title: Determination of types and binding sites of advanced glycation end products for substance P.
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.
authors.affiliation: Warwick Centre for Analytical Science, Department of Chemistry, University of Warwick, Coventry, CV4 7AL, United Kingdom.
authors.forename: Andrea F
authors.initials: AF
authors.lastname: Lopez-Clavijo
authors.forename: Mark P
authors.initials: MP
authors.lastname: Barrow
authors.forename: Naila
authors.initials: N
authors.lastname: Rabbani
authors.forename: Paul J
authors.initials: PJ
authors.lastname: Thornalley
authors.forename: Peter B
authors.initials: PB
authors.lastname: O'Connor
mesh_terms: D001665:Binding Sites / Q000502:physiology; D017127:Glycation End Products, Advanced / Q000737:chemistry / Q000378:metabolism*; D013373:Substance P / Q000737:chemistry / Q000378:metabolism*
chemical_list: D017127:Glycation End Products, Advanced; D013373:Substance P