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

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...

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Published inChemical 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
LanguageEnglish
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
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Summary: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 investigations was demonstrated by proteolysis studies and circular dichroism.
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ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc02003k