tailieunhanh - Báo cáo khoa học: Interaction of synthetic peptides corresponding to hepatitis G virus (HGV/GBV-C) E2 structural protein with phospholipid vesicles

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. | iFEBS Journal Interaction of synthetic peptides corresponding to hepatitis G virus HGV GBV-C E2 structural protein with phospholipid vesicles Cristina Larios1 2 Bart Christiaens3 M. Jose Gomara1 M. Asuncion Alsina2 and Isabel Haro1 1 Department of Peptide and Protein Chemistry IIQAB-CSIC Barcelona Spain 2 Associated Unit CSIC Department of PhysicalChemistry Faculty of Pharmacy University of Barcelona Spain 3 Laboratory of Lipoprotein Chemistry Department of Biochemistry Ghent University Belgium Keywords circular dichroism fluorescence assays hepatitis G virus HGV GBV-C lipid vesicles synthetic peptides Correspondence I. Haro Department of Peptide and Protein Chemistry IIQAB-CSIC Jordi Girona 18-26 08034 Barcelona Spain Fax 34 9320 45904 Tel 34 9340 06109 E-mail ihvqpp@ Received 25 February 2005 revised 8 March 2005 accepted 17 March 2005 doi 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 a-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. The hepatitis G virus HGV and the GB virus C GBV-C are strain variants of a recently discovered enveloped RNA virus belonging to the Flaviviridae

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