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Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides
Author(s) -
Marotta Ester,
Lapolla Annunziata,
Fedele Domenico,
Senesi Antonella,
Reitano Rachele,
Witt Matthias,
Seraglia Roberta,
Traldi Pietro
Publication year - 2003
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.431
Subject(s) - chemistry , glycation , maillard reaction , mass spectrometry , protein mass spectrometry , chromatography , electrospray ionization , fourier transform ion cyclotron resonance , sample preparation in mass spectrometry , amadori rearrangement , tandem mass spectrometry , peptide , matrix assisted laser desorption/ionization , human serum albumin , organic chemistry , desorption , biochemistry , adsorption , receptor
Abstract The Maillard reaction occurring between sugars and amino groups is important in living systems. When amino groups belonging to protein chains are involved, the Maillard reaction has been invoked as responsible for protein cross‐linking and the production of ‘toxic’ compounds. The reaction leads to the production of a heterogeneous group of substances, usually called advanced glycation end products (AGEs). Classical analytical approaches, such as spectroscopic (ultraviolet, fluorescence) and mass spectrometric (matrix‐assisted laser desorption/ionization, liquid chromatography/electrospray ionization mass spectrometry) methods, have shown that the digestion mixture is highly complex. However, there are clear differences between the digestion mixtures of glycated and unglycated human serum albumin (HSA). In the former case, possible glycated peptides belonging to the AGE peptide class may be identified. Tandem mass spectrometric experiments on selected species seemed to be promising as regards structural information, but it was thought of interest to undertake the present investigation, based on liquid chromatography/electrospray ionization Fourier transform mass spectrometry, in order to obtain definitive results on their elemental composition. Using this approach, about 20 glycated peptides were detected and their possible structures were postulated by examining the known sequence of HSA. Copyright © 2003 John Wiley & Sons, Ltd.