Dimeric Ankyrin with Inverted Module Promotes Bifunctional Property in Capturing Capsid to Impede HIV-1 Replication.

ABSTRACT: Several anti-HIV scaffolds have been proposed as complementary treatments to highly active antiretroviral therapy. Ank^GAG1D4, a designed ankyrin repeat protein, formerly demonstrated anti-HIV-1 replication by interfering with HIV-1 Gag polymerization. However, the improvement of the effectiveness was considered. Recently, the dimeric molecules of Ank^GAG1D4 were accomplished in enhancing the binding activity against HIV-1 capsid (CAp24). In this study, the interaction of CAp24 against the dimer conformations was elucidated to elaborate the bifunctional property. The accessibility of the ankyrin binding domains was inspected by bio-layer interferometry. By inverting the second module of dimeric ankyrin (Ank^GAG1D4_NC-CN), the CAp24 interaction K

SUBMITTER: Juntit OA 

PROVIDER: S-EPMC10048781 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature