Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library

James J. Peterson, Claude F. Meares

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Several extended peptide substrates for the human liver enzymes cathepsin B and cathepsin D have been selected as cleavable linkers for lysosomal proteolysis of bioconjugates. A one-bead-one-peptide combinatorial library of 94 fluorogenic substrates was employed. We designed this library to explore a set of substrates containing nonionizable/nonoxidizable groups to meet the requirements of prelabeling [Li et al. (1994) Bioconjugate Chem. 5, 101-104] as well as to yield stable conjugates whose preparation is straightforward.

Original languageEnglish (US)
Pages (from-to)618-626
Number of pages9
JournalBioconjugate Chemistry
Volume9
Issue number5
DOIs
StatePublished - Sep 1998

Fingerprint

Peptide Library
Cathepsins
Cathepsin B
Cathepsin D
Fluorescent Dyes
Peptides
Proteolysis
Libraries
Fluorescence
Liver
Substrates
Enzymes

ASJC Scopus subject areas

  • Chemistry(all)
  • Organic Chemistry
  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library. / Peterson, James J.; Meares, Claude F.

In: Bioconjugate Chemistry, Vol. 9, No. 5, 09.1998, p. 618-626.

Research output: Contribution to journalArticle

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