Cytolytic and Antibacterial Activity of Synthetic Peptides Derived from Amoebapore, the Pore-Forming Peptide of Entamoeba histolytica

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 91; no. 7; pp. 2602 - 2606
• Main Authors: Leippe, Matthias, Andra, Jorg, Muller-Eberhard, Hans J.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 29.03.1994; National Acad Sciences; National Academy of Sciences
• Subjects: Amino Acid Sequence; Amino acids; Animals; Anti-Bacterial Agents - pharmacology; Antibacterials; Bacteria; Bacteria - drug effects; Bacteriology; Biochemistry; Biochemistry. Physiology. Immunology. Molecular biology; Biological and medical sciences; Cell membranes; Entamoeba histolytica; Entamoeba histolytica - chemistry; Entamoeba histolytica - pathogenicity; Erythrocytes - drug effects; Escherichia coli; Eukaryotic cells; Fundamental and applied biological sciences. Psychology; Hemolysis; Invertebrates; Ion Channels; Membrane Proteins - pharmacology; Membrane Proteins - toxicity; Molecular Sequence Data; Molecules; Peptide Fragments - chemical synthesis; Peptide Fragments - pharmacology; Peptide Fragments - toxicity; Phospholipids; Protozoa; Protozoan Proteins - pharmacology; Protozoan Proteins - toxicity; Sequencing; Structure-Activity Relationship; T lymphocytes; Protozoa; Cytolysis; Peptides; Structure activity relation; Pathogenic; Parasite; Rhizoflagellata; Entamoeba histolytica; Membrane pore; Antibacterial agent
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.91.7.2602

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 α-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 α-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 α-helix of amoebapore and the C-terminal hexapeptide of melittin from the venom of Apis mellifera.