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.

journal_name

Amino Acids

journal_title

Amino acids

authors

Kuhn-Nentwig L,Willems J,Seebeck T,Shalaby T,Kaiser M,Nentwig W

doi

10.1007/s00726-009-0471-0

subject

Has Abstract

pub_date

2011-01-01 00:00:00

pages

69-76

issue

1

eissn

0939-4451

issn

1438-2199

journal_volume

40

pub_type

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