Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library.
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.
Peterson
J J
JJ
Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616-5295, USA.
Meares
C F
CF
D000178:Acrylamides / Q000737:chemistry; D002401:Cathepsin B / Q000378:metabolism*; D002402:Cathepsin D / Q000378:metabolism*; D016503:Drug Delivery Systems; D005453:Fluorescence; D006801:Humans; D008099:Liver / Q000201:enzymology; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis; D011092:Polyethylene Glycols / Q000737:chemistry; D017421:Sequence Analysis; D013379:Substrate Specificity
D000178:Acrylamides; D019151:Peptide Library; D010455:Peptides; D011092:Polyethylene Glycols; D002401:Cathepsin B; D002402:Cathepsin D