A revolutionary new protein stabilisation technique has been developed by scientists funded by the Biotechnology and Biological Sciences Research Council (BBSRC) which could lead to 30 per cent more proteins being available as potential targets for drug development - opening up exciting possibilities in drug discovery.
Understanding the structure of proteins is a vital first step in developing new drugs, but to date, drug development has been slowed because due to their instability, proteins are difficult to work with in lab conditions. However, using nanoparticles, scientists from the Universities of Birmingham and Warwick have found a way to preserve membrane proteins intact, enabling detailed analysis of their structure and molecular functions.
These new findings, which have just been published online in the Journal of the American Chemical Society, will give scientists access to previously ignored proteins deemed too unstable to work with.
Professor Michael Overduin, from the University of Birmingham, who led the study, explained: "We have shown how a polymer can wrap around and preserve membrane proteins intact in stable nanoparticles. Membrane proteins are the most valuable but technically challenging targets for drug discovery. Finding a gentle solution that preserves their structure and activity, yet is robust enough for experimental interrogation, has eluded scientists for decades, but is now available."
Using a polymer - styrene maleic acid lipid particles (SMALPs), the researchers solubilised a pair of membrane proteins. They found that not only did the proteins maintain their folded structure, binding and enzyme activities in the SMALPs, but also that using the nanoparticles allowed them to be simply and rapidly used for virtually any laboratory analysis.
Advantages of SMALPs over traditional ways to solubilise proteins such as detergents include enhanced stability, activity and spectral quality
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| Contact: Matt Goode press.office@bbsrc.ac.uk 44-179-341-4694 Biotechnology and Biological Sciences Research Council Source:Eurekalert |
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