A new family of small (4kDa) neurotoxins from the venoms of spiders of the genus Phoneutria

Protein Pept Lett. 2008;15(7):700-8. doi: 10.2174/092986608785133708.

Abstract

A family of 4kDa neurotoxic peptides was purified from venoms of Phoneutria spiders. All have six cysteine residues, and low similarity with other neurotoxins. Three toxins caused moderate inhibition of L-type Ca(2+) channels. The structure of toxin PRTx27C3 was modeled and compared with toxin ADO1. The importance of four residues is suggested.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium Channel Blockers / chemistry
  • Calcium Channel Blockers / isolation & purification
  • Calcium Channel Blockers / toxicity
  • Calcium Channels, L-Type / drug effects
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Neurotoxins / chemistry*
  • Neurotoxins / genetics
  • Neurotoxins / isolation & purification
  • Neurotoxins / toxicity
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Electrospray Ionization
  • Spider Venoms / chemistry*
  • Spider Venoms / genetics
  • Spider Venoms / isolation & purification
  • Spider Venoms / toxicity
  • Spiders / chemistry*
  • Spiders / genetics

Substances

  • Calcium Channel Blockers
  • Calcium Channels, L-Type
  • Neurotoxins
  • Spider Venoms