Disulfiram as a potent metallo-β-lactamase inhibitor with dual functional mechanisms

被引：36

作者：

Chen, Cheng ^{[1
]}

Yang, Ke-Wu ^{[1
]}

Wu, Lin-Yu ^{[2
]}

Li, Jia-Qi ^{[1
]}

Sun, Le-Yun ^{[1
]}

机构：

[1] Northwest Univ, Coll Chem & Mat Sci, Innovat Lab Chem Biol, Minist Educ,Key Lab Synthet & Nat Funct Mol Chem, Xian 710127, Peoples R China

[2] Northwest Normal Univ, Coll Chem & Chem Engn, Lanzhou 730070, Gansu, Peoples R China

来源：

CHEMICAL COMMUNICATIONS | 2020年 / 56卷 / 18期

基金：

中国国家自然科学基金;

关键词：

Chemical bonds - Zinc compounds;

D O I：

10.1039/c9cc09074f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We report a promising NDM-1 inhibitor, disulfiram, which can covalently bind to NDM-1 by forming an S-S bond with the Cys208 residue. Its copper-containing metabolite in vivo, Cu(DTC)(2), also inactivated NDM-1 through oxidizing the Zn(ii) thiolate site of the enzyme, therefore exhibiting dual functional inhibitory potential against B1 and B2 subclass M beta Ls.

引用

页码：2755 / 2758

页数：4

共 50 条

[31] Optimized Synthesis of Indole Carboxylate Metallo-β-Lactamase Inhibitor EBL-3183
Baran, Andrei
Kuzmins, Jevgenijs
Kuznecovs, Jevgenijs
Farley, Alistair J. M.
Panduwawala, Tharindi
Parkova, Anete
Donets, Pavel A.
Brem, Jurgen
Suna, Edgars
Schofield, Christopher J.
Shubin, Kirill
ORGANIC PROCESS RESEARCH & DEVELOPMENT, 2023, 27 (04) : 692 - 706
[32] Chemoenzymatic asymmetric synthesis of the metallo-β-lactamase inhibitor aspergillomarasmine A and related aminocarboxylic acids
Haigen Fu
Jielin Zhang
Mohammad Saifuddin
Gea Cruiming
Pieter G. Tepper
Gerrit J. Poelarends
Nature Catalysis, 2018, 1 : 186 - 191
[33] Chemoenzymatic asymmetric synthesis of the metallo-β-lactamase inhibitor aspergillomarasmine A and related aminocarboxylic acids
Fu, Haigen
Zhang, Jielin
Saifuddin, Mohammad
Cruiming, Gea
Tepper, Pieter G.
Poelarends, Gerrit J.
NATURE CATALYSIS, 2018, 1 (03): : 186 - 191
[34] Arginine-containing peptides as potent inhibitors of VIM-2 metallo-β-lactamase
Rotondo, Caitlyn M.
Marrone, Laura
Goodfellow, Valerie J.
Ghavami, Ahmad
Labbe, Genevieve
Spencer, James
Dmitrienko, Gary I.
Siemann, Stefan
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2015, 1850 (11): : 2228 - 2238
[35] meta-Substituted benzenesulfonamide: a potent scaffold for the development of metallo-β-lactamase ImiS inhibitors
Liu, Ya
Chen, Cheng
Sun, Le-Yun
Gao, Han
Zhen, Jian-Bin
Yang, Ke-Wu
RSC MEDICINAL CHEMISTRY, 2020, 11 (02): : 259 - 267
[36] Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-β-lactamase
Toney, JH
Fitzgerald, PMD
Grover-Sharma, N
Olson, SH
May, WJ
Sundelof, JG
Vanderwall, DE
Cleary, KA
Grant, SK
Wu, JK
Kozarich, JW
Pompliano, DL
Hammond, GG
CHEMISTRY & BIOLOGY, 1998, 5 (04): : 185 - 196
[37] Thiohydroxypyridinones as a scaffold for the development of potent New Delhi metallo-β-lactamase-1 inhibitors
Adamek, Rebecca
Credille, Cy
Thomas, Pei
Fast, Walter
Cohen, Seth
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2017, 254
[38] 3-Bromopyruvate as a potent covalently reversible inhibitor of New Delhi metallo-β-lactamase-1 (NDM-1)
Kang, Peng-Wei
Su, Jian-Peng
Sun, Le-Yun
Gao, Han
Yang, Ke-Wu
EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES, 2020, 142
[39] Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases
Lee, Jung Hun
Kim, Sang-Gyu
Jang, Kyung-Min
Shin, Kyoungmin
Jin, Hyeonku
Kim, Dae-Wi
Jeong, Byeong Chul
Lee, Sang Hee
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2024, 39 (01)
[40] Diversity and Proliferation of Metallo-β-Lactamases: a Clarion Call for Clinically Effective Metallo-β-Lactamase Inhibitors
Somboro, Anou M.
Sekyere, John Osei
Amoako, Daniel G.
Essack, Sabiha Y.
Bester, Linda A.
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2018, 84 (18)

← 1 2 3 4 5 →