Designing new pharmaceutical derivatives for potential inhibition of human immunodeficiency virus protease enzyme inhibition; a comprehensive in silico study.

In the ongoing effort to address viral diseases, the utilization of enzyme inhibitors targeting viral enzymes has emerged as a notable and effective strategy. The prevalence of hazardous and potentially fatal viral infections, such as Acquired Immunodeficiency Syndrome (AIDS), emphasizes the importance of exploring these inhibitors to advance healthcare solutions. This study conducts a comprehensive examination of the interaction between Indinavir and HIV protease, evaluating the functional efficacy of designed analogs based on Indinavir using docking tools. Quantum mechanics calculations are used for precise analysis of the structural and molecular properties of each designed analog. Additionally, ADMET studies for these compounds are examined to increase the evaluation of potential side effects and physicochemical properties. Molecular dynamics simulations are performed to deepen understanding and evaluate the inhibitory potential of these compounds on the protease enzyme. In conclusion, this comprehensive approach, integrating quantum mechanics calculations, ADMET screening, molecular docking, and molecular dynamics aims to enhance results in the development of antiviral candidates and refinement of existing drugs. Results introduce Lig12 as a designed compound that shows higher enzyme inhibition ability compared to Indinavir. This study emphasizes the importance of innovative drug design approaches in addressing the evolving challenges posed by viral infections. However, it is imperative to acknowledge the necessity for further experimental validations to verify the current findings and ensure their relevance.