Liposome-induced conformational changes of an epitopic peptide and its palmitoylated derivative of influenza virus hemagglutinin.
The conformation of synthetic HA317-329-NH2 representing the major B- and T-cell epitopic region of influenza virus hemagglutinin, its palmitoylated derivative (HA317-329-Thr(Pal)-NH2), and the intersubunit peptide (HA317-341-NH2) comprising also the fusion peptide, were studied in aqueous buffer and in the presence of neutral and negatively charged liposomes. The free peptide is unordered in aqueous solution, even in the presence of liposomes. However, grafting the palmitic acid or the fusion peptide onto the C-terminus of the peptide enables the hydrophilic HA317-329 to adopt folded (turn) and beta-strand structure on the surface of neutral and negatively charged liposomes, respectively. The results emphasize the importance of some kind of anchor for achieving a specific conformation of epitopic peptide HA317-329-NH2 on the surface of liposomes.
Institute of Biophysics, Biological Research Center, Szeged, Hungary.
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Laczkó
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Hollósi
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Vass
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GK
Tóth
D006388:Hemagglutinins / Q000737:chemistry* / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry* / Q000378:metabolism; D009975:Orthomyxoviridae / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
D006388:Hemagglutinins; D008081:Liposomes; D014764:Viral Proteins