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

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.

Novel dietary factors in diabetic and non-diabetic kidney disease

“…However, nearly 50% of the total blood volume was collected during the cardiac bleed and our findings are in accordance with a previous study where perfusion was performed [263]. Another important caveat, is that while the dosing strategy used in this model was based on estimated average consumption of CML in human high AGE diets from previous studies, the model albumin protein is not representative of the whole spectrum of AGEs observed in the diet, both free and protein bound [397][398][399]. It needs to be established whether the uptake and bio-distribution of AGE modified albumin is consistent with other commonly consumed AGE modified proteins.…”

Methodology of Drought Stress Research: Experimental Setup and Physiological Characterization

“…It is important to mention, that accumulation of sugars at the background of reactive oxygen species (ROS) overproduction (usually accompanying plant response to drought) might result in enhanced formation of reactive carbonyl compounds (RCCs) and glycation of plant proteins [122,123], similar to the mechanism recently reported to occur under plant ageing [124]. Additional in vitro experiments with peptide and protein models showed formation of various glycoxidative modifications of lysyl and arginyl residues [125,126,127,128], prospectively with an impact on pro-inflammatory properties of glycated proteins [129]. Hence, these modifications might affect nutritional properties of plant-derived foods.…”

Insights into chemical and sensorial aspects to understand and manage beer aging using chemometrics

“…Under the beer pH (4 to 5), the ARP undergoes 1,2 enolization, and the subsequent release of an amine leads predominantly to a 3‐deoxyosone (an α‐dicarbonyl) (Vanderhaegen et al., 2006). Further dehydration and cyclization lead to advanced glycation end products as heterocyclic compounds 5‐hydroxymethylfurfural (5‐HMF) or furfural (FA), long known as aging indicators that can interfere in the beer mouthfeel (Figure 1) (Baert et al., 2012; Li, Yang, Yang, Shan, & Dong, 2009; Shimizu et al., 2001; Soboleva, Vikhnina, Grishina, & Frolov, 2017). In a final stage, condensation reactions lead to the formation of melanoidins, a class of brown nitrogenous polymers, and copolymers soluble in water (Hellwig, Witte, & Henle, 2016; Martins et al., 2001; Oliveira et al., 2016).…”