3/29/2023 0 Comments Rage of mages map editorThe type of protein and glycation substrate determine a range of the observed effects. This process can contribute to a pool of AGEs accumulating locally in vivo and affecting tissue biology.ĪGEs can affect the structure and change properties of the modified proteins or cause aggregation, resulting in pathological changes. The intermediate glycation product can further rearrange towards more advanced structures, including cross-links. It is confirmed by the identification of intact melibiose moieties. Finally, our results suggest that the formation of in vitro MAGE adduct is initiated by coupling melibiose to a model myoglobin protein. The difference was reflected in characteristic fluorescence that results from protein structural changes and impact on a heme group of the model myoglobin protein. Glycation in a dry state was more efficient in the formation of structures containing an intact melibiose moiety (21.9%) compared to glycation under aqueous conditions (15.6%). The targeted peptide analysis identified structurally different AGEs, including crosslinking and non-crosslinking modifications associated with lysine, arginine, and histidine residues. Using liquid chromatography coupled with mass spectrometry, we analyzed the physicochemical properties and structures of myoglobin glycated with melibiose under different conditions. In vitro MAGE is efficiently generated under dry conditions in contrast to the reaction carried in an aqueous solvent. The in vivo analog accumulates in several tissues however, its origin still needs explanation. ![]() MAGE (melibiose-derived advanced glycation end-product) is the glycation product generated in the reaction of a model protein with melibiose.
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