Amino acid specificity of glycation and protein-AGE crosslinking reactivities determined with a dipeptide SPOT library

Advanced glycation end products (AGEs) contribute to changes in protein conformation, loss of function, and irreversible crosslinking. Using a library of dipeptides on cellulose membranes (SPOT library), we have developed an approach to systematically assay the relative reactivities of amino acid si...

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Bibliographic Details
Published in:Nature biotechnology 1999-10, Vol.17 (10), p.1006-1010
Main Authors: Münch, Gerald, Schicktanz, Dorothee, Behme, Andrea, Gerlach, Manfred, Riederer, Peter, Palm, Dieter, Schinzel, Reinhard
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - metabolism
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Cross-Linking Reagents - chemistry
Dipeptides - chemistry
Dipeptides - metabolism
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Glucose - metabolism
Glycation End Products, Advanced
Molecular Sequence Data
Peptide Library
Proteins
Proteins - chemistry
Proteins - metabolism
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Summary:Advanced glycation end products (AGEs) contribute to changes in protein conformation, loss of function, and irreversible crosslinking. Using a library of dipeptides on cellulose membranes (SPOT library), we have developed an approach to systematically assay the relative reactivities of amino acid side chains and the N-terminal amino group to sugars and protein-AGEs. The sugars react preferentially with cysteine or tryptophan when both the alpha-amino group and the side chains are free. In peptides with blocked N-terminus and free side chains, cysteine, lysine, and histidine were preferred. Crosslinking of protein-AGEs to dipeptides with free side chains and blocked N termini occurred preferentially to arginine and tryptophan. Dipeptide SPOT libraries are excellent tools for comparing individual reactivities of amino acids for nonenzymatic modifications, and could be extended to other chemically reactive molecules.
ISSN:1087-0156
1546-1696
DOI:10.1038/13704