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

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.

• Authors: Lucia Kuhn-Nentwig, Jean Willems, Thomas Seebeck, Tarek Shalaby, Marcel Kaiser, Wolfgang Nentwig
• Journal: Amino acids (Amino Acids) Vol. 40 Issue 1 Pg. 69-76 (Jan 2011) ISSN: 1438-2199 [Electronic] Austria
• PMID: 20140690 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Anti-Infective Agents
• Antimicrobial Cationic Peptides
• Antineoplastic Agents
• Cytotoxins
• Insecticides
• Peptides
• Spider Venoms
• cupiennin 1a

Topics

• Animals
• Anti-Infective Agents (chemistry, pharmacology)
• Antimicrobial Cationic Peptides
• Antineoplastic Agents (chemistry, pharmacology)
• Bacteria (drug effects)
• Cell Line, Tumor
• Cytotoxins (chemistry, pharmacology)
• Drosophila melanogaster (drug effects)
• Humans
• Insecticides (chemistry, pharmacology)
• Molecular Structure
• Parasites (drug effects)
• Peptides (chemistry, pharmacology)
• Spider Venoms (chemistry, pharmacology)
• Spiders (chemistry)