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 |
Fingerprint
ASJC Scopus subject areas
- Chemistry(all)
- Organic Chemistry
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library. / Peterson, James J.; Meares, Claude F.
In: Bioconjugate Chemistry, Vol. 9, No. 5, 09.1998, p. 618-626.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library
AU - Peterson, James J.
AU - Meares, Claude F.
PY - 1998/9
Y1 - 1998/9
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0032170893&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032170893&partnerID=8YFLogxK
U2 - 10.1021/bc980059j
DO - 10.1021/bc980059j
M3 - Article
C2 - 9736496
AN - SCOPUS:0032170893
VL - 9
SP - 618
EP - 626
JO - Bioconjugate Chemistry
JF - Bioconjugate Chemistry
SN - 1043-1802
IS - 5
ER -