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Int. J. Mol. Sci. 2017, 18(12), 2557; https://doi.org/10.3390/ijms18122557

Probing Protein Glycation by Chromatography and Mass Spectrometry: Analysis of Glycation Adducts

1
Department of Biochemistry, St. Petersburg State University, 199034 Saint Petersburg, Russia
2
Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
These authors contributed equally to the work.
*
Author to whom correspondence should be addressed.
Received: 8 October 2017 / Revised: 26 November 2017 / Accepted: 27 November 2017 / Published: 28 November 2017
(This article belongs to the Special Issue Glyoxalase System in Health and Disease 2017)
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Abstract

Glycation is a non-enzymatic post-translational modification of proteins, formed by the reaction of reducing sugars and α-dicarbonyl products of their degradation with amino and guanidino groups of proteins. Resulted early glycation products are readily involved in further transformation, yielding a heterogeneous group of advanced glycation end products (AGEs). Their formation is associated with ageing, metabolic diseases, and thermal processing of foods. Therefore, individual glycation adducts are often considered as the markers of related pathologies and food quality. In this context, their quantification in biological and food matrices is required for diagnostics and establishment of food preparation technologies. For this, exhaustive protein hydrolysis with subsequent amino acid analysis is the strategy of choice. Thereby, multi-step enzymatic digestion procedures ensure good recoveries for the most of AGEs, whereas tandem mass spectrometry (MS/MS) in the multiple reaction monitoring (MRM) mode with stable isotope dilution or standard addition represents “a gold standard” for their quantification. Although the spectrum of quantitatively assessed AGE structures is continuously increases, application of untargeted profiling techniques for identification of new products is desired, especially for in vivo characterization of anti-glycative systems. Thereby, due to a high glycative potential of plant metabolites, more attention needs to be paid on plant-derived AGEs. View Full-Text
Keywords: advanced glycation end products (AGEs); amino acid analysis; exhaustive hydrolysis; glycation; glycation adducts; glyoxalase; LC-MS/MS; stable isotope dilution; standard addition advanced glycation end products (AGEs); amino acid analysis; exhaustive hydrolysis; glycation; glycation adducts; glyoxalase; LC-MS/MS; stable isotope dilution; standard addition
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Soboleva, A.; Vikhnina, M.; Grishina, T.; Frolov, A. Probing Protein Glycation by Chromatography and Mass Spectrometry: Analysis of Glycation Adducts. Int. J. Mol. Sci. 2017, 18, 2557.

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