Site-specific cross-linking of collagen peptides by lysyl advanced glycation endproducts

• Published in: Chemical communications (Cambridge, England) Vol. 50; no. 38; pp. 4944 - 4946
• Main Authors: Kamalov, M., Harris, P. W. R., Cooper, G. J. S., Brimble, M. A.
• Format: Journal Article
• Language: English
• Published: CAMBRIDGE Royal Soc Chemistry 18.05.2014
• Subjects: Chemistry; Chemistry, Multidisciplinary; Chromatography, High Pressure Liquid; Circular Dichroism; Collagen - chemistry; Collagen - metabolism; Dimerization; Glycation End Products, Advanced - chemistry; Glycation End Products, Advanced - metabolism; Glyoxal - chemistry; Lysine - chemistry; Physical Sciences; Pyruvaldehyde - chemistry; Science & Technology; Trypsin - metabolism; N-ALPHA-HIPPURYLLYSINE; MAILLARD REACTION; LYSINE; MODEL PEPTIDES; PROTEINS; END-PRODUCTS; GLYOXAL; METHYLGLYOXAL

Cross-linking of proteins by advanced glycation endproducts (AGEs) causes a host of pathological conditions but their exact roles are unknown. Cross-linking lysyl AGEs were synthesized and incorporated into two types of collagen peptides. The utility of these cross-linked peptides for biochemical in...