Language
English
Publication Date
1-11-2024
Journal
Journal of Medicinal Chemistry
DOI
10.1021/acs.jmedchem.3c01834
PMID
38117688
PMCID
PMC11489902
PubMedCentral® Posted Date
1-11-2025
PubMedCentral® Full Text Version
Author MSS
Abstract
β-Lactamase enzymes hydrolyze and thereby provide bacterial resistance to the important β-lactam class of antibiotics. The OXA-48 and NDM-1 β-lactamases cause resistance to the last-resort β-lactams, carbapenems, leading to a serious public health threat. Here, we utilized DNA-encoded chemical library (DECL) technology to discover novel β-lactamase inhibitors. We exploited the β-lactamase enzyme-substrate binding interactions and created a DECL targeting the carboxylate-binding pocket present in all β-lactamases. A library of 10
Keywords
beta-Lactamase Inhibitors, Anti-Bacterial Agents, beta-Lactamases, beta-Lactams, Penicillins, DNA, Microbial Sensitivity Tests
Published Open-Access
yes
Recommended Citation
Park, Suhyeorn; Fan, Jiayi; Chamakuri, Srinivas; et al., "Exploiting the Carboxylate-Binding Pocket of β-Lactamase Enzymes Using a Focused DNA-Encoded Chemical Library" (2024). Faculty and Staff Publications. 2404.
https://digitalcommons.library.tmc.edu/baylor_docs/2404
Graphical Abstract
Included in
Biological Phenomena, Cell Phenomena, and Immunity Commons, Biomedical Informatics Commons, Genetics and Genomics Commons, Medical Genetics Commons, Medical Molecular Biology Commons, Medical Specialties Commons