Endomorphin-2 with a beta-turn backbone constraint retains the potent micro-opioid receptor agonist properties

J Med Chem. 2008 Jan 10;51(1):173-7. doi: 10.1021/jm7010222. Epub 2007 Dec 7.

Abstract

The constitutional similarity with different secondary structure preference between the Aba-Gly and the spiro-Aba-Gly scaffolds were exploited to design the novel endomorphin-2 analogs Tyr-spiro-( R/ S)-Aba-Gly-Phe-NH(2) ( 1 and 2) and Tyr-( R/ S)-Aba-Gly-Phe-NH(2) ( 3 and 4). The ( R)-spiro analog 1 was found to be a potent and selective micro-opioid agonist/partial agonist ( K (imicro) = 29.3 nM, IC(50) = 50 nM, K(e) = 0.57). NMR experiments and molecular modeling indicated that its backbone adopts mainly a beta-turn in aqueous solution.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / chemistry
  • Protein Structure, Secondary
  • Receptors, Opioid, mu / agonists*
  • Solutions
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Oligopeptides
  • Receptors, Opioid, mu
  • Solutions
  • endomorphin 2