Title

Curcumin binds in silico to anti-cancer drug target enzyme MMP-3 (human stromelysin-1) with affinity comparable to two known inhibitors of the enzyme

Authors

Affiliation

¹College of Applied Medical Sciences, Jazan University, Jazan, KSA; ²Index Medical College Hospital and Research Center, Indore, India

Email

akbidwai@yahoo.com;  *Corresponding author

Article Type

Hypothesis

Date

Received July 22, 2015; Accepted July 29, 2015; Published August 31, 2015

In silico interaction of curcumin with the enzyme MMP-3 (human stromelysin-1) was studied by molecular docking using AutoDock 4.2 as the docking software application. AutoDock 4.2 software serves as a valid and acceptable docking application to study the interactions of small compounds with proteins. Interactions of curcumin with MMP-3 were compared to those of two known inhibitors of the enzyme, PBSA and MPPT. The calculated free energy of binding (∆G binding) shows that curcumin binds with affinity comparable to or better than the two known inhibitors. Binding interactions of curcumin with active site residues of the enzyme are also predicted. Curcumin appears to bind in an extendended conformation making extensive VDW contacts in the active site of the enzyme. Hydrogen bonding and pi-pi  interactions with key active site residues is also observed. Thus, curcumin can be considered as a good lead compound in the development of new inhibitors of MMP-3 which is a potential target of anti-cancer drugs. The results of these studies can serve as a starting point for further computational and experimental studies.

Keywords

curcumin, docking, AutoDock, MMP-3, drug design

Citation

Jerah et al. Bioinformation 11(8): 387-392 (2015)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.