Beta-Endorphin: dissociation of receptor binding activity from analgesic potency

Proc Natl Acad Sci U S A. 1980 Apr;77(4):2303-4. doi: 10.1073/pnas.77.4.2303.

Abstract

Biological activities of synthetic camel beta-endorphin and human beta-endorphin (beta h-EP) have been measured by the radioreceptor binding assay, using [Tyr27-3H]-beta h-EP as the primary ligand and by the tail-flick test for analgesic potency. Four synthetic analogs of beta h-EP, namely [Gly31]-beta h-EP-Gly-NH2, [Gly31]-beta h-EP-Gly-Gly-NH2, [Gln8,Gly31]-beta h-EP-Gly-Gly-NH2, and [CH3(CH2)4NH231]-beta h-EP, have also been assayed by the same procedures. Results indicate a clear dissociation of radioreceptor binding activity from analgesic potency.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Analgesia*
  • Endorphins / metabolism
  • Endorphins / pharmacology*
  • Hormones / metabolism
  • Pain / physiopathology*
  • Radioligand Assay
  • Receptors, Opioid / metabolism*
  • Structure-Activity Relationship

Substances

  • Endorphins
  • Hormones
  • Receptors, Opioid