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N-acylhydrazones containing glycine residue 3a-j and 8a-h were synthesized as HIV-1 capsid protein assembly inhibitors. The structures of the novel N-acylhydrazone derivatives were characterized using different spectroscopic methods. Antiviral activity demonstrated that compound 8c bearing 4-methylphenyl moiety was the most active with low cytotoxicity.

In this study, we have modified 4-hydroxypyran-2-ones, especially introduced heteroatoms (S or O) into the substituents, and detected their interactions with the binding pockets of HIV-1 protease (PR). The results indicated that the ethoxyl groups at C-2 0 and C-5 0 of the phenyl ring could enhance the affinities to the S 1 0 and S 2 0 pockets and improve the inhibitory activities. The most potent compound 10f with an IC 50 of 3.5 nM in enzymatic assay also exhibited good antiviral activity at the cellular level; it exhibited an EC 50 value of 2.9 lM in Simian immunodeficiency virus-infected CEM cells and suppressed the PR activity in 293T cells using western blot analysis.