A Comparative Study of Various Synthesis and Activities of Inhibitors of Metallo-Β-Lactamase: A Review | Original Article
Resistance to b-lactam antibiotics is mediated primarily by enzymes that hydrolytically inactivate the drugs by one of two mechanisms: serine nucleophilic attack or metaldependent activation of a water molecule. Serine b-lactamases are countered in the clinic by several codrugs that inhibit these enzymes, thereby rescuing antibiotic action. The synthesis enabled confirmation of the stereochemical configuration of the compound and offers a route for the synthesis of derivatives in the future of particular concern is the metallo-β-lactamases (MBLs), which are a family of di-zinc containing metalloenzymes capable of hydrolyzing a very broad range of common β-lactam antibiotics. MBLs are not inhibited by clavulanic acid, a drug commonly co-administered with β-lactam antibiotics as an inhibitor of other serine β -lactamases. The aim of the research is to design, dock (computer calculation of an optimum fit of a molecule into an enzyme active site to find a possible docking geometry and energy), synthesize and assay of potent and selective inhibitors of MBLs (IMP-1).