New insight into HIV
Joint research from NPL, the University of Edinburgh, IBM's Watson Research Center and Diamond Light Source provides new insight into a fusion protein that enables HIV to infect host cells.
The research team probed the structural changes that occur in two peptide fragments of a fusion protein, known as gp41, in HIV-1. The protein helps the virus gain entry into a host cell and infect it.
With a better understanding of the mechanisms of the fusion protein, drug developers can begin to target weaknesses within it, and eventually manufacture drugs that prevent HIV from infecting healthy cells.
In this project, one of the 'beamlines' at the Diamond Light Source synchrotron facility in Oxfordshire was used to obtain a detailed picture of how these peptide fragments may behave in membrane environments. Proteins are sequences of amino acids known as primary structures. The two peptide fragments studied here are widely separated in the primary structure of the fusion protein but make contact when the viral and host cell membranes come together. One peptide fragment is attached to the viral membrane, and the other anchors itself to the human cell membrane.
The contacts between the peptides are dynamic and provide evidence for a regulatory mechanism of HIV fusion which can be further investigated in the design of inhibitors that prevent the fusion process. Such inhibitors could potentially form the basis of new antiretroviral drugs to treat people with AIDS.
This research is a part of the NPL-led international research project Multi-scale measurements in biophysical system, which is jointly funded by the NPL Strategic Research programme and the Scottish Universities Physics Alliance.
The full research article, Membrane mediated regulation in free peptides of HIV-1 gp41: minimal modulation of the hemifusion phase, was published in Physical Chemistry Chemical Physics - the Royal Society of Chemistry's premier forum for physical chemistry research.
For further information, please contact Max Ryadnov.