| Literature DB >> 27121013 |
Margherita Brindisi1,2, Simone Brogi1,2, Simone Giovani1,2, Sandra Gemma1,2, Stefania Lamponi1,2, Filomena De Luca3, Ettore Novellino4, Giuseppe Campiani1,2, Jean-Denis Docquier3, Stefania Butini1,2.
Abstract
Metallo-β-lactamases (MBLs) represent one of the most important and widespread mechanisms of resistance to β-lactam antibiotics (including the life-saving carbapenems), against which no clinically useful inhibitors are currently available. We report herein a structure-based high-throughput docking (HTD) campaign on three clinically-relevant acquired MBLs (IMP-1, NDM-1 and VIM-2). The initial hit NF1810 (1) was optimized providing the broad-spectrum inhibitor 3i, which is able to potentiate the in vitro activity of cefoxitin on a VIM-2-producing E. coli strain.Entities:
Keywords: Antibiotic resistance; docking; metallo-β-lactamase
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Year: 2016 PMID： 27121013 DOI： 10.3109/14756366.2016.1172575
Source DB: PubMed Journal: J Enzyme Inhib Med Chem ISSN： 1475-6366 Impact factor: 5.051