Computational molecular docking and structural specificity of bipyrazoles as non-zinc chelating inhibitors of MMP-13
by G. Nirmala; YesuBabu Adimulam; P. Seetharamaiah
International Journal of Computational Biology and Drug Design (IJCBDD), Vol. 9, No. 1/2, 2016

Abstract: Matrix metalloproteinases (MMP) degrade extra cellular matrix proteins. Matrix MMPs are structurally similar, but differ in substrate specificity. A large number of MMP inhibitors have been described as zinc binding groups; however, in this paper we report computational identification of novel bipyrazoles as non-zinc chelating inhibitors of MMP-13. Molecular docking analysis performed between a set of 37 bipyrazoles vs. MMP-13 resulted in compound 26 observed with a score of −241 kcal/mol which is nearly half fold than the 456C bound ligand (−155.299 kcal/mol). The binding orientations of all bipyrazoles are geometrically similar to the co-crystallised ligand of 456C. Considering the distance (A°) between zinc atom and nearest N atom on pyrazole as well as Lipinski's rule of 5, compound 2 might act as a non-zinc chelating inhibitor.

Online publication date: Sun, 28-Feb-2016

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