Title |
Evaluation of novel Saquinavir analogs for resistance mutation compatibility and potential as an HIV-Protease inhibitor drug
|
Authors |
Amit Jayaswal1, Ankita Mishra1, Hirdyesh Mishra2 & Kavita Shah3* |
Affiliation |
1Bioinformatics Department, Mahila Mahavidyalaya, Banaras Hindu University, Varanasi 221005, India; 2Physics Department, MMV, Banaras Hindu University, Varanasi 221005, India; 4Institute of Environment and Sustainable Development, Banaras Hindu University, Varanasi 221005, India
|
|
kavitashah@bhu.ac.in; *Corresponding author
|
Article Type |
Hypothesis |
Date |
Received March 26, 2014; Accepted April 03, 2014; Published April 23, 2014
|
Abstract |
A fundamental issue related to therapy of HIV-1 infection is the emergence of viral mutations which severely limits the long term efficiency of the HIV-protease (HIV-PR) inhibitors. Development of new drugs is therefore continuously needed. Chemoinformatics enables to design and discover novel molecules analogous to established drugs using computational tools and databases. Saquinavir, an anti-HIV Protease drug is administered for HIV therapy. In this work chemoinformatics tools were used to design structural analogs of Saquinavir as ligand and molecular dockings at AutoDock were performed to identify potential HIV-PR inhibitors. The analogs S1 and S2 when docked with HIV-PR had binding energies of -4.08 and -3.07 kcal/mol respectively which were similar to that for Saquinavir. The molecular docking studies revealed that the changes at N2 of Saquinavir to obtain newly designed analogs S1 (having N2 benzoyl group at N1) and S2 (having 3-oxo-3phenyl propanyl group at N2) were able to dock with HIV-PR with similar affinity as that of Saquinavir. Docking studies and computationally derived pharmacodynamic and pharmacokinetic properties’ comparisons at ACD/I-lab establish that analog S2 has more potential to evade the problem of drug resistance mutation against HIV-1 PR subtype-A. S2 can be further developed and tested clinically as a real alternative drug for HIV-1 PR across the clades in future.
|
Keywords |
HIV protease, Drug design, Drug resistance, Lead identification, Molecular Docking, Pharmacokinetics, Saquinavir.
|
Citation |
Jayaswal et al.
Bioinformation 10(4): 227-232 (2014) |
Edited by |
P Kangueane
|
ISSN |
0973-2063
|
Publisher |
|
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. |