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

Abstract:

: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 this 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 beta-type conformations upon vesicle interaction.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Sospedra P,Muñoz M,García M,Alsina MA,Mestres C,Haro I

doi

10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.C

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

477-88

issue

7

eissn

0006-3525

issn

1097-0282

pii

10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.C

journal_volume

54

pub_type

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