Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/90262
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dc.contributorDepartment of Applied Biology and Chemical Technologyen_US
dc.creatorWang, Yen_US
dc.creatorLiang, Zen_US
dc.creatorZheng, Yen_US
dc.creatorLeung, ASLen_US
dc.creatorYan, SCen_US
dc.creatorSo, PKen_US
dc.creatorLeung, YCen_US
dc.creatorWong, WLen_US
dc.creatorWong, KYen_US
dc.date.accessioned2021-06-02T01:33:31Z-
dc.date.available2021-06-02T01:33:31Z-
dc.identifier.urihttp://hdl.handle.net/10397/90262-
dc.language.isoenen_US
dc.publisherRoyal Society of Chemistryen_US
dc.rights© 2021 The Author(s).en_US
dc.rightsThis article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence (https://creativecommons.org/licenses/by-nc/3.0/)en_US
dc.rightsThe following publication Wang, Y., Liang, Z., Zheng, Y., Leung, A. S. L., Yan, S. C., So, P. K., ... & Wong, K. Y. (2021). Rational structural modification of the isatin scaffold to develop new and potent antimicrobial agents targeting bacterial peptidoglycan glycosyltransferase. RSC Advances, 11(29), 18122-18130 is available at https://doi.org/10.1039/d1ra02119ben_US
dc.titleRational structural modification of the isatin scaffold to develop new and potent antimicrobial agents targeting bacterial peptidoglycan glycosyltransferaseen_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.spage18122en_US
dc.identifier.epage18130en_US
dc.identifier.volume11en_US
dc.identifier.issue29en_US
dc.identifier.doi10.1039/d1ra02119ben_US
dcterms.abstractA series of isatin derivatives bearing three different substituent groups at the N-1, C-3 and C-5 positions of the isatin scaffold were systematically designed and synthesized to study the structure–activity relationship of their inhibition of bacterial peptidoglycan glycosyltransferase (PGT) activity and antimicrobial susceptibility against S. aureus, E. coli and methicillin-resistant Staphylococcus aureus (MRSA (BAA41)) strains. The substituents at these sites are pointing towards three different directions from the isatin scaffold to interact with the amino acid residues in the binding pocket of PGT. Comparative studies of their structure–activity relationship allow us to gain better understanding of the direction of the substituents that contribute critical interactions leading to inhibition activity against the bacterial enzyme. Our results indicate that the modification of these sites is able to maximize the antimicrobial potency and inhibitory action against the bacterial enzyme. Two compounds show good antimicrobial potency (MIC = 3 μg mL−1 against S. aureus and MRSA; 12–24 μg mL−1 against E. coli). Results of the inhibition study against the bacterial enzyme (E. coli PBP 1b) reveal that some compounds are able to achieve excellent in vitro inhibitions of bacterial enzymatic activity (up to 100%). The best half maximal inhibitory concentration (IC50) observed among the new compounds is 8.9 μM.en_US
dcterms.accessRightsopen accessen_US
dcterms.bibliographicCitationRSC advances, 2021, v. 11, no. 29, p. 18122-18130en_US
dcterms.isPartOfRSC advancesen_US
dcterms.issued2021-
dc.identifier.scopus2-s2.0-85106432341-
dc.identifier.eissn2046-2069en_US
dc.description.validate202106 bcvcen_US
dc.description.oaVersion of Recorden_US
dc.identifier.FolderNumbera0896-n01-
dc.identifier.SubFormID2102-
dc.description.fundingSourceRGCen_US
dc.description.fundingTextPolyU 153338/16Pen_US
dc.description.pubStatusPublisheden_US
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