Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi

FEBS Lett. 2016 Jul;590(14):2286-96. doi: 10.1002/1873-3468.12255. Epub 2016 Jun 30.

Abstract

Scorpine-like peptides are two domain peptides found in different scorpion venoms displaying various antimicrobial, cytolytic, and potassium channel-blocking activities. The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine-like peptide from the venom of Hoffmannihadrurus gertschi. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel-blocking and antiparasitic activities. Our results are important to rationalize the structure-function relationships of a pharmacologically versatile molecular scaffold.

Keywords: Hoffmannihadrurus gertschi (previously Hadrurus gertschi); KTx potassium channel-blocking toxin; antiparasitic; scorpine; solution structure NMR and HgeD.

Publication types

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

MeSH terms

  • Animals
  • Antiparasitic Agents / chemistry*
  • Antiparasitic Agents / pharmacology
  • Arthropod Proteins / chemistry*
  • Arthropod Proteins / pharmacology
  • Peptides / chemistry*
  • Peptides / pharmacology
  • Protein Structure, Secondary
  • Scorpion Venoms / chemistry*
  • Scorpion Venoms / pharmacology
  • Scorpions / chemistry*
  • Taenia / growth & development

Substances

  • Antiparasitic Agents
  • Arthropod Proteins
  • Peptides
  • Scorpion Venoms