Indexed In Scopus
  Scopus ID: 21100926589

HIV-1 Protease Drug-resistant Mutations and Inhibitor Binding Mechanism: A Review on Hybrid Quantum Mechanics/Molecular Mechanics Approach

Neha Kumari, Gurpreet Bamrah, Amrita Biswas and Saurabh Srivastava

Abstract

HIV-1 (Human immunodeficiency virus type one) protease (PR) is a decisive enzyme for the replication of HIV-1. It is important in the progression of acquired immunodeficiency syndrome (AIDS). The viral enzyme integrase is required for HIV-1 replication because it permits viral DNA to be integrated into the DNA of the host cell. Because of this integration process, the virus is able to develop mutations in its protease, which leads to resistance to certain inhibitors. The current study aims to provide an overview of the molecular mechanisms underlying drug resistance in HIV-1 PR, which occurs as a result of various mutations. The computational studies involving hybrid quantum mechanics (QM) and molecular mechanics (MM) methods provides accurate data regarding the dynamics of the inhibitor-protease complex. This study contributes to a deeper understanding of the inhibitor-protease complex in various mutations and shed light on potential strategies to combat drug resistance in HIV-1 treatment.

Published on: December 28, 2023
doi: 10.17756/nwj.2023-s5-047
Citation: Kumari N, Bamrah G, Biswas A, Srivastava S. 2023. HIV-1 Protease Drug-resistant Mutations and Inhibitor Binding Mechanism: A Review on Hybrid Quantum Mechanics/Molecular Mechanics Approach. NanoWorld J 9(S5): S240-S247.

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