A biophysical characterization of the interaction of a hepatitis C virus membranotropic peptide with micelles
Abstract
Membrane fusion is a highly regulated process that allows enveloped viruses to enter cells and replicate. Viral glycoproteins trigger membrane fusion by means of internal sequences known as fusion peptides. The hepatitis C virus (HCV) genome encodes the envelope glycoproteins E1 and E2, but their specific roles in the fusion step and the localization of the fusion peptide remain uncharacterized. Here, we studied the biophysics of the interactions between the glycoprotein E2 peptide HCV421-445 and four different micellar systems providing ionic, non-ionic and zwitterionic surfaces to investigate the importance of electrostatic interactions for peptide-membrane binding. Circular dichroism, fluorescence spectroscopy and calorimetry were used to characterize peptide-micelle interactions and structural changes. Fluorescence quenching showed that HCV421-445 interacts with SDS or CTAB ionic, n-OGP non-ionic and DPC zwitterionic micelles. The indole ring of Trp seems to anchor the peptide in micelles. Trp residues seem to be more deeply inserted in ionic and non-ionic micelles where peptide interactions are more stable than with DPC zwitterionic micelles. The interaction with zwitterionic micelles appears to occur at the surface. Both ...Continue Reading
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