English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/21935
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Miscibility of Hepatitis A synthetic antigen peptides with lipid monolayers: effect of the amino acid sequence change

AuthorsSospreda, Patricia; Espina, Marta; Alsina, M. Asunción; Haro Villar, Isabel; Mestres, Concepció
KeywordsHepatitis A virus
Synthetic peptides
Lipid monolayers
Electrostatic interactions
Issue Date9-Jan-2003
PublisherElsevier
CitationJournal of Physical Chemistry B - Condensed Phase 107(1): 203-208 (2003)
AbstractInteraction of hepatitis A virus (HAV) with cells during infection and immunological response is not yet well-known. It seems that hydrophobic and electrostatic interactions with the membrane lipids play an important role as well as the RGD triplet located within the (110−121) linear HAV epitope which belongs to the HAV−VP3 structural protein. To obtain more knowledge about these interactions in the present work we have studied the miscibility of two HAV peptides (where the RGD triplet was replaced by RGE and RKD) with three different lipids (dipalmitoylphosphatidylcholine, dipalmitoylphosphatidylglycerol, and stearylamine) through compression isotherms. Both peptides [Lys]113 VP3110 and [Glu]114 VP3110 showed deviations from ideality consistent with miscibility, except in some cases at the collapse pressure. In all cases the interactions were higher with [Glu]114 VP3110. However, these interactions were positive in the majority of cases and then not related with the net charge of the lipid that was different in any case. These results seems to point to the fact that hydrophobic interactions play a major role, even though the compressibility of the peptide should also to be taken into account.
Description6 pages, 9 figures, 4 tables.-- Available online Dec 3, 2002.
Publisher version (URL)http://dx.doi.org/10.1021/jp021459d
URIhttp://hdl.handle.net/10261/21935
DOI10.1021/jp021459d
ISSN1520-6106
E-ISSN1520-5207
Appears in Collections:(IQAC) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.