Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases

The urgent demand for effective countermeasures against metallo-β-lactamases (MBLs) necessitates development of novel metallo-β-lactamase inhibitors (MBLIs). This study is dedicated to identifying critical chemical moieties within previously developed MBLIs, and critical MBLs should serve as the tar...

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Main Authors: Jung Hun Lee, Sang-Gyu Kim, Kyung-Min Jang, Kyoungmin Shin, Hyeonku Jin, Dae-Wi Kim, Byeong Chul Jeong, Sang Hee Lee
Format: Article
Language:English
Published: Taylor & Francis Group 2024-12-01
Series:Journal of Enzyme Inhibition and Medicinal Chemistry
Subjects:
Online Access:https://www.tandfonline.com/doi/10.1080/14756366.2024.2318830
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author Jung Hun Lee
Sang-Gyu Kim
Kyung-Min Jang
Kyoungmin Shin
Hyeonku Jin
Dae-Wi Kim
Byeong Chul Jeong
Sang Hee Lee
author_facet Jung Hun Lee
Sang-Gyu Kim
Kyung-Min Jang
Kyoungmin Shin
Hyeonku Jin
Dae-Wi Kim
Byeong Chul Jeong
Sang Hee Lee
author_sort Jung Hun Lee
collection DOAJ
description The urgent demand for effective countermeasures against metallo-β-lactamases (MBLs) necessitates development of novel metallo-β-lactamase inhibitors (MBLIs). This study is dedicated to identifying critical chemical moieties within previously developed MBLIs, and critical MBLs should serve as the target in MBLI evaluations. Using the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA), a systematic literature analysis was conducted, and the NCBI RefSeq genome database was exploited to access the abundance profile and taxonomic distribution of MBLs and their variant types. Through the implementation of two distinct systematic approaches, we elucidated critical chemical moieties of MBLIs, providing pivotal information for rational drug design. We also prioritised MBLs and their variant types, highlighting the imperative need for comprehensive testing to ensure the potency and efficacy of the newly developed MBLIs. This approach contributes valuable information to advance the field of antimicrobial drug discovery.
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spelling doaj.art-c847db5836704a938c7f1d43908ced9e2024-12-26T09:30:44ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742024-12-0139110.1080/14756366.2024.2318830Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamasesJung Hun Lee0Sang-Gyu Kim1Kyung-Min Jang2Kyoungmin Shin3Hyeonku Jin4Dae-Wi Kim5Byeong Chul Jeong6Sang Hee Lee7National Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaDivision of Life Sciences, Jeonbuk National University, Jeonju, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaDivision of Life Sciences, Jeonbuk National University, Jeonju, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaThe urgent demand for effective countermeasures against metallo-β-lactamases (MBLs) necessitates development of novel metallo-β-lactamase inhibitors (MBLIs). This study is dedicated to identifying critical chemical moieties within previously developed MBLIs, and critical MBLs should serve as the target in MBLI evaluations. Using the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA), a systematic literature analysis was conducted, and the NCBI RefSeq genome database was exploited to access the abundance profile and taxonomic distribution of MBLs and their variant types. Through the implementation of two distinct systematic approaches, we elucidated critical chemical moieties of MBLIs, providing pivotal information for rational drug design. We also prioritised MBLs and their variant types, highlighting the imperative need for comprehensive testing to ensure the potency and efficacy of the newly developed MBLIs. This approach contributes valuable information to advance the field of antimicrobial drug discovery.https://www.tandfonline.com/doi/10.1080/14756366.2024.2318830Metallo-β-lactamase inhibitorchemical moietymetallo-β-lactamase variant type
spellingShingle Jung Hun Lee
Sang-Gyu Kim
Kyung-Min Jang
Kyoungmin Shin
Hyeonku Jin
Dae-Wi Kim
Byeong Chul Jeong
Sang Hee Lee
Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
Journal of Enzyme Inhibition and Medicinal Chemistry
Metallo-β-lactamase inhibitor
chemical moiety
metallo-β-lactamase variant type
title Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
title_full Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
title_fullStr Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
title_full_unstemmed Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
title_short Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
title_sort elucidation of critical chemical moieties of metallo β lactamase inhibitors and prioritisation of target metallo β lactamases
topic Metallo-β-lactamase inhibitor
chemical moiety
metallo-β-lactamase variant type
url https://www.tandfonline.com/doi/10.1080/14756366.2024.2318830
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