Web Release Date: March 29,
Tripeptide Probes for Tripeptidyl Protease I Production via Gene Transfer
and
Department of Chemistry, University of Iowa, Iowa City, Iowa 52242-1294 and Program in Gene Therapy, Departments of Internal Medicine, Neurology, Physiology & Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242-1294
Received November 19, 2002
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.
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