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  • Title: Amino acid specificity of glycation and protein-AGE crosslinking reactivities determined with a dipeptide SPOT library.
    Author: Münch G, Schicktanz D, Behme A, Gerlach M, Riederer P, Palm D, Schinzel R.
    Journal: Nat Biotechnol; 1999 Oct; 17(10):1006-10. PubMed ID: 10504703.
    Abstract:
    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.
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