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

Bioconjug Chem. 1998 Sep-Oct;9(5):618-26. doi: 10.1021/bc980059j.

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 9(4) 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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acrylamides / chemistry
  • Cathepsin B / metabolism*
  • Cathepsin D / metabolism*
  • Drug Delivery Systems
  • Fluorescence
  • Humans
  • Liver / enzymology
  • Peptide Library*
  • Peptides / chemical synthesis
  • Polyethylene Glycols / chemistry
  • Sequence Analysis
  • Substrate Specificity

Substances

  • Acrylamides
  • Peptide Library
  • Peptides
  • Polyethylene Glycols
  • Cathepsin B
  • Cathepsin D