Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells
Autor: | Marcel Kaiser, Lucia Kuhn-Nentwig, Thomas Seebeck, Tarek Shalaby, Jean Willems, Wolfgang Nentwig |
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Rok vydání: | 2009 |
Předmět: |
Insecticides
Clinical Biochemistry Spider Venoms Peptide Venom Antineoplastic Agents 580 Plants (Botany) Biology Proteomics Biochemistry Stereospecificity Anti-Infective Agents Cell Line Tumor 540 Chemistry Animals Humans Parasites chemistry.chemical_classification Bacteria Molecular Structure Cytotoxins Organic Chemistry Spiders biology.organism_classification Cupiennius salei Cytolysis Drosophila melanogaster chemistry Cancer cell 570 Life sciences biology 590 Animals (Zoology) Peptides Antimicrobial Cationic Peptides |
Zdroj: | Kuhn-Nentwig, Lucia; Willems, Jean; Seebeck, Thomas; Shalaby, Tarek; Kaiser, Marcel; Nentwig, Wolfgang (2011). Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells. Amino acids, 40(1), pp. 69-76. Wien: Springer Vienna 10.1007/s00726-009-0471-0 |
ISSN: | 1438-2199 |
DOI: | 10.1007/s00726-009-0471-0 |
Popis: | 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. |
Databáze: | OpenAIRE |
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