Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/21935
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Miscibility of Hepatitis A synthetic antigen peptides with lipid monolayers: effect of the amino acid sequence change |
Autor: | Sospedra, Patricia; Espina, Marta; Alsina, M. Asunción CSIC; Haro Villar, Isabel CSIC ORCID ; Mestres, Concepció | Palabras clave: | Hepatitis A virus Synthetic peptides Lipid monolayers Electrostatic interactions |
Fecha de publicación: | 9-ene-2003 | Editor: | Elsevier | Citación: | Journal of Physical Chemistry B - Condensed Phase 107(1): 203-208 (2003) | Resumen: | Interaction 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. | Descripción: | 6 pages, 9 figures, 4 tables.-- Available online Dec 3, 2002. | Versión del editor: | http://dx.doi.org/10.1021/jp021459d | URI: | http://hdl.handle.net/10261/21935 | DOI: | 10.1021/jp021459d | ISSN: | 1520-6106 | E-ISSN: | 1520-5207 |
Aparece en las colecciones: | (IQAC) Artículos |
Mostrar el registro completo
CORE Recommender
SCOPUSTM
Citations
2
checked on 16-abr-2024
WEB OF SCIENCETM
Citations
2
checked on 29-feb-2024
Page view(s)
347
checked on 17-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.