Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development

  • Angew Chem Int Ed Engl. 2015 May 11;54(20):5948-51. doi: 10.1002/anie.201500342.
Malgorzata Broncel  1 ,  Remigiusz A Serwa ,  Paulina Ciepla ,  Eberhard Krause ,  Margaret J Dallman ,  Anthony I Magee ,  Edward W Tate
Affiliations
  • 1. Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ (UK).
PMID: 25807930 DOI: 10.1002/anie.201500342
Abstract

Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic Peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in Cell Culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development.

Keywords
capture reagents; lipidation; mass spectrometry; post-translational modification; proteomics.
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