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.
Highlights
Glycation is a non-enzymatic post-translational modification of proteins with reducing sugars and α-dicarbonyl products of their degradation [1]
We provide a comprehensive review of existing chromatographic and mass spectrometric techniques used for characterization of protein glycation adducts, i.e., analytical approaches relying on the methods of amino acid analysis
Based on the experiments with polylysine [94], Lapolla and co-workers proposed this technique as a potential tool for diabetes mellitus (DM) diagnostics, and demonstrated clear differences of pyrolysis profiles obtained for glycated albumin from those, acquired with untreated protein [95] (Table 1)
Summary
Glycation is a non-enzymatic post-translational modification of proteins with reducing sugars and α-dicarbonyl products of their degradation [1]. AGEs can be quantified spectrophotometrically by a characteristic increase in absorbance (300–400 nm) [68,69] or by fluorescence at the excitation and emission wavelengths of 370 and 440 nm, respectively [70,71] Both these techniques lack specificity, and do not provide information about individual AGE classes, that dramatically reduces their diagnostic potential. These techniques suffer from a high degree of non-specific binding and typically do not allow simultaneous quantification of several AGEs [72,73] In this context, implementation of mass spectrometry (MS) in analysis of protein glycation products dramatically increases its sensitivity, selectivity, precision, and robustness [74,75]. Thereby we consider individual protein-derived and free amino acids as the targets of MS analysis and discuss them in the context of the actual trends in Maillard research
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