A novel HIV-1 gp41 tripartite model for rational design of HIV-1 fusion inhibitors with improved antiviral activity

摘要

Objectives: During HIV-1 fusion process, the N-terminal heptad repeat (NHR) of the HIV-1 glycoprotein 41 (gp41) interacts with the C-terminal heptad repeat (CHR) to form the fusion active six-helix bundle, thus being an effective target for the design of CHR peptide-based HIV-1 fusion inhibitors. To overcome the limitations of the simplified helix wheel model of six-helix bundle, we herein developed a novel HIV-1 gp41 NHRCHR- NHR tripartite model for the rational design of HIV-1 fusion inhibitors with improved antiviral activities.