Allosteric interaction of dynorphin and myelin basic protein with muscarinic receptors

Pharmacology. 1993 Dec;47(6):351-9. doi: 10.1159/000139118.


Interaction of the basic peptides dynorphin A and myelin basic protein with muscarinic receptors was investigated in rat heart and cerebral cortex using radioligand receptor binding assays. Results showed that these peptides inhibit the binding of the muscarinic ligand [3H]N-methylscopolamine at equilibrium and alter the kinetics of ligand dissociation in an allosteric fashion. The number of basic amino acid residues in the composition of dynorphin A is important in eliciting its allosteric interactions. Our data suggest that endogenous basic peptides play a role in regulating the conformation of muscarinic receptors.

Publication types

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

MeSH terms

  • Allosteric Regulation
  • Amino Acid Sequence
  • Animals
  • Cerebral Cortex / chemistry
  • Cerebral Cortex / drug effects
  • Drug Interactions
  • Dynorphins / pharmacology*
  • Heart / drug effects
  • In Vitro Techniques
  • Male
  • Molecular Sequence Data
  • Myelin Basic Protein / pharmacology*
  • Myocardium / chemistry
  • Radioligand Assay
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, Muscarinic / drug effects
  • Receptors, Muscarinic / metabolism*


  • Myelin Basic Protein
  • Receptors, Muscarinic
  • Dynorphins