Journal article
Tripeptide probes for tripeptidyl protease I production via gene transfer
Journal of medicinal chemistry, Vol.46(9), pp.1603-1608
04/24/2003
DOI: 10.1021/jm020525x
PMID: 12699378
Abstract
Tripeptides derived from 5-chloroanthraquinone hydrazide and anthraquinone hydrazide have been prepared as potential reagents to probe cellular expression of tripeptidyl protease I (TPP-I). Attempted chemical synthesis of Gly-l-Pro-l-Ala-chloroanthraquinone hydrazide, a compound that had been reported to serve as a substrate for this enzyme, was complicated by formation of a pyrazoloquinone. In contrast, formation of pyrazoloquinones was not observed during coupling reactions with anthraquinone hydrazide, and several tripeptide derivatives of this compound were prepared. The most attractive probe for TPP-I activity in tests with mouse kidney tissue sections proved to be Gly-l-Pro-l-Ser anthraquinone hydrazide.
Details
- Title: Subtitle
- Tripeptide probes for tripeptidyl protease I production via gene transfer
- Creators
- MeeKyoung Kim - Department of Chemistry, University of Iowa, Iowa City, Iowa 52242-1294, USAQinwen MaoBeverly L DavidsonDavid F Wiemer
- Resource Type
- Journal article
- Publication Details
- Journal of medicinal chemistry, Vol.46(9), pp.1603-1608
- Publisher
- United States
- DOI
- 10.1021/jm020525x
- PMID
- 12699378
- ISSN
- 0022-2623
- eISSN
- 1520-4804
- Language
- English
- Date published
- 04/24/2003
- Academic Unit
- Neuroscience and Pharmacology; Chemistry
- Record Identifier
- 9983985834802771
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