Achatin-I, an endogenous neuroexcitatory tetrapeptide from Achatina fulica Férussac containing a D-amino acid residue

Biochem Biophys Res Commun. 1989 May 15;160(3):1015-20. doi: 10.1016/s0006-291x(89)80103-2.

Abstract

A tetrapeptide named achatin-I was purified from the suboesophageal and cerebral ganglia of the African giant snail Achatina fulica Férussac, and evoked a potent neuroexcitatory effect. The amino acid sequence of achatin-I is Gly-D-Phe-Ala-Asp. Achatin-I induced a voltage-dependent inward current, due to Na+, on the identifiable giant neuron, periodically oscillating neuron (PON), of the same snail. All possible isomers of achatin-I were synthesized using the solid-phase method. The sensitivity of the neuron to achatin-I and its isomers was strictly stereospecific; among the various isomers, only achatin-I showed marked effects (ED50 = 2.29 x 10(-6)M), while Gly-D-Phe-D-Ala-Asp, the synthetic D-Ala-isomer, was less than 10(-3) active.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Cell Membrane / drug effects
  • Cell Membrane / physiology
  • Electric Conductivity
  • Esophagus / analysis
  • Ganglia / analysis
  • Molecular Sequence Data
  • Molecular Weight
  • Neurons / drug effects
  • Neurons / physiology*
  • Neuropeptides / isolation & purification
  • Neuropeptides / pharmacology*
  • Snails / analysis*
  • Stereoisomerism

Substances

  • Amino Acids
  • Neuropeptides
  • achatin I