Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

P. Sospedra, M. Muñoz, M. García, M. A. Alsina, C. Mestres, I. Haro

Research output: Indexed journal article Articlepeer-review

8 Citations (Scopus)


Shorter analogues of a continuous epitope of hepatitis A virus, VP3(110-121) peptide, failed to react with convalescent sera, indicating the importance of the entire peptide in the epitope structure. To better understand the influence of the structural properties of the 12-mer peptide epitope on its biological activity, the interaction of smaller peptide analogues with phospholipid biomembrane models was investigated by a combination of spectroscopic and biophysical techniques. In this article we describe our findings concerning the surface activity and the interaction of peptides with simple mono- and bilayer membranes composed of a zwitterionic phospholipid (dipalmitoyl phosphatidylcholine, DPPC), an anionic phospholipid (dipalmitoyl phosphatidylglicerol, DPPG), or a DPPC/DPPG mixture. The results indicate that the net negative charge of the peptide is in some way responsible of the specific interactions between VP3(110-121) and membrane phospholipids, and necessary to induce β-type conformations upon vesicle interaction.

Original languageEnglish
Pages (from-to)477-488
Number of pages12
Issue number7
Publication statusPublished - Dec 2000
Externally publishedYes


  • Biomembrane models
  • CD
  • Fluorescence
  • Hepatitis A virus
  • Monolayers
  • Synthetic peptides


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