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 journalArticle

35 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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    Tong, Y., Olczak, J., Zabrocki, J., Gershengorn, M. C., Marshall, G. R., & Moeller, K. D. (2000). Constrained peptidomimetics for TRH: cis-peptide bond analogs. Tetrahedron, 56(50), 9791-9800. https://doi.org/10.1016/S0040-4020(00)00886-3