Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins

Chembiochem. 2016 Oct 4;17(19):1800-1803. doi: 10.1002/cbic.201600213. Epub 2016 Jul 29.

Abstract

Dietary unsaturated fatty acids, such as oleic acid, have been shown to be covalently incorporated into a small subset of proteins, but the generality and diversity of this protein modification has not been studied. We synthesized unsaturated fatty-acid chemical reporters and determined their protein targets in mammalian cells. The reporters can induce the formation of lipid droplets and be incorporated site-specifically onto known fatty-acylated proteins and label many proteins in mammalian cells. Quantitative proteomics analysis revealed that unsaturated fatty acids modify similar protein targets to saturated fatty acids, including several immunity-associated proteins. This demonstrates that unsaturated fatty acids can directly modify many proteins to exert their unique and often beneficial physiological effects in vivo.

Keywords: chemical reporter; fatty acids; fatty-acylation; fluorescent probes; quantitative proteomics; unsaturated fatty acids.

Publication types

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

MeSH terms

  • Acylation
  • Animals
  • Cell Line
  • Fatty Acids, Unsaturated / chemistry
  • Fatty Acids, Unsaturated / metabolism*
  • HeLa Cells
  • Humans
  • Mice
  • Proteins / analysis*
  • Proteins / chemistry*
  • Proteins / metabolism
  • Proteomics*

Substances

  • Fatty Acids, Unsaturated
  • Proteins