Molecular docking analysis of Curcumin analogues as Matrix metalloproteinases (MMP 2 and MMP 9) inhibitors

Abstract

The present study describes molecular docking analysis of curcumin analogues as inhibitors of matrix metalloproteinase 2 (MMP 2) and matrix metalloproteinase 9 (MMP 9). Sixteen curcumin analogues were evaluated on the docking behaviour of MMP 2 and MMP 9. And investigation also carried out on their putative binding sites using Discovery Studio Version 3.1. Docking and binding free energy analysis revealed that compound 16 and compound 15 exhibited the maximum binding energy (-57.75 and -60.82 kcal/mol) with that of MMP 2 and MMP 9. Interestingly, compound 1 [2, 5-bis (2, 3-dimethoxy benzylidene) cyclopentanone] has shown to interact with His211 and His230 amino acid residue of MMP 2 and MMP 9 respectively. Thus, the results of this present study exhibited the potential of these curcumin analogues as MMP 2 and MMP 9 inhibitory agents.