Ar. Hipkiss et al., NONENZYMATIC GLYCOSYLATION OF THE DIPEPTIDE L-CARNOSINE, A POTENTIAL ANTI-PROTEIN-CROSS-LINKING AGENT, FEBS letters, 371(1), 1995, pp. 81-85
The dipeptide carnosine (beta-alanyl-L-histidine) was readily glycosyl
ated non-enzymatically upon incubation with the sugars glucose, galact
ose, deoxyribose and the triose dihydroxyacetone, Carnosine inhibited
glycation of actyl-Lys-His-amide by dihydroxyacetone and it protected
alpha-crystallin, superoxide dismutase and catalise against glycation
and cross-linking mediated by ribose, deoxyribose, dihydroxyacetone, d
ihydroxyacetone phosphate and fructose. Unlike certain glycated amino
acids, glycated carnosine was cion-mutagenic. The potential biological
and therapeutic significance of these observations are discussed.