Optimizing the Binding of Fullerene Inhibitors of the HIV-1 Protease through Predicted Increases in Hydrophobic Desolvation||

SH Friedman, PS Ganapathi, Y Rubin…

Index: Friedman; Ganapathi; Rubin; Kenyon Journal of Medicinal Chemistry, 1998 , vol. 41, # 13 p. 2424 - 2429

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Citation Number: 210

Abstract

We have developed and applied a computational strategy to increase the affinity of fullerene- based inhibitors of the HIV protease. The result is a~ 50-fold increase in affinity from previously tested fullerene compounds. The strategy is based on the design of derivatives which may potentially increase hydrophobic desolvation upon complex formation, followed by the docking of the hypothetical derivatives into the HIV protease active site and ...