Contact
    Start Publications Mechanism of an Amphipathic a-Helical Peptide’s Antiviral ...
    ←  Publication Finder
    QSense

    Mechanism of an Amphipathic a-Helical Peptide’s Antiviral Activity Involves Size-Dependent Virus Particle Lysis

    Year: 2009

    Journal: ACS Chem. Biol., 2009, 4 (12), pp 1061–1067, 20100827

    Authors: Cho N-J. †, Dvory-Sobol H. †, Xiong A. †, Cho S-J., Frank C.W. §, Glenn J.S. †‡*

    Last authors: Jeffrey S. Glenn

    Organizations: † Department of Medicine, Division of Gastroenterology and Hepatology, Stanford University School of Medicine ‡ Palo Alto Veterans Administration § Department of Chemical Engineering, Stanford University, Stanford, California 94305 Park Systems Corp., Suwon, Korea

    Country: USA, US, United States of America

    The N-terminal region of the hepatitis C virus (HCV) nonstructural protein NS5A contains an amphipathic α-helix that is necessary and sufficient for NS5A membrane association. A synthetic peptide (AH) comprising this amphipathic helix is able to lyse lipid vesicles that serve as a model system for virus particles. Based on quartz crystal microbalance-dissipation (QCM-D) experiments, the degree of vesicle rupturing was found to be inversely related to vesicle size, with maximal activity in the size range of several medically important viruses. In order to confirm and further study vesicle rupture, dynamic light scattering (DLS) and atomic force microscopy (AFM) experiments were also performed. The size dependence of vesicle rupturing helps explain the peptide’s observed effect on the infectivity of a wide range of viruses. Further, in vitro studies demonstrated that AH peptide treatment significantly decreased the infectivity of HCV particles. Thus, the AH peptide might be used to rupture HCV particles extra-corporally (for HCV prevention) and within infected individuals (for HCV therapy).