Synthesis and evaluation of new endomorphin analogues modified at the Pro2 residue

Domenica Torino, Adriano Mollica, Francesco Pinnen, Gino Lucente, Federica Feliciani, Peg Davis, Josephine Lai, Shou Wu Ma, Frank Porreca, Victor J. Hruby

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

Six new endomorphin analogues, incorporating constrained amino acids in place of native proline have been synthesized. Residues of (S)-azetidine-2-carboxylic acid (Aze), 3,4-dehydro-(S)-proline (Δ3Pro), azetidine-3-carboxylic acid (3Aze) and dehydro-alanine (ΔAla) have been used to prepare [Δ3Pro2]EM-2 (1), [Aze2]EM-1 (2), [Aze2]EM-2 (3), [3Aze2]EM-1 (4), [3Aze2]EM-2 (5) and [ΔAla2]EM-2 (6). Binding assays and functional bioactivities for μ- and δ-receptors are reported. The highest affinity, bioactivity and selectivity are shown by peptides 2 and 3 containing the Aze residue.

Original languageEnglish (US)
Pages (from-to)4115-4118
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume19
Issue number15
DOIs
StatePublished - Aug 1 2009

Keywords

  • 3,4-Didehydro-(S)-proline
  • Azetidine carboxylic acids
  • Didehydro-alanine
  • Endomorphins
  • μ-Receptors

ASJC Scopus subject areas

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

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