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 α-helical domains. For structure-function analysis, synthetic peptides were constructed corresponding to these four...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 91; no. 7; pp. 2602 - 2606 |
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Main Authors | , , |
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 | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.91.7.2602 |