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

Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins.

Author information

1
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, 1230 York Avenue, New York, NY, 10065, USA.
2
The Crick Institute, 215 Euston Road, London, NW1 2BE, UK.
3
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, 1230 York Avenue, New York, NY, 10065, USA. hhang@rockefeller.edu.

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

PMID:
27350074
PMCID:
PMC5050088
DOI:
10.1002/cbic.201600213
[Indexed for MEDLINE]
Free PMC Article

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