Behaviour of a peptide sequence from the GB virus C/hepatitis G virus E2 protein in Langmuir monolayers: Its interaction with phospholipid membrane models

Silvia Pérez-López, Marina Nieto-Suárez, Concepció Mestres, M. Asunción Alsina, Isabel Haro, Nuria Vila-Romeu

Research output: Indexed journal article Articlepeer-review

15 Citations (Scopus)

Abstract

The GB virus C/hepatitis G virus (GBV C/HGV) is a Flaviviridae member that despite its non pathogenicity, has become of great interest given that it could inhibit the replication of the human immunodeficiency virus (HIV). Therefore, a better knowledge of the virus peptides involved in the cellular membrane fusion mechanism has become our aim. The selected peptide, named E2(347-363), corresponds to the GBV-C/HGV E2 protein and has been synthesized in order to study its interaction with in vitro membrane models. Two phospholipids, varying the charge and the unsaturations of the hydrocarbon chain have been chosen: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DOPG). For our porpoise, we have used the Langmuir monolayer technique and Brewster angle microscopy (BAM) to gain deeper insight into the peptide/lipid interactions. The results obtained allow us to argue in favour of considering E2(347-363) a success candidate for developing further experiments in order to determine its potential role in the GBV C/HGV virus/cell membrane fusion process.

Original languageEnglish
Pages (from-to)153-161
Number of pages9
JournalBiophysical Chemistry
Volume141
Issue number2-3
DOIs
Publication statusPublished - May 2009
Externally publishedYes

Keywords

  • BAM
  • Fusion peptide
  • GBV-C/HGV
  • Hepatitis G
  • Membranes
  • Phospholipid Langmuir monolayers

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