Antiviral activity of α-helical stapled peptides designed from the HIV-1 capsid dimerization domain.

ABSTRACT:

Background

The C-terminal domain (CTD) of HIV-1 capsid (CA), like full-length CA, forms dimers in solution and CTD dimerization is a major driving force in Gag assembly and maturation. Mutations of the residues at the CTD dimer interface impair virus assembly and render the virus non-infectious. Therefore, the CTD represents a potential target for designing anti-HIV-1 drugs.

Results

Due to the pivotal role of the dimer interface, we reasoned that peptides from the α-helical region of the dimer interface might be effective as decoys to prevent CTD dimer formation. However, these small peptides do not have any structure in solution and they do not penetrate cells. Therefore, we used the hydrocarbon stapling technique to stabilize the α-helical structure and confirmed by confoc

SUBMITTER: Zhang H 

PROVIDER: S-EPMC3097154 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature