Amino Acids

, Volume 40, Issue 1, pp 69–76

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

  • Lucia Kuhn-Nentwig
  • Jean Willems
  • Thomas Seebeck
  • Tarek Shalaby
  • Marcel Kaiser
  • Wolfgang Nentwig
Original Article

DOI: 10.1007/s00726-009-0471-0

Cite this article as:
Kuhn-Nentwig, L., Willems, J., Seebeck, T. et al. Amino Acids (2011) 40: 69. doi:10.1007/s00726-009-0471-0

Abstract

Cupiennin 1a, a cytolytic peptide isolated from the venom of the spider Cupiennius salei, exhibits broad membranolytic activity towards bacteria, trypanosomes, and plasmodia, as well as human blood and cancer cells. In analysing the cytolytic activity of synthesised all-d- and all-l-cupiennin 1a towards pro- and eukaryotic cells, a stereospecific mode of membrane destruction could be excluded. The importance of negatively charged sialic acids on the outer leaflet of erythrocytes for the binding and haemolytic activity of l-cupiennin 1a was demonstrated. Reducing the overall negative charges of erythrocytes by partially removing their sialic acids or by protecting them with tri- or pentalysine results in reduced haemolytic activity of the peptide.

Keywords

Cupiennin 1a M-ctenitoxin-Cs1a Spider Cupiennius salei Cytolytic activity Cancer cells Protozoan parasites Non-stereospecificity 

Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Lucia Kuhn-Nentwig
    • 1
  • Jean Willems
    • 2
  • Thomas Seebeck
    • 3
  • Tarek Shalaby
    • 4
  • Marcel Kaiser
    • 5
  • Wolfgang Nentwig
    • 1
  1. 1.Institute of Ecology and EvolutionUniversity of BernBernSwitzerland
  2. 2.Department of Medicine Laboratory of BiochemistryInterdisciplinary Research Centre, K.U. LeuvenKortrijkBelgium
  3. 3.Institute of Cell BiologyUniversity of BernBernSwitzerland
  4. 4.Children’s Hospital ZürichUniversity Children’s ClinicZurichSwitzerland
  5. 5.Swiss Tropical InstituteBaselSwitzerland

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