Title

Authors

Affiliation

¹Department of Pharmacology and Therapeutics, King George's Medical University, (Erstwhile C.S.M. Medical University), Lucknow- - 226 003, India; ²Institute of Genetics and Hospital for Genetic Diseases, Osmania University, Hyderabad - 500 016, India; ³In silico Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452 010, India

Email

sinha.chanda17@gmail.com; drskhattri@gmail.com; *Corresponding authors

Article Type

Hypothesis

Date

Received September 10, 2014; Accepted September 23, 2014; Published October 30, 2014

The HIV-1 protein Vif is essential for in vivo viral replication that targets the human DNA-editing enzyme, APOBEC3G (A3G), which inhibits replication of retroviruses. The Vif-A3G interactions are believed to be important targets for antiviral drug development. Since the interactions of A3G and Vif evade the ubiquitination pathways in human host, the viral replication precedes which otherwise spreads infection. In this study, two potent Vif inhibitors RN 18 and VEC5 have been evaluated for their inhibitory potential employing ligand receptor and protein-protein interactions studies. VEC 5 showed better interaction with Vif than RN18. Predicted data show that VEC5 bound Vif and RN18 bound Vif showed diminished interaction to A3G compared to inhibitor unbound Vif. However, this should be further validated using in vitro studies. 

Keywords

Vif, Vif inhibitors, RN18, VEC5, Protein – Protein docking, VIF-A3G interactions.

Citation

Sinha et al.   Bioinformation 10(10): 611-616 (2014)
 

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.