Probing the bradykinin receptor: Mapping the geometric topography using ethers of hydroxyproline in novel peptides

D. J. Kyle, J. A. Martin, R. M. Burch, J. P. Carter, S. Lu, S. Meeker, J. C. Prosser, J. P. Sullivan, J. Togo, L. Noronha-Blob, J. A. Sinsko, R. F. Walters, L. W. Whaley, R. N. Hiner

Research output: Contribution to journalArticlepeer-review

Abstract

Five decapeptides were prepared, each having the generic primary sequence D-Arg0-Arg1-Pro2-Hyp3-Gly4-Thi5-Ser6-X7-Y8-Arg9. A C-terminal β-turn was anticipated when X was an alkyl ether of D-4-hydroxyproline in either the cis or trans geometric state and Y was either a Tic or Oic residue. Whereas cis ethers have only very weak receptor affinities, the trans ethers are signifcantly more potent in binding to guinea pig smooth muscle having K(i) values as low as 0.16 nM. Notably, these peptides do not contain a D-aromatic amino acid at position 7 of the primary sequence.

Original languageEnglish (US)
Pages (from-to)513-525
Number of pages13
JournalAgents and Actions
Volume38
Issue numberSUPPL. I
StatePublished - Jan 1 1992
Externally publishedYes

ASJC Scopus subject areas

  • Toxicology
  • Pharmacology (medical)

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