Abstract
The HIV-1 fusion peptide, which is a short hydrophobic peptide from the gp41 coat glycoprotein that participates in the infection of a cell, interacts with model lipid bilayer membranes in a concentration-dependent manner. The interaction of the peptide with the bilayer also strongly depends on the lipid composition. Here, molecular dynamics simulations were performed to investigate lipid-specific interactions that arise shortly after the binding of a less-fusogenic variant of the HIV-1 fusion peptide to a lipid bilayer composed of a mixture of dimyristoyl phosphatidylcholine and dimyristoyl phosphatidylglycerol. The impact of peptide concentration was also studied. An improved understanding was gained of the lipid-specific interactions experienced by the FP. New insight was also gained into how the peptide concentration changes these interactions.
Original language | English |
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Article number | 285 |
Journal | Biomolecules |
Volume | 14 |
Issue number | 3 |
DOIs | |
State | Published - Mar 2024 |
Funding
This research used resources at the Spallation Neutron Source: a DOE Office of Science User Facility operated by the Oak Ridge National Laboratory. This research used resources of the Compute and Data Environment for Science (CADES) at the Oak Ridge National Laboratory, which is supported by the Office of Science of the U.S. Department of Energy under contract No. DE-AC05-00OR22725.
Keywords
- HIV-1
- molecular dynamics simulations
- viral fusion peptide