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Título

Analysis of the differential conformational behavior of two antigens of the hepatitis A virus through molecular dynamics and physicochemical measurements

AutorCantó, Josep; Haro Villar, Isabel; Alsina, M. Asunción; Pérez, Juan J.
Palabras claveHepatitis A virus
Synthetic peptides
Stables monolayers
Fecha de publicación12-jun-2003
EditorAmerican Chemical Society
CitaciónJournal of Physical Chemistry B - Condensed Phase 107(27): 6603-6608 (2003)
ResumenThe surface activity of peptides with proven antigenic activity toward the hepatitis A virus (HAV), [Glu114]VP3(110−121) and [Lys113]VP3(110−121), analogues of the VP3(110−121) antigen of HAV with sequence FWRGDLVFDFQV, was deduced from compression isotherm experiments. The results showed that the lysine analogue exhibits a surface area about three times smaller than that of the glutamic acid analogue. To understand whether this observed differential conformational behavior of the two peptide analogues is a characteristic feature of the peptide sequences, we carried out 10 ns molecular dynamics simulations of the two analogues in water. The results of this study confirm a differential conformational behavior of the two peptides and provide support to the hypothesis of this observed behavior as the reason for the different surface areas obtained from compression isotherm experiments.
Descripción6 pages, 7 figures, 2 tables.-- Printed version published Jul 10, 2003.
Versión del editorhttp://dx.doi.org/10.1021/jp022556+
URIhttp://hdl.handle.net/10261/21940
DOI10.1021/jp022556+
ISSN1520-6106 (Print)
1520-5207 (Online)
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