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

James J. Peterson; Claude F. Meares

doi:10.1021/bc980059j

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

James J. Peterson, Claude F. Meares

Chemistry

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

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 language	English (US)
Pages (from-to)	618-626
Number of pages	9
Journal	Bioconjugate Chemistry
Volume	9
Issue number	5
DOIs	https://doi.org/10.1021/bc980059j
State	Published - Sep 1998

ASJC Scopus subject areas

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

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

Abstract

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