Maillard Proteomics: Opening New Pages

Abstract

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.

Influence of lactose on the formation of whey protein microparticles obtained by dry heating at alkaline pH

“…The pattern of increase in CML content after DH in the presence of lactose is similar to the pattern observed for the color changes of the powders, and a linear regression was found between these 2 variables (P < 0.01). CML is one of the AGE that were produced during the Maillard reaction, together with many other AGE such as Pyrraline or formyl lysine (Soboleva, Schmidt, Vikhnina, Grishina, & Frolov, 2017).…”

Does Protein Glycation Impact on the Drought-Related Changes in Metabolism and Nutritional Properties of Mature Pea (Pisum sativum L.) Seeds?

“…Carbohydrate derivatives-sugar phosphates [4,5], sugar acids [6] and nucleotides [7]-were also reported as glycation agents. The products of early glycation, also known as Amadori and Heyns compounds, can be involved in oxidative degradation, often referred to as glycoxidation [8], yielding a structurally diverse group of advanced glycation end products (AGEs) [9]. Alternatively, AGEs can be formed by so-called oxidative or autoxidative glycosylation, i.e., formation of α-dicarbonyl compounds, mostly glyoxal (GO), methylglyoxal (MGO) and 3-deoxyglucosone (3-DG), and their interaction with lysyl, arginyl and cysteinyl residues [10].…”

Proteome Map of Pea (Pisum Sativum L.) Embryos&nbsp;Containing Different Amounts of Residual&nbsp;Chlorophylls

“…Sample pre-fractionation [33] and isoelectrofocusing (variation of pH gradients) [31,34] do not dramatically improve the situation. In this context, due to the better resolution of RP-HPLC, an LC-MS-based approach seemed promising [14]. Indeed, the most representative LC-MSbased study to date of Min et al, performed with soybean seeds, identified 1626 non-redundant proteins [35], which exceeds the best outcomes from gel-based proteomics surveys by at least two-fold [29].…”

“…However, as detergents, conventionally used for solubilization of protein isolates [5], dramatically affect efficiency of electrospray ionization (ESI) [13], it is difficult to find a compromise between completeness of protein reconstitution and sensitivity of MS analysis. In this context, the introduction of degradable detergents into proteomic practice helped to overcome this caveat [14]. Thus, commercially available detergents such as RapiGest™ and Anionic Acid-Labile Surfactant II (AALS II) gave a deeper insight in the proteomes of young barley [15] and developing oilseed rape [16] seeds.…”