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Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides (Articolo in rivista)

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Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides (Articolo in rivista) (literal)

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Marotta E. (1), Lapolla A. (2), Fedele D. (2), Senesi A. (2), Reitano R. (2), Witt M. (3), Seraglia R. (1), Traldi P. (1) (2003)
Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides
in Journal of mass spectrometry (Print)
(literal)

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Marotta E. (1), Lapolla A. (2), Fedele D. (2), Senesi A. (2), Reitano R. (2), Witt M. (3), Seraglia R. (1), Traldi P. (1) (literal)

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L'articolo è stato pubblicato su una rivista internazionale autorevole. IF:2,68 (dati 2002) (literal)

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Si è intrapreso questo lavoro con lo scopo di identificare alcuni AGE peptidi, analizzando i prodotti di digestione triptica di HSA glicata in vitro. I risultati ottenuti hanno permesso di identificare circa 20 peptidi glicati e di mettere in evidenza la presenza di alcuni peptidi, la cui formazione può essere razionalizzata solo con reazioni di cross-link intramolecolari. Questultimo dato può spiegare il fatto che la reazione di digestione enzimatica di HSA glicata dà origine ad un minor numero di peptidi, come se la proteina modificata abbia una struttura terziaria diversa che limita lazione dellenzima. (literal)

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(1)CNR-ISTM sez. di Padova; (2)Università di Padova; (3)Bruker Daltonik, Bremen, Germany (literal)

Titolo

Accurate mass measurements by Fourier transform mass spectrometry in the study of advanced glycation end products/peptides (literal)

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. (literal)

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