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 | |
| State | Published - Sep 1998 |
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ASJC Scopus subject areas
- Chemistry(all)
- Organic Chemistry
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
Peterson, J. J., & Meares, C. F. (1998). Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library. Bioconjugate Chemistry, 9(5), 618-626. https://doi.org/10.1021/bc980059j