Prediction of drug binding affinities by comparative binding energy analysis

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • A R Ortiz - , European Molecular Biology Laboratory (EMBL) Heidelberg, Structures & Biocomputing (Author)
  • M T Pisabarro - , Structural Bioinformatics (Research Group), Technology Platform BIOTEC, European Molecular Biology Laboratory (EMBL) Heidelberg, University of Alcalá (Author)
  • F Gago - , University of Alcalá (Author)
  • R C Wade - , European Molecular Biology Laboratory (EMBL) Heidelberg, Structures & Biocomputing (Author)

Abstract

A new computational method for deducing quantitative structure-activity relationships (QSARs) using structural data from ligand-macromolecule complexes is presented. First, the ligand-macromolecule interaction energy is computed for a set of ligands using molecular mechanics calculations. Then, by selecting and scaling components of the ligand-macromolecule interaction energy that show good predictive ability, a regression equation is obtained in which activity is correlated with the interaction energies of parts of the ligands and key regions of the macromolecule. Application to the interaction of the human synovial fluid phospholipase A2 with 26 inhibitors indicates that the derived QSAR has good predictive ability and provides insight into the mechanism of enzyme inhibition. The method, which we term comparative binding energy (COMBINE) analysis, is expected to be applicable to ligand-receptor interactions in a range of contexts including rational drug design, host-guest systems, and protein engineering.

Details

Original languageEnglish
Pages (from-to)2681-91
Number of pages11
JournalJournal of medicinal chemistry
Volume38
Issue number14
Publication statusPublished - 7 Jul 1995
Peer-reviewedYes

External IDs

Scopus 0029000922

Keywords

Keywords

  • Binding Sites, Binding, Competitive, Electricity, Humans, Models, Molecular, Pharmaceutical Preparations/chemistry, Phospholipases A/antagonists & inhibitors, Phospholipases A2, Structure-Activity Relationship, Synovial Fluid/enzymology, Thermodynamics