title: Self-assembling peptide nanotubes with antiviral activity against hepatitis C virus.
abstract: Hepatitis C virus (HCV) infects chronically 3% of the world population and the current therapy against this pathogen is only partially effective. With the aim of developing novel antiviral strategies against HCV, we screened a D,L-α-peptide library using an unbiased methodology based on a cell culture infection system for HCV. We found a family of highly active amphiphilic eight-residue cyclic D,L-α-peptides that specifically blocked entry of all tested HCV genotypes into target cells at a postbinding step without affecting infection by other enveloped RNA viruses. Structure-activity relationship studies indicate that antiviral activity was dependent on cyclic D,L-α-peptide self-assembly processes and that, although they possess a net neutral charge, they display a characteristic charge distribution. Our results indicate that supramolecular amphiphilic peptide structures constitute a class of highly selective HCV entry inhibitors.
authors: Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037, USA.
authors: Ana
authors: A
authors: Montero
authors: Pablo
authors: P
authors: Gastaminza
authors: Mansun
authors: M
authors: Law
authors: Guofeng
authors: G
authors: Cheng
authors: Francis V
authors: FV
authors: Chisari
authors: M Reza
authors: MR
authors: Ghadiri
mesh_terms: D000595:Amino Acid Sequence; D000998:Antiviral Agents / Q000494:pharmacology*; D045744:Cell Line, Tumor; D016174:Hepacivirus / Q000187:drug effects*; D006801:Humans; D045333:Nanotubes, Peptide / Q000737:chemistry*; D019151:Peptide Library; D012367:RNA, Viral / Q000032:analysis; D013329:Structure-Activity Relationship; D014779:Virus Replication / Q000187:drug effects
chemical_list: D000998:Antiviral Agents; D045333:Nanotubes, Peptide; D019151:Peptide Library; D012367:RNA, Viral