Design and synthesis of membrane fusion inhibitors against the feline immunodeficiency virus
Autor: | Shinya Oishi, Nobutaka Fujii, Tadafumi S. Tochikura, Hajime Tsujimoto, Masao Matsuoka, Hiroki Nishikawa, Fuminori Mizukoshi, Kazuki Shimane, Yasuyo Kodera, Eiichi Kodama, Hirotaka Kamitani, Hiroaki Ohno, Tsuyoshi Watabe |
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Rok vydání: | 2009 |
Předmět: |
Repetitive Sequences
Amino Acid Feline immunodeficiency virus viruses Clinical Biochemistry Molecular Sequence Data Pharmaceutical Science Immunodeficiency Virus Feline Biochemistry Membrane Fusion Virus Protein Structure Secondary Cell membrane Structure-Activity Relationship Viral Envelope Proteins Viral entry Drug Discovery medicine Animals Amino Acid Sequence Molecular Biology chemistry.chemical_classification biology Organic Chemistry Lipid bilayer fusion biology.organism_classification Virology Heptad repeat medicine.anatomical_structure chemistry Lentivirus Cats Molecular Medicine Glycoprotein Peptides Protein Binding |
Zdroj: | Bioorganicmedicinal chemistry. 17(14) |
ISSN: | 1464-3391 |
Popis: | Feline immunodeficiency virus (FIV) is a pathogenic virus that causes an AIDS-like syndrome in the domestic cats. For viral entry and infection, fusion between the virus and the cell membrane is the critical process and this process is mediated by an envelope glycoprotein gp40. We have identified fusion inhibitory peptides from the heptad repeat-2 (HR2) of gp40. Remodeling of the original sequences using alpha-helix-inducible motifs revealed the interactive residues of gp40. Comparative analysis of HR2 peptides derived from four FIV strains demonstrated that the interactive surface of the Shizuoka strain-derived HR2 peptides provides the highest affinity of all the FIV strains examined. |
Databáze: | OpenAIRE |
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