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Cupiennin 1d*: the cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus.

  • 2002-09-11
Published in:
  • FEBS letters. - 2002
Amino Acid Sequence
Animals
Anti-Bacterial Agents
Antimicrobial Cationic Peptides
Circular Dichroism
Drosophila melanogaster
Drug Evaluation, Preclinical
Erythrocytes
Hemolysin Proteins
Hemolysis
Humans
Insecticides
Microbial Sensitivity Tests
Molecular Sequence Data
Protein Conformation
Spider Venoms
Structure-Activity Relationship
English 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.
Language
  • English
Open access status
bronze
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Persistent URL
https://folia.unifr.ch/global/documents/143749
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