title: Protease profiling using a fluorescent domino peptide cocktail.
abstract: Five hexapeptides were prepared containing, in a domino-type arrangement, all 25 possible dipeptides between (1) aromatic, (2) hydrophobic, (3) positively charged, (4) negatively charged, and (5) small and polar amino acids. The peptides were fluorescence labeled at the N-terminus with a (7-coumaryl)oxyacetyl group, allowing the selective detection of N-terminal cleavage products. The five peptides were used as a cocktail reagent in an HPLC analysis. The cocktail produced specific cleavage patterns, or fingerprints, for a variety of proteases. This domino peptide cocktail can be used as a general reagent for protease identification and functional profiling.
authors.affiliation: Department of Chemistry & Biochemistry, University of Berne, Freiestrasse 3, 3012 Berne, Switzerland.
authors.forename: Yang
authors.initials: Y
authors.lastname: Yongzheng
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Reymond
mesh_terms: D002851:Chromatography, High Pressure Liquid; D005456:Fluorescent Dyes; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000032:analysis*; D019151:Peptide Library; D013379:Substrate Specificity
chemical_list: D005456:Fluorescent Dyes; D009842:Oligopeptides; D019151:Peptide Library; D010447:Peptide Hydrolases