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Influence of Phospholipidic Charge on the Interaction of a Multiple Antigenic Peptide from Hepatitis A Virus with Monolayers and Bilayers

✍ Scribed by Mestres, C.; Ortiz, A.; Haro, I.; Reig, F.; Alsina, M. A.


Book ID
127281016
Publisher
American Chemical Society
Year
1997
Tongue
English
Weight
257 KB
Volume
13
Category
Article
ISSN
0743-7463

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several antigenic peptide molecules, or multiple antigenic The interaction of the synthetic multiple antigenic peptide conpeptides (MAP), are more efficient immunogens (3,4), struct MAP 4 -VP1(11-25) with lipid membranes was studied by a partly because they confer some conformational stability to co

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The interaction of the multiple antigenic peptide MAP 4 VP3 with lipid membranes has been studied by spectroscopic techniques. MAP 4 VP3 is a multimeric peptide that corresponds to four units of the sequence 110 -121 of the capsid protein VP3 of hepatitis A virus. In order to evaluate the electrosta

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The synthesis of a VP3(110-121)~HAV peptide was carried out by solid phase methodology. A physicochemical study on the interaction of this peptide with phospholipids involving lipid mono-and bilayers is described. The surface activity of the peptide is indicative of a medium hydrophobic character su

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un arnphiputhic striicfiirr cornhination of@-sheet and a-helix alignedparullel to thP mc.mbrunc sirrficcc, involving the N-terminal rc~sidiies, and pcndruting onlv u short distance into (he h ~,drophohic core. Thc C-tcrminul purl. kiith u comhinufion of @-turn and @-sheet Ttriicture, remains UI thc