Acquired immune deficiency syndrome (AIDS), caused by HIV virus, is one of the world’s deadly disease with significant impact on the modern world. The present investigation aims to assess the binding mode of Darunavir with HIV protease inhibitor and role of water in drug receptor interaction by using docking analysis. Docking analysis revealed that, carbonyl oxygen, sulfonyl oxygen, amino nitrogen and furan oxygen are actively involved in electrostatic interaction with HIV protease. Carbonyl oxygen elicit hydrogen bonding with AspB25 (% of H- bonding is 65% and interatomic distance 2.8 A0), AspA25 (% H-bonding 42% and interatomic distance 2.59 A0) whereas furan ring oxygen form H-bond with AspB30 (% H-bonding 11% and interatomic distance 3.42 A0). To analyse the close contact of Darunavir and HIV protease, we have recorded the drug receptor interaction within four A0. Noticeably, both oxygen of sulfone elicit hydrogen bonding with IleA50 and IleB50 through water. Subsequently, amino nitrogen form Hbond with AspA30 through the involvement of water. The present docking analysis concluded that Darunavir interact with HIV protease through hydrogen bonding where involvement of water in drug receptor interaction serves as evidence for the future development of new protease inhibitor.
