Topographical requirements for delta opioid ligands: presence of a carboxyl group in position 4 is not critical for deltorphin high delta receptor affinity and analgesic activity

Biochem Biophys Res Commun. 1991 Nov 14;180(3):1290-7. doi: 10.1016/s0006-291x(05)81335-x.

Abstract

To investigate the role of the carboxyl group in deltorphin molecules, we have synthesized three new analogues in which the acidic amino acid residues in position 4 of the deltorphins were replaced by non-acidic but hydrophilic amino acids residues. The three analogues, [Ser4]-, [Gln4]-, and [Cys4]-deltorphin, all are as potent or more potent than either deltorphin I or II at delta opioid receptors and possess good delta selectivities. The excellent correlation between their in vitro delta receptor potencies and their intrathecal antinociception activity forms a strong argument for involvement of those receptors in spinal nociceptive modulation in the rats.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Analgesics / chemistry*
  • Animals
  • Binding, Competitive
  • Brain / metabolism*
  • Male
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Oligopeptides / pharmacology
  • Pain*
  • Protein Conformation
  • Radioligand Assay
  • Rats
  • Rats, Inbred Strains
  • Receptors, Opioid / drug effects
  • Receptors, Opioid / metabolism*
  • Receptors, Opioid, delta

Substances

  • Analgesics
  • Oligopeptides
  • Receptors, Opioid
  • Receptors, Opioid, delta
  • deltorphin I, Ala(2)-
  • deltorphin II, Ala(2)-