Cupiennin 1d*: the cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus.
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.
Kuhn-Nentwig
Lucia
L
Zoological Institute, University of Bern, Baltzerstrasse 6, CH-3012, Bern, Switzerland. lucia.kuhn@zos.unibe.ch
Dathe
Margitta
M
Walz
Alfred
A
Schaller
Johann
J
Nentwig
Wolfgang
W
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D002942:Circular Dichroism; D004331:Drosophila melanogaster / Q000187:drug effects; D004353:Drug Evaluation, Preclinical / Q000379:methods; D004912:Erythrocytes / Q000187:drug effects; D006460:Hemolysin Proteins / Q000737:chemistry / Q000494:pharmacology; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D007306:Insecticides / Q000737:chemistry / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013111:Spider Venoms / Q000737:chemistry* / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D006460:Hemolysin Proteins; D007306:Insecticides; D013111:Spider Venoms; C467055:cupiennin 1D, Cupiennius salei