S. Gurudeeban
Matrix metalloproteinase (MMP) also known as matrixins, play an important role in wound healing, tissue engineering and embryogenesis. The action of MMP inhibited by several endogenous tissue inhibitors but the pathological condition requires exogenous inhibitor from natural or synthetic source. Therefore, the present study is aimed to evaluate the inhibitory effect of rutin on metalloproteinase. The active sites of target proteins were predicted through 3DLignadsite. Based on the Lamarckian genetic algorithm, the energy minimized rutin was docked with MMP2, MMP3, MMP8 and MMP12 using Autodock 4.2. The result indicates the interaction of rutin exhibited binding free energy of MMP2 as -10.19kcalmol-1 on GLU, MMP8 as -8.83kcalmol-1 on LEU, THR, MMP3 as -8.83kcalmol-1 on ALA, HIS and MMP12 as -6.08kcalmol-1 CYS and HIS57 residues. We conclude rutin as an effective matrix metalloproteinase inhibitor. Further studies will confirm the usage of rutin as a matrix metalloproteinase inhibitor.
