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Cupiennin 1d*: the cytolytic activity depends on the hydrophobic N‐terminus and is modulated by the polar C‐terminus
Author(s) -
Kuhn-Nentwig Lucia,
Dathe Margitta,
Walz Alfred,
Schaller Johann,
Nentwig Wolfgang
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03219-2
Subject(s) - drosophila melanogaster , peptide , amphiphile , chemistry , lytic cycle , cytolysis , biophysics , biochemistry , microbiology and biotechnology , c terminus , n terminus , polar , biological activity , peptide sequence , amino acid , biology , cytotoxicity , in vitro , immunology , virus , organic chemistry , copolymer , gene , polymer , physics , astronomy
To investigate structural features modulating the biological activity of cupiennin 1 peptides from the spider Cupiennius salei , three truncated cupiennin 1d analogs were synthesized. The fact that their growth inhibiting effect on Gram‐negative and Gram‐positive bacteria, their lytic activity with human red blood cells and their insecticidal effect on Drosophila melanogaster correlates with structural properties shows that the hydrophobic N‐terminal chain segment includes the major determinants of structure and activity. The polar C‐terminus seems to modulate peptide accumulation at negatively charged cell surfaces via electrostatic interactions and has no important effect on the peptides’ amphipathic secondary structure.