Oxidative degradation of N ε-fructosylamine-substituted peptides in heated aqueous systems
| Autor: | Andrej Frolov, Ralf Hoffmann, Uta Greifenhagen |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Glycation End Products
Advanced Spectrometry Mass Electrospray Ionization Glycosylation Hot Temperature Clinical Biochemistry Kinetics Lysine Biochemistry Medicinal chemistry chemistry.chemical_compound Glycation Amadori rearrangement Organic chemistry Ferrous Compounds Fragmentation (cell biology) Chromatography High Pressure Liquid chemistry.chemical_classification Reactive oxygen species Aqueous solution Organic Chemistry Water Solutions Glucose chemistry Peptides Reactive Oxygen Species 2-Aminoadipic Acid Oxidation-Reduction |
| Zdroj: | Amino Acids. 47:1065-1076 |
| ISSN: | 1438-2199 0939-4451 |
| DOI: | 10.1007/s00726-015-1940-2 |
| Popis: | Glycation, or non-enzymatic glycosylation, is a common protein modification formed by reactions between reducing sugars (i.e. aldoses and ketoses) with protein amino groups. Resulting Amadori and Heyns compounds, respectively, can be oxidatively degraded yielding a structurally heterogeneous group of advanced glycation end-products. We have studied this process in aqueous conditions at 95 °C in terms of appearing products and their formation kinetics in the presence or absence of reactive oxygen species (ROS)-generating systems (iron(II) sulfate). RP-HPLC-ESI-MS revealed 20 products, 12 of which were confirmed after synthesis by identical retention times and fragmentation patterns. These products accumulated during the incubation period of 4 h (N(ε)-carboxymethyl-, N(ε)-formyl- and N(ε)-methyl lysine) or appeared intermediately (2-aminoadipic semialdehyde, N(ε)-ethanalyl lysine). Acidic and basic amino acid residues near the glycation site and elevated ROS levels in the reaction mixture had significant effects on both product formation and degradation kinetics. |
| Databáze: | OpenAIRE |
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