title: Designing of peptide substrates. Different approaches exemplified by new chromogenic substrates for kallikreins and urokinase.
abstract: Chromogenic peptide substrates for serine proteases have been designed by using two approaches: (1) by using the natural substrate as a model and (2) by structure-activity correlations obtained through screening of a large number of tripeptides. Some recent examples, substrates for kallikreins and urokinase are given.
mesh_terms: D000596:Amino Acids; D010450:Endopeptidases; D007610:Kallikreins / Q000097:blood; D010455:Peptides / Q000032:analysis*; D013329:Structure-Activity Relationship; D014568:Urokinase-Type Plasminogen Activator
chemical_list: D000596:Amino Acids; D010455:Peptides; D010450:Endopeptidases; D007610:Kallikreins; D014568:Urokinase-Type Plasminogen Activator