Abstract
Nonenzymatic glycation (Maillard reaction) is a posttranslational modification of peptides and proteins by sugars, which, after a cascade of reactions, leads to the formation of a complex family of irreversibly changed advanced glycation end products (AGE) implicated in the pathogenesis of human diseases. Last reversible intermediates of this reaction are Amadori/Heyns compounds formed in glucose/fructose induced modification of peptides. The stability of these compounds determines the further course of the reaction.
To provide information concerning the preparation of model systems as well as the fate of glycated opioid peptides introduced in the human circulation, the enzymatic (80 % human serum) and chemical (PBS) stability of Amadori and Heyns compounds related to the endogenous opioid pentapeptides leucine- and methionine-enkephalin (Tyr-Gly-Gly-Phe-Leu/Met) were investigated.
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Jakas, A. (2013). The Maillard Reaction Induced Modifications of Endogenous Opioid Peptide Enkephalin. In: Cudic, P. (eds) Peptide Modifications to Increase Metabolic Stability and Activity. Methods in Molecular Biology, vol 1081. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-652-8_9
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DOI: https://doi.org/10.1007/978-1-62703-652-8_9
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