The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.

ABSTRACT: The increasing number of pathogens expressing metallo-β-lactamases (MBLs), and in this way achieving resistance to β-lactam antibiotics, is a significant threat to global public health. A promising strategy to treat such resistant pathogens is the co-administration of MBL inhibitors together with β-lactam antibiotics. However, an MBL inhibitor suitable for clinical use has not yet been identified. Verona integron-encoded metallo-β-lactamase 2 (VIM-2) is a widespread MBL with a broad substrate spectrum and hence is an interesting drug target for the treatment of β-lactam-resistant infections. In this study, three triazolylthioacetamides were tested as inhibitors of VIM-2. One of the tested compounds showed clear inhibition of VIM-2, with an IC₅₀ of 20 µM. The crystal structure of

SUBMITTER: Christopeit T 

PROVIDER: S-EPMC5101582 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature