Lopez-Clavijo, Andrea F., Barrow, Mark P., Rabbani, Naila, Thornalley, Paul J. and O’Connor, Peter B. (2012) Determination of types and binding sites of advanced glycation end products for substance P. Analytical Chemistry, Vol.84 (No.24). pp. 10568-10575. doi:10.1021/ac301583d

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Abstract

Glycation by endogenous dicarbonyl metabolites such as glyoxal is an important spontaneous post-translational (PTM) modification of peptides and proteins associated with structural and functional impairment. The aim of this study was to investigate types and site of PTM of glyoxal-derived advanced glycation end-products–in the neuropeptide substance P by ultrahigh-resolution Fourier transform ion cyclotron resonance (FTICR), mass spectrometry, and tandem mass spectrometry (MS/MS) experiments. The main site of PTM by glyoxal was the side chain guanidine moiety of the arginine residue. Binding site identification has been achieved by electron capture dissociation, double-resonance electron capture dissociation, and collision-activated dissociation, with assignment of the modified amino acid residue with mass error <1 ppm.

Item Type:	Journal Article
Divisions:	Faculty of Science > Chemistry Faculty of Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016) Faculty of Medicine > Warwick Medical School
Journal or Publication Title:	Analytical Chemistry
Publisher:	American Chemical Society
ISSN:	0003-2700
Official Date:	2012
Dates:	Date Event 2012 Published
Volume:	Vol.84
Number:	No.24
Page Range:	pp. 10568-10575
DOI:	10.1021/ac301583d
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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