_CR59 publication-title: Drug Target Insight. doi: 10.4137/DTI.S12519 – volume: 291 start-page: 2357 year: 2001 ident: 10039_CR1 publication-title: Science doi: 10.1126/science.1059820 – volume: 9 start-page: 7308 year: 2019 ident: 10039_CR20 publication-title: Sci. Rep. doi: 10.1038/s41598-019-43828-w – volume: 00 start-page: 1 year: 2021 ident: 10039_CR51 publication-title: Expert Rev. Clin. Pharmacol. doi: 10.1080/17512433.2021.1959318 – volume: 52 start-page: 3099 year: 2012 ident: 10039_CR53 publication-title: J. Chem. Inf. Mod. doi: 10.1021/ci300367a – ident: 10039_CR61 – volume: 7 start-page: 119 year: 2020 ident: 10039_CR63 publication-title: J. Genet. Genom. doi: 10.1016/j.jgg.2020.02.001 – volume: 45 start-page: 493 year: 1966 ident: 10039_CR32 publication-title: Am. J. Clin. Pathol. doi: 10.1093/ajcp/45.4_ts.493 – volume: 1685 start-page: 43 year: 2018 ident: 10039_CR43 publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-7366-8_4 – volume: 58 start-page: 4066 year: 2015 ident: 10039_CR64 publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.5b00104 – volume: 14 start-page: 69 year: 2020 ident: 10039_CR22 publication-title: Biosci. Trends. doi: 10.5582/bst.2020.01020 – ident: 10039_CR26 doi: 10.22034/ijnc.2020.131337.1124 – volume: 56 start-page: 195 year: 1975 ident: 10039_CR55 publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-1-4684-7529-6_9 – ident: 10039_CR38 doi: 10.1093/nar/28.1.235 – volume: 2 start-page: 273 year: 1991 ident: 10039_CR60 publication-title: Rev. Comput. Chem. doi: 10.1002/9780470125793.ch7 – ident: 10039_CR14 doi: 10.17516/1998-2836-0226 – volume: 2 start-page: 66 year: 2012 ident: 10039_CR28 publication-title: Int. J. Biosci. – ident: 10039_CR9 doi: 10.3897/pharmacia.68.e56543 – ident: 10039_CR8 doi: 10.17516/1998-2836-0199 – volume: 446 start-page: 1046 year: 2007 ident: 10039_CR4 publication-title: Nature doi: 10.1038/nature05819 – volume: 25 start-page: 5433 year: 2020 ident: 10039_CR21 publication-title: Molecules doi: 10.3390/molecules25225433 – volume: 103 start-page: 8577 year: 1995 ident: 10039_CR46 publication-title: J. Chem. Phys. doi: 10.1063/1.470117 – ident: 10039_CR33 – ident: 10039_CR37 – volume: 416 start-page: 371 year: 2006 ident: 10039_CR2 publication-title: Meth. Enzymol. doi: 10.1016/S0076-6879(06)16024-3 – ident: 10039_CR23 doi: 10.25177/JCCMM.4.4.RA.10663 – volume: 52 start-page: 876 year: 1962 ident: 10039_CR31 publication-title: Phytopathology – volume: 8 year: 2021 ident: 10039_CR52 publication-title: Front. Mol. Biosci. doi: 10.3389/fmolb.2021.628585 – ident: 10039_CR11 doi: 10.2478/auoc-2021-0002 – volume: 37 start-page: 785 year: 1988 ident: 10039_CR35 publication-title: Phys. Rev. B. doi: 10.1103/PhysRevB.37.785 – ident: 10039_CR16 doi: 10.9734/bpi/cacb/v6/8670D |
| SSID | ssj0007428 |
| Score | 2.496614 |
