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Books and chapters

Kühn-Wache, K.; Hoffmann, T.; Manhart, S.; Brandt, W.; Demuth, H.-U.; The Specificity of DP IV for Natural Substrates is Peptide Structure Determined Adv. Exp. Med. Biol. 524 57-63 (2004) DOI: 10.1007/0-306-47920-6_6
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Our results indicate that the substrate properties of peptides are encoded by their own structure. That means, that substrate characteristics depend not only on the primary structure around the catalytic site rather C-terminal located secondary interactions strongly influence the binding and catalysis of the substrates. Such interaction sites seem to force the ligand in a proper orientation to the active site of DP IV. As result of these relations the hydrolysis of peptides with non-proline and non-alanine residues in P1-position (Ser, Val, Gly) becomes possible in longer peptides.Such specific secondary interactions opens the opportunity for development of new inhibitors.

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