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

[21] Halogen-Substituted Triazolethioacetamides as a Potent Skeleton for the Development of Metallo-β-Lactamase Inhibitors
Zhang, Yilin
Yan, Yong
Liang, Lufan
Feng, Jie
Wang, Xuejun
Li, Li
Yang, Kewu
MOLECULES, 2019, 24 (06):
[22] In Vitro Potentiation of Carbapenems with ME1071, a Novel Metallo-β-Lactamase Inhibitor, against Metallo-β-Lactamase-Producing Pseudomonas aeruginosa Clinical Isolates
Ishii, Yoshikazu
Eto, Maki
Mano, Yoko
Tateda, Kazuhiro
Yamaguchi, Keizo
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2010, 54 (09) : 3625 - 3629
[23] Molecular Mechanisms of Substrate Recognition and Specificity of New Delhi Metallo-β-Lactamase
Chiou, Jiachi
Leung, Thomas Yun-Chung
Chen, Sheng
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2014, 58 (09) : 5372 - 5378
[24] Epidemiology of extended-spectrum β-lactamase/metallo-β-lactamase
Migliavacca, R.
Balzaretti, M.
Nucleo, E.
D'Andrea, M. M.
Mugnaioli, C.
Spalla, M.
Giani, T.
Rossolini, G. M.
Pagani, L.
INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS, 2007, 29 : S90 - S90
[25] New Delhi metallo-β-lactamase in Jamaica
Thoms-Rodriguez, Camille-Ann
Mazzulli, Tony
Christian, Nicole
Willey, Barbara M.
Boyd, David A.
Mataseje, Laura F.
Mulvey, Michael R.
Christie, Celia D. C.
Nicholson, Alison M.
JOURNAL OF INFECTION IN DEVELOPING COUNTRIES, 2016, 10 (02): : 183 - 187
[26] Metallo-β-lactamase: Inhibitors and reporter substrates
Fast, Walter
Sutton, Larry D.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2013, 1834 (08): : 1648 - 1659
[27] New Delhi metallo-β-lactamase 1
de Costa, Ayesha
Mavalankar, Dileep
LANCET INFECTIOUS DISEASES, 2010, 10 (11): : 752 - 752
[28] Captopril analogues as metallo-β-lactamase inhibitors
Yusof, Yusralina
Tan, Daniel T. C.
Arjomandi, Omid Khalili
Schenk, Gerhard
McGeary, Ross P.
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2016, 26 (06) : 1589 - 1593
[29] Computational studies of a metallo-β-lactamase.
Salsbury, FR
Brooks, CL
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2001, 221 : U413 - U413
[30] Metallo-β-Lactamase Expression Confers an Advantage to Pseudomonas aeruginosa Isolates Compared with Other β-Lactam Resistance Mechanisms, Favoring the Prevalence of Metallo-β-Lactamase Producers in a Clinical Environment
Corich, Lucia
Dolzani, Lucilla
Tonin, Enrico A.
Vitali, Luca A.
Lagatolla, Cristina
MICROBIAL DRUG RESISTANCE, 2010, 16 (03) : 223 - 230

← 1 2 3 4 5 →