Format

Send to

Choose Destination
Biochem Biophys Res Commun. 1997 Mar 6;232(1):227-30.

Acid-stable fluorescent advanced glycation end products: vesperlysines A, B, and C are formed as crosslinked products in the Maillard reaction between lysine or proteins with glucose.

Author information

1
Institute of Bio-Active Science, Nippon Zoki Pharmaceutical Co. Ltd., Hyogo, Japan.

Abstract

Vesperlysines A and B, 6-hydroxy-1,4-di{6-(L-norleucyl)}-1H-pyrrolo[3,2-b]pyridinium and its 5-methyl derivative, respectively, and Vesperlysine C, 5-hydroxy-methyl-1,6-di{6-(L-norleucyl)}-1H-pyrrolo[3,4-b] pyridinium, are isolated as major fluorescent advanced glycation end products (AGEs) from hydrochloric acid hydrolysis of AGE-BSA, bovine serum albumin (BSA) modified by the Maillard reaction with glucose. These fluorophores are glycation products and not artifacts of hydrolysis, since they are also detected in the reaction mixture of lysine and glucose prior to hydrolysis. Vesperlysines are crosslinked products from two lysine side-chains in proteins and are considered to be generated from lysines and the oxidative degradation of glucose, because the six carbon skeleton of glucose in its original form was not incorporated into each structure. These compounds are most likely glycoxidation products like pentosidine. This reasoning is supported by the formation of the same compounds in the Maillard reactions in which ascorbic acid or other sugars with shorter carbon chains are used.

PMID:
9125137
DOI:
10.1006/bbrc.1997.6262
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center