Molecular modeling and binding energy calculations for drug resistant mutations in HIV-1 protease-inhibitor complexes

摘要

HIV-1 protease (Pr) processes polyprotein gene products into structural proteins and enzymes essential for maturation and infectivity of the virus.HIV-1 Pr inhibitors (PrI) developed by high-throughput screeening and structure-based drug design have shown significant promise in anti-AIDS therapy.However,the clinical effectiveness of PrIs is limited by rapid emergence of drug-resistant mutations.