N-Terminal pyrazinones: a new class of peptide-bound advanced glycation end-products
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
The reaction of peptide Gly-Ala-Phe with the alpha-dicarbonyl compounds glyoxal and methylglyoxal was studied under physiological conditions (pH=7.4, 37degreesC). Using HPLC with UV and fluorescence detection, a rapid derivatization of the peptide and the concomitant formation of well-defined products were observed. The products, which showed characteristic UV absorbance (lambda(max)=320 to 340 nm) and fluorescence (lambda(ex)=330 to 340 nm, lambda(em)=395 to 405 nm), were identified by ESI-MS and NMR spectroscopic analysis as the N-terminally pyrazinone-modified peptides I (N-[2-(2-oxo-2H-pyrazin-1-yl)-propyl]-phenylalanine) and II (N-[2-(5-methyl-2-oxo-2H-pyrazin-1-yl)-propionyl]-phenylalanine). Model experiments revealed that the reactivity of the N-termini of peptides towards a derivatization by glyoxal is in the same order of magnitude as that of arginine, which generally is attributed as main target for alpha-dicarbonyl compounds in proteins. Incubation of insulin with glyoxal proved the protein-bound formation of pyrazinones, with the N-terminus of the B-chain as the main target. According to these results, we conclude that N-terminal pyrazinones represent a new type of advanced glycation end-products (AGEs) with significance for biological systems and foods.
Details
Original language | English |
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Pages (from-to) | 9-18 |
Number of pages | 10 |
Journal | Amino Acids |
Volume | 27 |
Issue number | 1 |
Publication status | Published - Aug 2004 |
Peer-reviewed | Yes |
External IDs
Scopus | 4444281151 |
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WOS | 000223266300002 |
Keywords
Sustainable Development Goals
Keywords
- glycation, Maillard reaction, pyrazinone, advanced glycation end-product (AGE), glyoxal, methylglyoxal, insulin, EPSILON-CARBOXYMETHYLLYSINE, CHEMICAL-MODIFICATION, DIABETIC-PATIENTS, MAILLARD REACTION, TISSUE PROTEINS, GLYOXAL, METHYLGLYOXAL, IDENTIFICATION, MECHANISM, GLUCOSE