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Electrospray ionization mass spectrometric analysis of complexes between peptide‐derived Amadori products and borate ions
Author(s) -
Kijewska Monika,
Kluczyk Alicja,
Stefanowicz Piotr,
Szewczuk Zbigniew
Publication year - 2009
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.4347
Subject(s) - chemistry , amadori rearrangement , peptide , mass spectrometry , tandem mass spectrometry , fragmentation (computing) , electrospray ionization , chromatography , hydrolysis , moiety , protein mass spectrometry , medicinal chemistry , combinatorial chemistry , organic chemistry , biochemistry , glycation , receptor , computer science , operating system
Hexose‐modified peptides, products of the enzymatic hydrolysis of glycated proteins, could be used as markers of diabetes mellitus , the aging process and other diseases. The main difficulty in this approach is the detection of glycated peptides in the complex mixtures of compounds. In this study we investigated the formation of borate complexes of the peptide‐derived Amadori products by high‐resolution mass spectrometry (HRMS) and tandem mass spectrometry (MS/MS) experiments. It was found that the formation of a complex with the borate ion stabilizes the sugar moiety, resulting in the simplification of the fragmentation patterns of peptide‐derived Amadori products. The level of dehydration, as well as the elimination of formaldehyde from the precursor ions of borate complexes, was lower as compared to the free peptide. On the other hand the intensity of the b‐ and y‐type ions for borate complexes is significantly higher in comparison to the free peptide‐derived Amadori product. Moreover, the elimination of a whole hexose moiety was not detected in the examined peptides. Copyright © 2009 John Wiley & Sons, Ltd.