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Inhibition of Glycosylation Processes: the Reaction between Pyridoxamine and Glucose
Author(s) -
Adrover Miquel,
Vilanova Bartolomé,
Muñoz Francisco,
Donoso Josefa
Publication year - 2005
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200590074
Subject(s) - pyridoxamine , glycosylation , pyridoxal , chemistry , amadori rearrangement , pyridoxine , biochemistry , schiff base , glycation , stereochemistry , enzyme , receptor
Glycosylation of proteins by glucose produces toxic and immunogenic compounds called ‘advanced glyclosylation end products’ (AGEs), which are the origin of pathological symptoms in various chronic diseases. In this work, a kinetic study of the reaction between glucose ( 2 ) and pyridoxamine ( 1 ) – a potent inhibitor of AGEs formation both in vivo and in vitro – was conducted. The NH 2 group of pyridoxamine was found to react with the CO group of glucose to form the Schiff base 9 ( Scheme 2 ). Subsequently, the Schiff base gives rise to other products, including compound 3 , pyridoxal, pyridoxine, and 4‐pyridoxic acid. Compound 3 inhibits the Amadori rearrangement, and prevents the formation of other CO groups capable of triggering glycosylation processes. Pyridoxal and pyridoxine can also inhibit protein glycosylation via other previously reported mechanisms.