ABSTRACT
Human immunodeficiency virus 1 (HIV-1) aspartyl protease performs a critically important step in the viral life cycle. Immature viral Gag and Gag–Pol polyproteins are processed by cleavage to form structural and enzyme components, before assembly into nascent, infectious virions. Darunavir is a synthetic nonpeptidyl small molecule analog of amprenavir that inhibits the dimerization and catalytic activity of the protease enzyme (Hayashi et al., 2014; Koh et al., 2007), thereby preventing viral maturation. The chemical structure is similar to that of amprenavir; however, the terminal tetra-hydrofuran (THF) group is fused to a second THF group, to form a bis-THF moiety.
