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 journalArticle

8 Scopus citations


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
Issue number10
StatePublished - Oct 1993


ASJC Scopus subject areas

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

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