| Snippet | Carbohydrate esters are significant in medicinal chemistry because of their efficacy for the synthesis of biologically active drugs. In the present study,... |
| SourceID | pubmedcentral proquest pubmed crossref springer |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 261 |
| SubjectTerms | Acylation Anti-Bacterial Agents - pharmacology Anti-Infective Agents - pharmacology Antibacterial activity Antifungal agents Antimicrobial agents Antiviral Agents - chemistry Antiviral Agents - pharmacology Biochemistry Biological activity Biomedical and Life Sciences Computer applications COVID-19 Esters Esters - pharmacology Free energy Galactose Humans Hydrogen bonding Life Sciences Minimum inhibitory concentration Molecular Docking Simulation Molecular dynamics Molecular Dynamics Simulation Original Original Article Pathology Peptide Hydrolases Pharmacokinetics Proteinase Proteinase inhibitors SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 Statistical analysis Toxicity Tribute to Professor Sen-itiroh Hakomori |
| SummonAdditionalLinks | – databaseName: Health & Medical Collection (ProQuest) dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3NbtQwELagCMGlghZKoCAjIS6sRf4cJ1zQslBVSEWIpWhvUfwTNdLG2ZLdQ_pYvAQ3nokZb7KrpaK3KHYSJzPxzNgz30fIq0jCvG84ZwXXBYtLX7LUmJIFUoM7XiZaRljvfPYlOT2PP8_4rF9wa_u0ymFOdBO1bhSukb8Fwy0ysH1p9n5xyZA1CndXewqN2-QOQpdh8CVmm4ALwz43E0NYwdA16otm-tI5geU7ISZ04W5otGuYrnmb15Mm_9k5dQbp5AHZ7z1JOl6L_iG5ZewBORxbiKLrjr6mLrfTLZofkLsfhqN7k4Hh7ZD8PjMgpjn984t9ZGApkHpn0YHxapDDkzoMhZYWLV00S0wqgqdV9qKSFTL0UPB26XT8bcomzQ8WUgf4ACaRGnvV1eYdbTsLzmVbtSMK0qvqykE-FfMR_TqeTke0Hoh5KXx8XLDfOdXZAq5oaVvVPcEYjMRqermCm61qqhwbxbrhETk_-fR9csp6YgemYhEvWSyUHyjhqzKC8EdKEyZS6QJLSnyhs0BzzgsEepMuYM1MJn2eKm2yMvKVENFjsmcba54QqsM4iQpfqEzxOBAqlYUIuZIZuHKZ0KFHgkGquepRz5F8Y55v8ZpRE3LQhNxpQh555M3mmsUa8-PG3seDsuT9_9_mW231yMtNM4gXt2MKa5oV9gnBP-NpkHjkaK1bm8dFHKEUE7i52NG6TQdEBd9tsdWFQwcH8xZAEOqR0aCf22H9_y2e3vwWz8j9EOs-XMrSMdlb_lyZ5-CNLeUL98v9BQjGNUY priority: 102 providerName: ProQuest |
| Title | Methyl β-D-galactopyranoside esters as potential inhibitors for SARS-CoV-2 protease enzyme: synthesis, antimicrobial, PASS, molecular docking, molecular dynamics simulations and quantum computations |
| URI | https://link.springer.com/article/10.1007/s10719-021-10039-3 https://www.ncbi.nlm.nih.gov/pubmed/35037163 https://www.proquest.com/docview/2647955489 https://www.proquest.com/docview/2620785816 https://pubmed.ncbi.nlm.nih.gov/PMC8761875 |
| Volume | 39 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3NbtNAEF7RVgguCFoohhItEuJCVvLfem1ubkipQK2qhqBwsrw_Vi3F64CTg3ksXoIbz8Tsxk4JBSROjrzrta0Zz3yTnfkGoRcBB7uvKCU5lTkJC5eTWKmCeFwCHC8iyQNT73x2Hp1Ow3czOuuKwpo-273fkrSW-pdiN2YKbnyTgmX2L4MdtEchdjd6PfXTjf2FYM_aXwgmiAFEXanMn9fYdkc3MObNVMnf9kutGzq5j-51-BGna4E_QLeU3kcHqYbYuWrxS2wzOu1f5fvo9nH_686o7-t2gL6fKRDOHP_4Rt4Q8A-m4c6iBZdVm86d2DInNDhv8KJemlQiuFupr0pemr48GDAunqSXEzKqPxIfW5oHcIRY6a9tpV7jptUAKZuyGWKQWVmVlugpnw_xRTqZDHHVt-PFEiwxvOLWqVbncEWDm7Lq2orBk2iJP69gsVWFhe1BsR54iKYn4w-jU9K1cyAiZOGShEy4nmCuKAIIejhXfsSFzE0hictk4klKaW7o3bgNUxOVcJfGQqqkCFzBWPAI7epaq8cISz-MgtxlIhE09JiIec58KngCAC5h0neQ10s1Ex3XuWm5Mc-uWZqNJmSgCZnVhCxw0KvNNYs108c_Zx_1ypJ1X32TAbhkCeCzOHHQ880wiNdswuRa1SszxwdURmMvctDhWrc2twuoIVCMYHG2pXWbCYYLfHtEl1eWExycmgehp4OGvX5eP9bf3-LJ_01_iu76pvrDJi4dod3ll5V6BphsyQdoh83YAO2lbz-9H8PxeHx-cTmwH-ZPOGs2EA |
