Identification of protease substrates by combinatorial profiling on TentaGel beads
- 11 October 2007
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- No. 43,p. 4453-4455
- https://doi.org/10.1039/b713595e
Abstract
Reacting a 65 536 member combinatorial library of octapeptides on TentaGel beads with various proteases followed by selective staining of the free amino termini at the reacted bead surface and sequence determination by amino acid analysis allowed the rapid identification of protease substrates.Keywords
This publication has 34 references indexed in Scilit:
- A General Method for Designing Combinatorial Peptide Libraries Decodable by Amino Acid AnalysisJournal of Combinatorial Chemistry, 2007
- Methods for mapping protease specificityCurrent Opinion in Chemical Biology, 2007
- Modulation of Infectivity in Phage Display as a Tool to Determine the Substrate Specificity of ProteasesChemBioChem, 2006
- Smart Combinatorial Assays for the Determination of Protease Activity and InhibitionQSAR & Combinatorial Science, 2005
- Human and mouse proteases: a comparative genomic approachNature Reviews Genetics, 2003
- Irreversible Inhibitors of Serine, Cysteine, and Threonine ProteasesChemical Reviews, 2002
- Synthesis of a statistically exhaustive fluorescent peptide substrate library for profiling protease specificityBioorganic & Medicinal Chemistry Letters, 2000
- Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity.Proceedings of the National Academy of Sciences of the United States of America, 1994
- Substrate Phage: Selection of Protease Substrates by Monovalent Phage DisplayScience, 1993
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967