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.
journal_name
Amino Acidsjournal_title
Amino acidsauthors
Kuhn-Nentwig L,Willems J,Seebeck T,Shalaby T,Kaiser M,Nentwig Wdoi
10.1007/s00726-009-0471-0subject
Has Abstractpub_date
2011-01-01 00:00:00pages
69-76issue
1eissn
0939-4451issn
1438-2199journal_volume
40pub_type
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