Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.
The pore-forming peptide amoebapore is considered part of the cytolytic armament of pathogenic Entamoeba histolytica. Amoebapore is composed of 77 amino acid residues arranged in four alpha-helical domains. For structure-function analysis, synthetic peptides were constructed corresponding to these four domains: H1 (residues 1-22), H2 (25-39), H3 (40-64), and H4 (67-77). The peptides H1 and H3, representing two highly amphipathic alpha-helical regions of amoebapore, possessed pore-forming activity. Peptide H3 displayed cytolytic and antibacterial functions similar to those of natural amoebapore. The most potent antibacterial activity and the broadest activity spectrum were expressed by H1-Mel, a hybrid molecule composed of the N-terminal alpha-helix of amoebapore and the C-terminal hexapeptide of melittin from the venom of Apis mellifera.
Leippe
M
M
Department of Molecular Biology, Bernhard Nocht Institute for Tropical Medicine, Hamburg, Federal Republic of Germany.
Andrä
J
J
Müller-Eberhard
H J
HJ
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects*; D004748:Entamoeba histolytica / Q000737:chemistry* / Q000472:pathogenicity; D004912:Erythrocytes / Q000187:drug effects*; D006461:Hemolysis; D007473:Ion Channels; D008565:Membrane Proteins / Q000494:pharmacology* / Q000633:toxicity; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology* / Q000633:toxicity; D015800:Protozoan Proteins / Q000494:pharmacology* / Q000633:toxicity; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D007473:Ion Channels; D008565:Membrane Proteins; D010446:Peptide Fragments; D015800:Protozoan Proteins; C041670:amoebapore proteins, protozoan