Structural basis for selective inhibition of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase: molecular docking and 3D QSAR studies

J Chem Inf Model. 2008 Apr;48(4):918-29. doi: 10.1021/ci700453j. Epub 2008 Feb 28.

Abstract

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is as an attractive target for the development of novel antitrypanosomatid agents. In the present work, comparative molecular field analysis and comparative molecular similarity index analysis were conducted on a large series of selective inhibitors of trypanosomatid GAPDH. Four statistically significant models were obtained ( r2 > 0.90 and q2 > 0.70), indicating their predictive ability for untested compounds. The models were then used to predict the potency of an external test set, and the predicted values were in good agreement with the experimental results. Molecular modeling studies provided further insight into the structural basis for selective inhibition of trypanosomatid GAPDH.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Glyceraldehyde-3-Phosphate Dehydrogenases / antagonists & inhibitors*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry
  • Molecular Sequence Data
  • Quantitative Structure-Activity Relationship
  • Sequence Homology, Amino Acid
  • Trypanosoma / enzymology*

Substances

  • Enzyme Inhibitors
  • Glyceraldehyde-3-Phosphate Dehydrogenases