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Title: Cationic glycosylated block co-β-peptide acts on the cell wall of Gram-positive bacteria as anti-biofilm agents
Authors: Zhang, Kaixi
Raju, Cheerlavancha
Zhong, Wenbin
Pethe, Kevin
Gründling, Angelika
Chan-Park, Mary B.
Keywords: Engineering::Chemical engineering::Polymers and polymer manufacture
Issue Date: 2021
Source: Zhang, K., Raju, C., Zhong, W., Pethe, K., Gründling, A. & Chan-Park, M. B. (2021). Cationic glycosylated block co-β-peptide acts on the cell wall of Gram-positive bacteria as anti-biofilm agents. ACS Applied Bio Materials, 4(5), 3749-3761.
Project: MOE2013-T3-1-002
Journal: ACS Applied Bio Materials
Abstract: Antimicrobial resistance is a global threat. In addition to the emergence of resistance to last resort drugs, bacteria escape antibiotics killing by forming complex biofilms. Strategies to tackle antibiotic resistance as well as biofilms are urgently needed. Wall teichoic acid (WTA), a generic anionic glycopolymer present on the cell surface of many Gram-positive bacteria, has been proposed as a possible therapeutic target, but its druggability remains to be demonstrated. Here we report a cationic glycosylated block co-β-peptide that binds to WTA. By doing so, the co-β-peptide not only inhibits biofilm formation, it also disperses preformed biofilms in several Gram-positive bacteria and resensitizes methicillin-resistant Staphylococcus aureus to oxacillin. The cationic block of the co-β-peptide physically interacts with the anionic WTA within the cell envelope, whereas the glycosylated block forms a nonfouling corona around the bacteria. This reduces physical interaction between bacteria-substrate and bacteria-biofilm matrix, leading to biofilm inhibition and dispersal. The WTA-targeting co-β-peptide is a promising lead for the future development of broad-spectrum anti-biofilm strategies against Gram-positive bacteria.
ISSN: 2576-6422
DOI: 10.1021/acsabm.0c01241
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Applied Bio Materials, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Fulltext Permission: embargo_20220524
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles
SBS Journal Articles
SCBE Journal Articles

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