Title

Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors

Authors

Suby T Baby1*, Shailendra Sharma1, Sreenivas Enaganti2, Roby P. Cherian3

Affiliation

1Faculty of Pharmaceutical Sciences, Jodhpur National University, Jodhpur, Rajasthan 342003, India; 2Bioinformatics division, Averin biotech, Nallakunta, Hyderabad, Telangana 500044, India; 3Jazan University, P.O.Box 114, Jazan 45142, Kingdom of Saudi Arabia.

Email

Suby T Baby - Email: subysusanbaby@yahoo.com; *Corresponding author

Article Type

Hypothesis

Date

Received April 9, 2016; Revised May 15, 2016; Accepted May 16, 2016; Published June 15, 2016

Heat Shock Protein 90 was a key molecular chaperone involved in the proteome stability maintenance and its interference in many signaling networks associated with cancer progression, makes it of an important target for cancer therapeutics. The present study aimed to identify potential lead molecule among the selected heterocyclic compounds against Human Hsp90 (PDB: 1YET) through docking using GOLD 3.1 and pharmacophore studies using Discovery studio 2.1. On the basis of the GOLD Fitness scores, the compounds Q1G and T21 showed better binding affinity. Further the analyzed structure pharmacophore results are in consistence with the docking results indicating that both these compounds show antagonistic activity towards HSP90 respectively.

Keywords

molecular chaperone, Heat Shock Protein 90, docking, pharmacophore, cancer, proteome

Citation

Baby et al. Bioinformation 12(3): 149-155 (2016)

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.