A global metabolite profiling approach to identify protein-metabolite interactions

J Am Chem Soc. 2008 Oct 29;130(43):14111-3. doi: 10.1021/ja806463c. Epub 2008 Oct 3.


Understanding the biochemical functions of proteins is an important factor in elucidating their cellular and physiological functions. Due to the predominance of biopolymer interactions in biology, many methods have been designed to interrogate and identify biologically relevant interactions that proteins make to DNA, RNA, and other proteins. Complementary approaches that can elucidate binding interactions between proteins and small molecule metabolites will impact the understanding of protein-metabolite interactions and fill a need that is outside the scope of current methods. Here, we demonstrate the ability to identify natural protein-metabolite interactions from complex metabolite mixtures by combining a protein-mediated small molecule enrichment step with a global metabolite profiling platform.

Publication types

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

MeSH terms

  • Anilino Naphthalenesulfonates / chemistry*
  • Binding, Competitive
  • Carrier Proteins / chemistry*
  • Chromatography, Liquid / methods
  • Fatty Acid-Binding Proteins / chemistry*
  • Glutathione Transferase / chemistry*
  • Humans
  • Immobilized Proteins / chemistry
  • Mass Spectrometry / methods
  • Membrane Proteins / chemistry*
  • Proteomics
  • Recombinant Fusion Proteins / chemistry
  • Retinol-Binding Proteins, Cellular / chemistry*
  • Time Factors
  • Tretinoin / chemistry*


  • Anilino Naphthalenesulfonates
  • Carrier Proteins
  • FABP2 protein, human
  • Fatty Acid-Binding Proteins
  • Immobilized Proteins
  • Membrane Proteins
  • Recombinant Fusion Proteins
  • Retinol-Binding Proteins, Cellular
  • STARD3 protein, human
  • Tretinoin
  • 1-anilino-8-naphthalenesulfonate
  • Glutathione Transferase