Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 27th March 2019 from 11:00 AM to 1:00 PM (GMT).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.

Issue 1, 2005
Previous Article Next Article

Protease profiling using a fluorescent domino peptide cocktail

Author affiliations


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.

Graphical abstract: Protease profiling using a fluorescent domino peptide cocktail

Back to tab navigation

Supplementary files

Publication details

The article was received on 06 Jan 2005, accepted on 30 Mar 2005 and first published on 12 Apr 2005

Article type: Paper
DOI: 10.1039/B419446B
Citation: Mol. BioSyst., 2005,1, 57-63

  •   Request permissions

    Protease profiling using a fluorescent domino peptide cocktail

    Y. Yongzheng and J. Reymond, Mol. BioSyst., 2005, 1, 57
    DOI: 10.1039/B419446B

Search articles by author