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Comparative Study of Various Non-Nucleoside Reverse Transcriptase Inhibitors on Different Reverse Transcriptase Enzyme

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  1. 1Department of Pharmaceutical chemistry, All India Shri Shivaji Memorial Society’s College of Pharmacy, Kennedy, Pune, INDIA.

CORRESPONDENCE

Shital Manoj Patil

Department of Pharmaceutical chemistry, All India Shri Shivaji Memorial Society’s College of Pharmacy, Kennedy, Pune, INDIA.

shital_patil@aissmscop.com

Received: 23-08-2017; Accepted: 09-10-2017.

Volume 51, Issue 4s (Supplement) · pp. s722-s728 · 2017 · DOI: 10.5530/ijper.51.4s.104

ABSTRACT

Context: Acquired immunodeficiency Syndrome (AIDS) is caused by Human immunodeficiency virus type 1 (HIV-1). 4-Thiazolidone nulecus is the target pharmacophore which have diverse biological activities including anti HIV activity.Aim: To study binding behavior of thiazolidinone derivatives on four different crystal structures of HIV- 1RT.Material and Method: Binding pattern of some thiazolidinone derivatives was gauged by molecular docking studies on four different receptors bearing PDB code 1ZD1, 1RT2, 1KLM, 1FKP of HIV–RT enzyme using V. Life MDS software. Result and Discussion: The studies revealed hydrogen bonds, hydrophobic interaction and pi-pi interactions playing significant role in binding of the molecules to the enzyme.Conclusion: Interactions, binding energy and dock score of molecule 6 was comparable with the standard drugs.

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    Patil, S. M., Asgaonkar, K. D., Chitre, T. S., Kinikar, A., Kharat, C., Bhoirekar, V., Athavale, M., & Katkar, M. (2017). Comparative Study of Various Non-Nucleoside Reverse Transcriptase Inhibitors on Different Reverse Transcriptase Enzyme. Indian Journal of Pharmaceutical Education and Research, 51(4s), s722-s728. https://doi.org/10.5530/ijper.51.4s.104

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    © 2017 Author(s)

    This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited. CC BY 4.0