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
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
收藏
页码:2755 / 2758
页数:4
相关论文
共 50 条
  • [41] Hydrolysis of Organophosphate Esters: Phosphotriesterase Activity of Metallo-β-lactamase and Its Functional Mimics
    Tamilselvi, A.
    Mugesh, Govindasamy
    CHEMISTRY-A EUROPEAN JOURNAL, 2010, 16 (29) : 8878 - 8886
  • [42] New Delhi metallo-β-lactamase: a cautionary tale
    Muir, A.
    Weinbren, M. J.
    JOURNAL OF HOSPITAL INFECTION, 2010, 75 (03) : 239 - 240
  • [43] Emergence of New Delhi Metallo-β-Lactamase, Austria
    Zarfel, Gernot
    Hoenigl, Martin
    Leitner, Eva
    Salzer, Helmut J. F.
    Feierl, Gebhard
    Masoud, Lilian
    Valentin, Thomas
    Krause, Robert
    Grisold, Andrea J.
    EMERGING INFECTIOUS DISEASES, 2011, 17 (01) : 129 - 130
  • [44] Novel DNA and RNA inhibitors of metallo-β-lactamase
    Shaw, RW
    Kim, SK
    Kim, KM
    Cottenoir, M
    Sims, CL
    Peng, J
    Fisher, AJ
    FASEB JOURNAL, 2006, 20 (05): : A898 - A898
  • [45] Polypyridine ligands as potential metallo-β-lactamase inhibitors
    La Piana, Luana
    Viaggi, Valentina
    Principe, Luigi
    Di Bella, Stefano
    Luzzaro, Francesco
    Viale, Maurizio
    Bertola, Nadia
    Vecchio, Graziella
    JOURNAL OF INORGANIC BIOCHEMISTRY, 2021, 215
  • [46] Human metallo-β-lactamase enzymes degrade penicillin
    Seydina M. Diene
    Lucile Pinault
    Vivek Keshri
    Nicholas Armstrong
    Saber Khelaifia
    Eric Chabrière
    Gustavo Caetano-Anolles
    Philippe Colson
    Bernard La Scola
    Jean-Marc Rolain
    Pierre Pontarotti
    Didier Raoult
    Scientific Reports, 9
  • [47] Inhibitors of the FEZ-1 metallo-β-lactamase
    Lienard, Benoit M. R.
    Horsfall, Louise E.
    Galleni, Moreno
    Frere, Jean-Marie
    Schofield, Christopher J.
    BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2007, 17 (04) : 964 - 968
  • [48] Targeting metallo-β-lactamase enzymes in antibiotic resistance
    King, Dustin T.
    Strynadka, Natalie C. J.
    FUTURE MEDICINAL CHEMISTRY, 2013, 5 (11) : 1243 - 1263
  • [49] Structural basis of metallo-β-lactamase resistance to taniborbactam
    Drusin, Salvador I.
    Le Terrier, Christophe
    Poirel, Laurent
    Bonomo, Robert A.
    Vila, Alejandro J.
    Moreno, Diego M.
    ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2024, 68 (01)
  • [50] On the mechanism of the metallo-β-lactamase from Bacteroides fragilis
    Wang, ZG
    Fast, W
    Benkovic, SJ
    BIOCHEMISTRY, 1999, 38 (31) : 10013 - 10023