Kinetic characterization of a peptide inhibitor of trypsin isolated from a synthetic peptide combinatorial library

Gary S. Coombs, James Hazzard, David R. Corey

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Recently Eichler and Houghten1 have described the use of a combinatorial peptide library to optimize small trypsin inhibitors. Our kinetic analysis of the most inhibitory peptide, YYGAKIYRPDKM, reveals that it is an inefficiently cleaved substrate for trypsin due to a low kcat. possesses a relatively low KM, and may exhibit nonproductive binding.

Original languageEnglish (US)
Pages (from-to)611-614
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume5
Issue number6
DOIs
StatePublished - Mar 16 1995

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Peptide Library
Trypsin Inhibitors
Trypsin
Peptides
Kinetics
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Molecular Biology
  • Molecular Medicine
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Kinetic characterization of a peptide inhibitor of trypsin isolated from a synthetic peptide combinatorial library. / Coombs, Gary S.; Hazzard, James; Corey, David R.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 5, No. 6, 16.03.1995, p. 611-614.

Research output: Contribution to journalArticle

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