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Advanced glycation end-products/peptides: a preliminary investigation by LC and LC/MS
Authors:Lapolla Annunziata  Fedele Domenico  Senesi Antonella  Arico Nadia Concetta  Reitano Rachele  Seraglia Roberta  Astner Hubert  Traldi Pietro
Institution:a Dipartimento di scienze mediche e chirurghiche, università di Padova, Via Giustiniani 2, I-35100 Padova, Italy
b Forensic toxicology and antidoping, university hospital of Padova, Via Falloppio 50, I-35100 Padova, Italy
c CNR, Centro di studio sulla stabilità e reattività dei composti di coordinazione, Area della Ricerca, Corso Stati Uniti 4, I-35100 Padova, Italy
Abstract:An investigation on AGE-peptides, originating by proteolysis of in vitro glycated proteins, was carried out by LC methods with different detection applied to the mixture produced by proteinase K digestion of in vitro glycated human serum albumin (HSA). Classical approaches, like spectroscopic (UV, fluorescence) and mass spectrometric methods (MALDI, LC/ESI/MS), show that the digestion mixture is highly complex. However, there are clearcut differences between the digestion mixtures of glycated and unglycated HSA, in the former case allowing identification of possible glycated peptides belonging to the AGE-peptide class. MS/ MS experiments on selected species seem to be promising as regards structural information.
Keywords:Non-enzymatic glycation  LC/ESI/MS  LC/ESI/MS/MS  MALDI/MS
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