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Cytolytic and K+ channel blocking activities of β-KTx and scorpine-like peptides purified from scorpion venoms

  • E. Diego-García
  • Y. Abdel-Mottaleb
  • E. F. Schwartz
  • R. C. Rodríguez de la Vega
  • J. Tytgat
  • L. D. Possani
Research Article

Abstract.

Among the scorpion venom components whose function are poorly known or even show contrasting pharmacological results are those called “orphan peptides”. The most widely distributed are named β-KTx or scorpine-like peptides. They contain three disulfide bridges with two recognizable domains: a freely moving N-terminal amino acid sequence and a tightly folded C-terminal region with a cysteine-stabilized α/β (CS-αβ) motif. Four such peptides and three cloned genes are reported here. They were assayed for their cytolytic, antimicrobial and K+ channel-blocking activities. Two main characteristics were found: the existence of an unusual structural and functional diversity, whereby the full-length peptide can lyse cells or kill microorganisms, and a C-terminal domain containing the CS-αβ motif that can block K+ channels. Furthermore, sequence analyses and phylogenetic reconstructions are used to discuss the evolution of this type of peptide and to highlight the versatility of the CS-αβ structures.

Keywords.

Cysteine-stabilized α/β-motif cytolytic peptides DNA cloning gene topology K+ channel blocker scorpion toxin sequence analysis 

Copyright information

© Birkhaueser 2007

Authors and Affiliations

  • E. Diego-García
    • 1
  • Y. Abdel-Mottaleb
    • 2
  • E. F. Schwartz
    • 1
    • 3
  • R. C. Rodríguez de la Vega
    • 1
  • J. Tytgat
    • 2
  • L. D. Possani
    • 1
  1. 1.Departamento de Medicina Molecular y Bioprocesos, Instituto de BiotecnologiaUniversidad Nacional Autonoma de MexicoCuernavacaMexico
  2. 2.Laboratory of ToxicologyUniversity of LeuvenLeuvenBelgium
  3. 3.Laboratório de Toxinologia, Departamento de Ciências FisiológicasUniversidade de BrasíliaBrasíliaBrazil

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