Investigation of protein-ligand interactions by mass spectrometry

ChemMedChem. 2007 Apr;2(4):425-31. doi: 10.1002/cmdc.200600298.

Abstract

The rate of drug discovery is greatly dependent on the development and improvement of rapid and reliable analytical methods that allow screening for protein-ligand interactions. The solution-based methods for investigating protein-ligand interactions by mass spectrometry (MS), which are discussed in this paper, are hydrogen/deuterium exchange of protein backbone amide hydrogens, and photoaffinity labeling. Moreover, MS analysis of intact noncovalent protein-ligand complexes is described. Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) with its ultra-high resolution and excellent mass accuracy is also considered herein as it is gaining increasing popularity for a mass spectrometric investigation of protein-ligand interactions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Ligands*
  • Mass Spectrometry / methods*
  • Proteins / chemistry
  • Proteins / metabolism*
  • Spectroscopy, Fourier Transform Infrared
  • Structure-Activity Relationship

Substances

  • Ligands
  • Proteins