Constrained peptidomimetics for TRH: cis-peptide bond analogs

Yunsong Tong, Jacek Olczak, Janusz Zabrocki, Marvin C. Gershengorn, Garland R. Marshall, Kevin D. Moeller

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Two constrained analogs of the tripeptide hormone thyroliberin (TRH) have been synthesized. In both, the HisPro peptide bond of the hormone has been 'locked' into a cis-conformation. In the first analog, the constraint used was identical to the constraint used in an earlier trans-peptide bond analog that was a potent agonist for the TRH endocrine receptor TRH-R1. The second analog was built in order to take advantage of a tetrazole ring as the cis-peptide bond constraint. Neither analog showed agonist or antagonist behavior toward TRH-R1 suggesting that the cis-peptide bond conformation may not play a role in the affinity of TRH for TRH-R1. (C) 2000 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)9791-9800
Number of pages10
JournalTetrahedron
Volume56
Issue number50
DOIs
StatePublished - Dec 8 2000

Keywords

  • TRH endocrine receptor
  • Tetrazole ring
  • Tripeptide hormone thyroliberin

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