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 have been invoked as responsible fro protein cross-linking and the production of 'toxic' compunds. 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 of in vitro glycated human serum albumin (HSA)is highly complex. However, there are clear differences between the digestion products of in vitro glycated and unglycated HSA. In the former case, possible glycated peptides belonging to the AGE peptide class may be indentified. Tandem mass spectrometric experiments on selected species seemed to be promising as regards structural information, but it was thought of interest to under take 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.
Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides
Seraglia R;Traldi P
2003
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 have been invoked as responsible fro protein cross-linking and the production of 'toxic' compunds. 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 of in vitro glycated human serum albumin (HSA)is highly complex. However, there are clear differences between the digestion products of in vitro glycated and unglycated HSA. In the former case, possible glycated peptides belonging to the AGE peptide class may be indentified. Tandem mass spectrometric experiments on selected species seemed to be promising as regards structural information, but it was thought of interest to under take 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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
