Interaction of synthetic peptides corresponding to hepatitis G virus (HGV/GBV‐C) E2 structural protein with phospholipid vesicles

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Abstract
The interaction with phospholipid bilayers of two synthetic peptides with sequences corresponding to a segment next to the native N‐terminus and an internal region of the E2 structural hepatitis G virus (HGV/GBV‐C) protein [E2(7–26) and E2(279–298), respectively] has been characterized. Both peptides are water soluble but associate spontaneously with bilayers, showing higher affinity for anionic than zwitterionic membranes. However, whereas the E2(7–26) peptide is hardly transferred at all from water to the membrane interface, the E2(279–298) peptide is able to penetrate into negatively charged bilayers remaining close to the lipid/water interface. The nonpolar environment clearly induces a structural transition in the E2(279–298) peptide from random coil to α‐helix, which causes bilayer perturbations leading to vesicle permeabilization. The results indicate that this internal segment peptide sequence is involved in the fusion of HGV/GBV‐C to membrane.