Naslov
Glycosylation of a lysine-containing pentapeptides by glucuronic acid : new insights into the Maillard reaction

Autori
Horvat, Štefica ; Roščić, Maja

Izvornik
Carbohydrate research (0008-6215) 345 (2010), 3; 377-384

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
amadori ; glucuronic acid ; glycation ; 3-hydroxypyridine ; Maillard ; peptide

Sažetak
The formation of glycosylation products in model systems consisting of D-glucuronic acid (GlcA) and lysine-containing peptides, such as Lys-Gly-Gly-Phe-Leu (1), Gly-Lys-Gly-Phe-Leu (4) and Ac-Gly-Lys-Gly-Phe-Leu (6), was examined to evaluate the site specificity, extent and nature of modification. Peptides were reacted with GlcA either in solution or under dry-heating conditions. From the incubations performed in solution (MeOH), the corresponding (1-deoxy-D-fructofuranos-1-yl uronic acid)-peptide derivatives (Amadori compounds) were isolated. Whereas reaction of 1 resulted in the formation of mono-glycosylated Amadori compound 2 with the sugar moiety attached to the N-epsilon-amino group of the Lys residue, and its di-glycosylated analogue 3, exposure of 4 to GlcA afforded only di-glycosylated peptide 5. From the incubation of GlcA with Ac-Gly-Lys-Gly-Phe-Leu (6) performed under mild dry-heating conditions (50 oC) in environment of 75% relative humidity, besides Amadori compound 7, two new Maillard reaction products were isolated containing 3-hydroxypyridinium (8) and 3-hydroxy-picolinic acid moiety (9). The mechanism of pyridinium products formation is discussed.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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