Topological exploration of cyclic endomorphin-1 analogues, structurally defined models for investigating the bioactive conformation of MOR agonists

Protein Pept Lett. 2007;14(1):51-6. doi: 10.2174/092986607779117218.

Abstract

Although there have been several reports on the conformational analysis of endomorphin-1 (YPWF-NH(2)) and related MOR (mu-opioid receptor) agonists, a definitive, convincing model of the biologically active structure is not yet available. We recently reported the synthesis and pharmacological characterization of the atypical endomorphin-analogue agonist c[YpwFG]. In this paper we discuss the conformational analysis of c[YpwFG] in comparison to its epimers, for investigating the topological features responsible for ligand recognition and receptor activation, and the role of the different pharmacophores.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Models, Molecular
  • Oligopeptides / chemistry*
  • Opioid Peptides / chemistry*
  • Opioid Peptides / pharmacology*
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology*
  • Protein Structure, Secondary
  • Receptors, Opioid, mu / agonists*
  • Structure-Activity Relationship

Substances

  • Oligopeptides
  • Opioid Peptides
  • Peptides, Cyclic
  • Receptors, Opioid, mu
  • endomorphin 1