Enzymatic cleavage of peptide-linked radiolabels from immunoconjugates

Bioconjug Chem. 1999 Jul-Aug;10(4):553-7. doi: 10.1021/bc990010t.

Abstract

We have incorporated peptides selected by combinatorial library [Peterson, J. J., and Meares, C. F. (1998) Bioconjugate Chem. 9, 618-626) into peptide-linked radiolabeled immunoconjugates of the form DOTA-peptide-antibody. Decapeptide linkers -GFQGVQFAGF- and -GFGSVQFAGF-, selected for cleavage by human liver cathepsin B, were rapidly digested in vitro when compared to the simple model tetrapeptide motif of the prototype -GGGF- [Li, M., and Meares, C. F. (1993) Bioconjugate Chem. 4, 275-283]. Cleavage properties of these library-selected substrates for cathepsin B compared favorably with decapeptide linkers -GLVGGAGAGF- and -GGFLGLGAGF-, which incorporate two of the most labile extended cathepsin B substrates from the literature. The decapeptide linker -GFGSTFFAGF-, selected from the library for cleavage by human liver cathepsin D, was rapidly digested by cathepsin D while the others were not.

Publication types

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

MeSH terms

  • Cathepsin B / chemistry
  • Cathepsin D
  • Cathepsins / chemistry*
  • Chromatography, Thin Layer
  • Immunoconjugates / chemistry*
  • Liver / enzymology
  • Oligopeptides / chemistry*
  • Radiopharmaceuticals / chemistry*
  • Yttrium Radioisotopes

Substances

  • Immunoconjugates
  • Oligopeptides
  • Radiopharmaceuticals
  • Yttrium Radioisotopes
  • Cathepsins
  • Cathepsin B
  • Cathepsin D