Tripeptide probes for tripeptidyl protease I production via gene transfer

Mee Kyoung Kim, Qinwen Mao, Beverly L. Davidson, David F. Wiemer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1603-1608
Number of pages6
JournalJournal of Medicinal Chemistry
Issue number9
StatePublished - Apr 24 2003

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery


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