Abstract
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. Key words: Molecular Docking, Thiazolidinone, HIV, NNRTI.
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