| linkProvider | Springer Nature |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEF6VIlQuCFoegQKLBFzICr_WGyMhFFKqlDYVIi3KzXgfUS3FdooTIfOjOPAnuPGbmNnYiUJFb71F2fXa1ny7M-N5fIQ89yWc-4ZzlnCdsGDsSNYxZsxcqcEcH4da-ljvPDgO-6fBxxEfbZCfTS0MplU2Z6I9qHWh8Bv5a1DcIgLd14neTc8ZskZhdLWh0FjA4tBU38FlK98e7IF8X3je_oeTXp_VrAJMBSKYsUAox1XCUWMfbG8pjRdKpROsZ3CEjlzNOU-wy5i03lJkIunwjtImGvuOEsKHda-R66B4HUwhFKOlg4dupj35wY1haIrVRTp1qZ7AciEPE8gw-uqvK8IL1u3FJM1_IrVWAe7fJrdqy5V2F1C7QzZMvk12ujl47VlFX1KbS2o_0m-TG--bX1u9hlFuh_weGIDFhP75xfYYaCak-plWoCwL5AyltmdDSZOSTosZJjHB3dL8LJUpMgJRsK7psPt5yHrFF-ZR22ACVDA1-Y8qM29oWeVgzJZp2aaAljRLbYupZNKmn7rDYZtmDREwBWFjgGDtrypP4IqSlmlWE5rBk-Sans9hsXlGlWW_WAzcJadXIvJ7ZDMvcvOAUO0FoZ84QkWKB65QHZkIjysZgekYCe21iNtINVZ1l3Uk-5jEq_7QiIQYkBBbJMR-i7xaXjNd9Bi5dPZuA5a4Pm_KeLU7WuTZchjEi-GfJDfFHOd4YA_yjhu2yP0Ftpa38zm2bgxhcbGGuuUE7EK-PpKnZ7YbOahTF5zeFmk3-Fw91v_f4uHlb_GUbPVPBkfx0cHx4SNy08OaE5sutUs2Z9_m5jFYgjP5xG4_Sr5e9X7_C6hAcSc |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEF6VIh4XBC0PQ4FFAi5kVb_WGyMhFBKiltKqIhTlZrzrtWoptlOcCJmfxZE_wI3fxMzGThQqeustyq7XtubbnRnP4yPkuSfh3Necs5gnMfNTW7Ku1ilzZALmeBok0sN658OjYO_E_zDm4w3yq62FwbTK9kw0B3VSKvxGvguKW4Sg-7rhbtqkRRwPhm-nZwwZpDDS2tJpLCByoOvv4L5Vb_YHIOsXrjt8_7m_xxqGAaZ84c-YL5TtKGGr1AM7XErtBlIlMdY22CIJnYRzHmPHMWk8p1CH0uZdlegw9WwlhAfrXiFXhQdqE_aSGC-dPXQ5jRYAl4ahWdYU7DRlewJLh1xMJsNIrLeuFM9ZuucTNv-J2hplOLxNbjVWLO0tYHeHbOhii2z3CvDg85q-pCav1Hyw3yLX3rW_bvRbdrlt8vtQA0Qm9M9PNmCgpZD2Z1qD4iyRP5Sa_g0VjSs6LWeY0AR3y4rTTGbIDkTB0qaj3qcR65dfmEtNswlQx1QXP-pcv6ZVXYBhW2VVhwJysjwz7abiSYce90ajDs1bUmAKgsdgwdpfdRHDFRWtsrwhN4MnKRJ6NofF5jlVhgljMXCXnFyKyO-RzaIs9ANCE9cPvNgWKlTcd4Tqyli4XMkQzMhQJK5FnFaqkWo6riPxxyRa9YpGJESAhMggIfIs8mp5zXTRb-TC2TstWKLm7Kmi1U6xyLPlMIgXQ0Fxocs5znHBNuRdJ7DI_QW2lrfzOLZxDGBxsYa65QTsSL4-UmSnpjM5qFYHHGCLdFp8rh7r_2_x8OK3eEquw06PPu4fHTwiN10sPzGZUztkc_Ztrh-DUTiTT8zuo-TrZW_3v-6ddV0 |
| 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=Methyl+%CE%B2-D-galactopyranoside+esters+as+potential+inhibitors+for+SARS-CoV-2+protease+enzyme%3A+synthesis%2C+antimicrobial%2C+PASS%2C+molecular+docking%2C+molecular+dynamics+simulations+and+quantum+computations&rft.jtitle=Glycoconjugate+journal&rft.au=Amin%2C+Md+R&rft.au=Yasmin%2C+Farhana&rft.au=Dey%2C+Sujan&rft.au=Mahmud%2C+Shafi&rft.date=2022-04-01&rft.issn=1573-4986&rft.eissn=1573-4986&rft.volume=39&rft.issue=2&rft.spage=261&rft_id=info:doi/10.1007%2Fs10719-021-10039-3&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0282-0080&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0282-0080&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0282-0080&client=summon |