Role of hydrophobic interactions in binding S-(N-aryl/alkyl-N-hydroxy-carbamoyl) glutathiones to the active site of the antitumor target enzyme glyoxalase I

…, DL Whalen, DS Hamilton, DJ Creighton

Index: Kalsi; Kavarana; Lu; Whalen; Hamilton; Creighton Journal of Medicinal Chemistry, 2000 , vol. 43, # 21 p. 3981 - 3986

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Citation Number: 25

Abstract

Hydrophobic interactions play an important role in binding S-(N-aryl/alkyl-N- hydroxycarbamoyl) glutathiones to the active sites of human, yeast, and Pseudomonas putida glyoxalase I, as the log K i values for these mechanism-based competitive inhibitors decrease linearly with increasing values of the hydrophobicity constants (π) of the N- aryl/alkyl substituents. Hydrophobic interactions also help to optimize polar interactions ...