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• W2042917984 abstract "Through a series of synthetic model peptides, we have examined the structural requirements of the P2 and P3 residues in statine-based HIV protease (PR) inhibitors. Results agree with the general observations that, the more bulky the P3 aromatic hydrophobic side chain, the more potent is the inhibitor. At P2, an isopropyl side chain is critical in maintaining potency. Three-dimensional modeling demonstrates that the steric bulk of a leucyl residue or the unfavorable energy transfer, from water to enzyme, for a basic amino acid residue at P2 markedly compromises activity. A naphthylalaninyl-valyl P3-P2 substituted analogue inhibits PR with an IC50 value of 6 nM, and was also effective as an antiviral agent." @default.
• W2042917984 created "2016-06-24" @default.
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• W2042917984 date "1993-08-02" @default.
• W2042917984 modified "2023-09-27" @default.
• W2042917984 title "Model peptides to study the effects of P2and P3substitutions in statine-containing HIV proteinase inhibitors" @default.
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• W2042917984 doi "https://doi.org/10.1016/0014-5793(93)81020-z" @default.
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• W2042917984 hasPublicationYear "1993" @default.
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