Novel pseudosymmetric inhibitors of HIV-1 protease

Bioorganic & Medicinal Chemistry Letters
1993.0

Abstract

Compounds containing the easily accessible Phe[CH(OH)CH2N(NH)]Phe dipeptide isostere as a nonhydrolyzable replacement of the scissile amide bond in the natural substrate are potent inhibitors of HIV-1 protease. The expected symmetric binding pattern of the most potent inhibitor in this series (CGP 53820, IC50 = 9 nM) is illustrated by the X-ray analysis performed with the corresponding enzyme-inhibitor complex.

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