First chemical synthesis of a scorpion alpha-toxin affecting sodium channels: the Aah I toxin of Androctonus australis hector

J Pept Sci. 2004 Nov;10(11):666-77. doi: 10.1002/psc.582.

Abstract

Aah I is a 63-residue alpha-toxin isolated from the venom of the Buthidae scorpion Androctonus australis hector, which is considered to be the most dangerous species. We report here the first chemical synthesis of Aah I by the solid-phase method, using a Fmoc strategy. The synthetic toxin I (sAah I) was renatured in DMSO-Tris buffer, purified and subjected to thorough analysis and comparison with the natural toxin. The sAah I showed physico-chemical (CD spectrum, molecular mass, HPLC elution), biochemical (amino-acid composition, sequence), immunochemical and pharmacological properties similar to those of the natural toxin. The synthetic toxin was recognized by a conformation-dependent monoclonal anti-Aah I antibody, with an IC50 value close to that for the natural toxin. Following intracerebroventricular injection, the synthetic and the natural toxins were similarly lethal to mice. In voltage-clamp experiments, Na(v) 1.2 sodium channel inactivation was inhibited by the application of sAah I or of the natural toxin in a similar way. This work describes a simple protocol for the chemical synthesis of a scorpion alpha-toxin, making it possible to produce structural analogues in time.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Antibody Affinity
  • Electrophysiology
  • Mice
  • Neurotoxins / chemical synthesis*
  • Neurotoxins / pharmacology
  • Protein Renaturation
  • Scorpion Venoms / chemical synthesis*
  • Scorpion Venoms / pharmacology
  • Scorpions / pathogenicity*
  • Sodium Channel Blockers
  • Sodium Channels / drug effects*
  • Survival Rate
  • Type C Phospholipases / chemical synthesis*
  • Type C Phospholipases / immunology
  • Type C Phospholipases / pharmacology

Substances

  • Antibodies, Monoclonal
  • Neurotoxins
  • Scorpion Venoms
  • Sodium Channel Blockers
  • Sodium Channels
  • scorpion toxin I, Androctonus
  • Type C Phospholipases