Cupiennin 1d*: the cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus
Abstract
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.
- Publication:
-
FEBS Letters
- Pub Date:
- September 2002
- DOI:
- 10.1016/S0014-5793(02)03219-2
- Bibcode:
- 2002FEBSL.527..193K
- Keywords:
-
- Antimicrobial peptide;
- Bactericidal activity;
- Cupiennin 1;
- Hemolysis;
- Insecticidal activity;
- Cupiennius salei;
- CD;
- circular dichroism;
- ESI-MS;
- electrospray ionization mass spectrometry;
- Fmoc;
- 9-fluorenylmethoxy-carbonyl;
- H;
- hydrophobicity;
- POPC;
- 1-palmitoyl-2-oleoyl phosphatidylcholine;
- POPG;
- 1-palmitoyl-2-oleoyl phosphatidyl-DL-glycerol;
- SUVs;
- small unilamellar vesicles;
- TFE;
- trifluoroethanol;
- cupiennin*;
- synthesized cupiennin