Acetylcholine binding by a synthetic receptor: implications for biological recognition

Science. 1990 Dec 14;250(4987):1558-60. doi: 10.1126/science.2274786.

Abstract

The neurotransmitter acetylcholine (ACh) is bound with 50-micromolar affinity by a completely synthetic receptor (host) comprising primarily aromatic rings. The host provided an overall hydrophobic binding site, but one that could recognize the positive charge of the quaternary ammonium group of ACh through a stabilizing interaction with the electron-rich pi systems of the aromatic rings (cation-pi interaction). Similar interactions may be involved in biological recognition of ACh and other choline derivatives.

Publication types

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

MeSH terms

  • Acetylcholine / metabolism*
  • Affinity Labels
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cations
  • Drosophila
  • Electrochemistry
  • Immunoglobulin Fab Fragments / metabolism
  • Models, Molecular*
  • Molecular Sequence Data
  • Molecular Structure
  • Phosphorylcholine / metabolism
  • Quaternary Ammonium Compounds / metabolism*
  • Receptors, Cholinergic / chemistry
  • Receptors, Cholinergic / metabolism*
  • Thermodynamics
  • Torpedo

Substances

  • Affinity Labels
  • Cations
  • Immunoglobulin Fab Fragments
  • Quaternary Ammonium Compounds
  • Receptors, Cholinergic
  • Phosphorylcholine
  • Acetylcholine