Non‐enzymatic glycosylation of the dipeptide l‐carnosine, a potential anti‐protein‐cross‐linking agent

FEBS Letters

Syrris, Petros³  Michaelis, Jürgen¹  Hipkiss, Alan R.² 

[1] Peptide Technology Ltd., 4–10 Inman Road, Dee Why, NSW 2099, Australia;Division of Biomolecular Engineering, CSIRO, 103 Delhi Rd, North Ryde, NSW 2113, Australia;Molecular Biology and Biophysics Group, King's College London, Strand, London WC2R 2LS, UK

关键词: Carnosine;    Non-enzymatic glycosylation;    Diabetes;    Ageing;    AGE-product;    Ac-;    acetyl-;    2AF;    2-aminofluorene;    2AAF;    2-acetamidofluorene;    AGE-products;    advanced glycosylation end-products;    DAHP;    dihydroxyacetone phosphate;    DHA;    dihydroxyacetone;    PBS;    phosphate-buffered saline (150 mM NaCl;    10 nM sodium phosphate;    pH 7.4);   

DOI  :  10.1016/0014-5793(95)00849-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dipeptide carnosine (β-alanyl-l-histidine) was readily glycosylated non-enzymatically upon incubation with the sugars glucose, galactose, deoxyribose and the triose dihydroxyacetone. Carnosine inhibited glycation of actyl-Lys-His-amide by dihydroxyacetone and it protected α-crystallin, superoxide dismutase and catalise against glycation and cross-linking mediated by ribose, deoxyribose, dihydroxyacetone, dihydroxyacetone phosphate and fructose. Unlike certain glycated amino acids, glycated carnosine was non-mutagenic. The potential biological and therapeutic significance of these observations are discussed.

【 授权许可】

Unknown