Next Article in Journal
The Discrepant and Similar Responses of Genome-Wide Transcriptional Profiles between Drought and Cold Stresses in Cassava
Previous Article in Journal
A Split-Luciferase Reporter Recognizing GFP and mCherry Tags to Facilitate Studies of Protein–Protein Interactions
Article Menu
Issue 12 (December) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2017, 18(12), 2677;

Maillard Proteomics: Opening New Pages

Department of Biochemistry, St. Petersburg State University, Saint Petersburg 199034, Russia
Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, 06120 Halle, Germany
Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin-Luther Universität Halle-Wittenberg, 06108 Halle, Germany
Author to whom correspondence should be addressed.
Received: 7 November 2017 / Revised: 29 November 2017 / Accepted: 5 December 2017 / Published: 12 December 2017
(This article belongs to the Section Biochemistry)
Full-Text   |   PDF [3695 KB, uploaded 12 December 2017]   |  


Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress. View Full-Text
Keywords: advanced glycation end products (AGEs); bottom-up proteomics; glycation; glyoxalase; model synthetic peptides; plant glycation; post-translational modifications; proteomics advanced glycation end products (AGEs); bottom-up proteomics; glycation; glyoxalase; model synthetic peptides; plant glycation; post-translational modifications; proteomics

Graphical abstract

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).

Share & Cite This Article

MDPI and ACS Style

Soboleva, A.; Schmidt, R.; Vikhnina, M.; Grishina, T.; Frolov, A. Maillard Proteomics: Opening New Pages. Int. J. Mol. Sci. 2017, 18, 2677.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top