@article{Zhang:2021:10.1021/acsabm.0c01241,
author = {Zhang, K and Raju, C and Zhong, W and Pethe, K and Gründling, A and Chan-Park, MB},
doi = {10.1021/acsabm.0c01241},
journal = {ACS Applied Bio Materials},
pages = {3749--3761},
title = {Cationic glycosylated block Co-β-peptide acts on the cell wall of gram-positive bacteria as anti-biofilm agents},
url = {http://dx.doi.org/10.1021/acsabm.0c01241},
volume = {4},
year = {2021}
}

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TY  - JOUR
AB  - 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.
AU  - Zhang,K
AU  - Raju,C
AU  - Zhong,W
AU  - Pethe,K
AU  - Gründling,A
AU  - Chan-Park,MB
DO  - 10.1021/acsabm.0c01241
EP  - 3761
PY  - 2021///
SN  - 2576-6422
SP  - 3749
TI  - Cationic glycosylated block Co-β-peptide acts on the cell wall of gram-positive bacteria as anti-biofilm agents
T2  - ACS Applied Bio Materials
UR  - http://dx.doi.org/10.1021/acsabm.0c01241
UR  - https://pubs.acs.org/doi/10.1021/acsabm.0c01241
UR  - http://hdl.handle.net/10044/1/86951
VL  - 4
ER  - 

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