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: vumashankar@gmail.com |
|
| Received October 29, 2009; Accepted November 25, 2009; Published
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. |
| Abstract |
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 strategies
shall only pave way for developing unique and safer
anti-HIV drugs. In the present study, we propose a
Peptidomimetics based gp120 attachment inhibitor. In
human biological system, HIV-1 interacts with CD4 receptor
of the host via its surface glycoprotein gp120 establishing
initial attachment. This protein–protein interaction
interface forms the base to derive an inhibitor mimicking
backbone of the receptor. The mimicked inhibitor
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 identified
by MEDock software. Furthermore, the interacting
interface was analyzed manually for topology, and the
backbone of the ligand molecule was sketched based on it
with chemsketch. Moreover, the sketched ligand was optimized
and was docked with gp120 using Argus lab. Docking
results show six hydrogen bonds formation between
the ligand and binding interface of gp120. The ligand 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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