Selected article for: "helix bundle and heptad repeat"
Author: Ni, Ling; Gao, George F.; Tien, Po
Title: Rational design of highly potent HIV-1 fusion inhibitory proteins: Implication for developing antiviral therapeutics
  • Cord-id: lqioamh6
  • Document date: 2005_7_8
    • ID: lqioamh6
    Snippet: Recombinant protein containing one heptad-repeat 1 (HR1) segment and one HR2 segment of the HIV-1 gp41 (HR1–HR2) has been shown to fold into thermally stable six-helix bundle, representing the fusogenic core of gp41. In this study, we have used the fusogenic core as a scaffold to design HIV-1 fusion inhibitory proteins by linking another HR1 to the C terminus of HR1–HR2 (HR121) or additional HR2 to the N terminus of HR1–HR2 (HR212). Both recombinant proteins could be abundantly and solubly
    Document: Recombinant protein containing one heptad-repeat 1 (HR1) segment and one HR2 segment of the HIV-1 gp41 (HR1–HR2) has been shown to fold into thermally stable six-helix bundle, representing the fusogenic core of gp41. In this study, we have used the fusogenic core as a scaffold to design HIV-1 fusion inhibitory proteins by linking another HR1 to the C terminus of HR1–HR2 (HR121) or additional HR2 to the N terminus of HR1–HR2 (HR212). Both recombinant proteins could be abundantly and solubly expressed and easily purified, exhibiting high stability and potent inhibitory activity on HIV-1 fusion with IC(50) values of 16.2 ± 2.8 and 2.8 ± 0.63 nM, respectively. These suggest that these rationally designed proteins can be further developed as novel anti-HIV-1 therapeutics.

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