Tryptophan-norleucine 1,5-disubstituted tetrazoles as cis peptide bond mimics: Investigation of the bioactive conformation of a potent and selective peptide for the cholecystokinin-B receptor

Lakmal W. Boteju, Teresa Zalewska, Henry I. Yamamura, Victor J. Hruby

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

It has been suggested that the cis conformation about the TrpNMeNle amide bond is important in conferring high affinity and selectivity to CCK-B receptor ligands. Substitution of the cis amide bond mimic Trpψ(CH4)Nle into the peptide Gly-Trp-N-(Me)Nle-Asp-PheNH2 causes it to lose activity, suggesting that other structural effects of N-(Me)Nle incorporation may be important for high affinity selectivity for the CCK-B receptor.

Original languageEnglish (US)
Pages (from-to)2011-2016
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Volume3
Issue number10
DOIs
StatePublished - Oct 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Tryptophan-norleucine 1,5-disubstituted tetrazoles as cis peptide bond mimics: Investigation of the bioactive conformation of a potent and selective peptide for the cholecystokinin-B receptor'. Together they form a unique fingerprint.

Cite this