alexa Peptidomimetics Based Inhibitor Design for HIV 1 gp120 Attachment Protein
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Peptidomimetics Based Inhibitor Design for HIV 1 gp120 Attachment Protein

Umashankar Vetrivel1*, Priya Sankar2, Naveen kumar Nagarajan2, Gurunathan Subramanian1

1Department of Bioinformatics, SRM University, Ramapuram Campus, Chennai, India

2Deparment of Bioinformatics, University of Madras, Chennai, India

*Corresponding Author:
Dr. Umashankar Vetr ivel
Department of Bioinformatics, SRM University
Ramapuram Campus, Chennai, India
E-mail: [email protected]

Received Date: October 29, 2009; Accepted Date: November 25, 2009; Published Date: November 25, 2009

Citation: Vetrivel U, Sankar P, Nagarajan NK, Subramanian G (2009) Peptidomimetics Based Inhibitor Design for HIV – 1 gp120 Attachment Protein. J Proteomics Bioinform 2: 481-484. doi: 10.4172/jpb.1000109

Copyright: © 2009 Vetrivel U, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.



Peptidomimetics is a novel drug designing strategy in which an Insilico inhibitor is designed by mimicking the framework of a short peptide. Novel drug design str ate- gies shall only pave way for developing unique and safer anti-HIV drugs. In the present study, we propose a Peptidomimetics based gp120 attachment inhibitor. I n human biological system, HIV-1 interacts with CD4 r e- ceptor of the host via its surface glycoprotein gp1 20 es- tablishing initial attachment. This protein–protein inter- action interface forms the base to derive an inhibi tor mim- icking backbone of the receptor. The mimicked inhib itor derived in this study is based on the insilico interactions of soluble CD4 (SCD4) (precursor of CD4) with gp120 . The molecular interactions of SCD4 with gp120 were iden- tified by MEDock software. Furthermore, the interac ting interface was analyzed manually for topology, and t he backbone of the ligand molecule was sketched based on it with chemsketch. Moreover, the sketched ligand was op- timized and was docked with gp120 using Argus lab. Dock- ing results show six hydrogen bonds formation betwe en the ligand and binding interface of gp120. The liga nd was also found to be fit with good druggable character, as per Lipinski’s rule of five. Hence, this work addresses the drug likeness of the peptidomimetic ligand proposed.


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