Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6719
Title: Targeting clinically-relevant metallo-β-lactamases: from high-throughput docking to broad-spectrum inhibitors
Authors: Brindisi, Margherita 
Brogi, Simone
Giovani, Simone
Gemma, Sandra 
Lamponi, Stefania 
DE LUCA, Filomena
Novellino, Ettore
Campiani, Giuseppe 
Docquier, JEAN DENIS
Butini, Stefania 
Keywords: Antibiotic resistance; docking; metallo-β-lactamase
Issue Date: 2016
Project: None 
Journal: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
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.
Description: 
88778
URI: http://hdl.handle.net/20.500.12779/6719
ISSN: 1475-6366
DOI: 10.3109/14756366.2016.1172575
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