Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Leippe M,Andrä J,Müller-Eberhard HJdoi
10.1073/pnas.91.7.2602subject
Has Abstractpub_date
1994-03-29 00:00:00pages
2602-6issue
7eissn
0027-8424issn
1091-6490journal_volume
91pub_type
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