Profiling primary protease specificity by peptide synthesis on a solid support

Doeze, R H P and Maltman, B A and Egan, C L and Ulijn, R V and Flitsch, S L (2004) Profiling primary protease specificity by peptide synthesis on a solid support. Agewandte Chemie-International Edition, 43 (24). pp. 3138-3141. ISSN 1433-7851 (https://doi.org/10.1002/anie.200353367)

Abstract

Reverse screening: A greatly simplified primary screening of protease specificity has been achieved by monitoring the fluorescence during the protease-catalyzed coupling of amino acids instead of peptide hydrolysis on a solid support (see picture, AA=amino acid). This approach paves the way for flexible, rapid, high-throughput identification and characterization of proteases without the need for expensively labeled peptide arrays.

ORCID iDs

Ulijn, R V ORCID: https://orcid.org/0000-0001-7974-3779

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• Item metadata

  Item type:	Article
  ID code:	43940
  Dates:	Date Event 14 June 2004 Published
  Keywords:	profiling, primary protease specificity, peptide synthesis, solid support, hydrolysis, substrate specificity, enzymes, fluorescent probe, high-throughput screening, Chemistry, Pharmacy and materia medica, Chemistry(all), Catalysis
  Subjects:	Science > Chemistry Medicine > Pharmacy and materia medica
  Department:	Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Faculty of Science > Pure and Applied Chemistry
  Depositing user:	Pure Administrator
  Date deposited:	30 May 2013 11:23
  Last modified:	20 Jan 2021 20:42
  URI:	https://strathprints.strath.ac.uk/id/eprint/43940