Published 2021-08-27
Copyright (c) 2017
This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.
Abstract
The life-threatening infections and pandemic spread of Human Immunodeficiency virus-1 (HIV-1), the etiologic agent of AIDS, has promoted an unending scientific effort to understand and control the disease. The resultant understanding of HIV-1 life cycle has defined many different targets for potential drug intervention. HIV protease enzyme responsible for cleaving large polyprotein precursors into biologically active protein products is an important target for the treatment of AIDS. However drug resistance is a persistent problem and new protease inhibitors are needed. Tipranavir, one of the protease inhibitors most recently approved for clinical use has been shown to be potent against viruses harbouring multidrug resistance mutations such as V82A and L90M, but even this drug is shown to lose potency due to certain mutations or mutation patterns. Thus 10 derivatives of the drug Tipranavir, chemically diverse from the initial hit were generated and screened to determine their ability to interact with protease. Further analysis revealed one unique compound with high binding ability from the initial hit and its possibility for new class of protease inhibitors is discussed in this report.