Cathepsin Substrates as Cleavable Peptide Linkers in Bioconjugates, Selected from a Fluorescence Quench Combinatorial Library

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 94 fluorogenic substrates was employed. We designed this library to explore...

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Bibliographic Details
Published in:Bioconjugate chemistry Vol. 9; no. 5; pp. 618 - 626
Main Authors: Peterson, James J, Meares, Claude F
Format: Journal Article
Language:English
Published: United States American Chemical Society 01-09-1998
Subjects:
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
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Summary: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.
Bibliography:istex:C37993FF8B4A19178590AF92693CF381C0F4D1FA
ark:/67375/TPS-NQSB60M6-G
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1043-1802
1520-4812
DOI:10.1021/bc980059j