Biophysical studies of HIV-1 glycoprotein-41 interactions with peptides and small molecules - Effect of lipids and detergents.

ABSTRACT:

Background

The hydrophobic pocket (HP) of HIV-1 glycoprotein-41 ectodomain is defined by two chains of the N-heptad repeat trimer, within the protein-protein interface that mediates 6HB formation. It is a potential target for inhibitors of viral fusion, but its hydrophobic nature and proximity to membrane in situ has precluded ready analysis of inhibitor interactions.

Methods

We evaluated the sensitivity of ¹⁹F NMR and fluorescence for detecting peptide and small molecule binding to the HP and explored the effect of non-denaturing detergent or phospholipid as cosolvents and potential mimics of the membrane environment surrounding gp41.

Results

Chemical shifts of aromatic fluorines were found to be sensitive to changes in the hydrogen bonding network that oc

SUBMITTER: Zhou G 

PROVIDER: S-EPMC7540966 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature