Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.

Eitemau Tebyg

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• DMP 323, a nonpeptide cyclic urea inhibitor of human immunodeficiency virus (HIV) protease, specifically and persistently blocks intracellular processing of HIV gag polyprotein.
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• Solvation studies of DMP323 and A76928 bound to HIV protease: analysis of water sites using grand canonical Monte Carlo simulations.
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• In vitro anti-human immunodeficiency virus (HIV) activity of XM323, a novel HIV protease inhibitor.
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• Evolution of cyclic peptide protease inhibitors
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