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Conformational behavior of the HAV‐VP3(110–121) peptidic sequence and synthetic analogs in membrane environments studied by CD and computational methods
Author(s) -
Pérez José A.,
Cantó Josep,
Reig Francisca,
Pérez Juan J.,
Haro Isabel
Publication year - 1998
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199806)45:7<479::aid-bip2>3.0.co;2-l
Subject(s) - chemistry , sequence (biology) , membrane , biophysics , stereochemistry , biochemistry , biology
The present study was undertaken to examine the structural features that may be important to explain the immunogenicity of the (110–121) peptide sequence (FWRGDLVFDFQV) of VP3 capsid protein of hepatitis A virus. A conformational analysis of the preferred conformations by CD and molecular mechanics was carried out. Present results suggest that the interaction with liposomes as biomembrane model induces and stabilizes the amphipathic β‐structure of the peptide. To study the contribution of amino acid replacements at the RGD tripeptide as well as the influence of the peptide chain length on peptide conformation, solid‐phase peptide synthesis of several peptide analogs was carried out and the peptide conformation was studied using CD spectroscopy. The results show that the RGD sequence is necessary to induce the β‐structure in the presence of liposomes. © 1998 John Wiley & Sons, Inc. Biopoly 45: 479–492, 1998