Protein preservation

A protein stabilisation technique could lead to 30 per cent more proteins being available as potential targets for drug development.

A protein stabilisation technique developed by scientists and funded by the Biotechnology and Biological Sciences Research Council (BBSRC) could lead to 30 per cent more proteins being available as potential targets for drug development.

Understanding the structure of membrane proteins is a vital first step in developing new drugs. However, the lack of a general means of solubilising, stabilising and structurally characterising the proteins has frustrated efforts to understand their mechanisms and exploit their potential value.

However, scientists from Birmingham and Warwick universities have now found a way to preserve membrane proteins intact, enabling detailed analysis of their structure and molecular functions.

Using a lipid containing nanoparticles bounded by styrene maleic acid copolymer, the researchers solubilised a pair of membrane proteins that then maintained their folded structure and properties, allowing them to be used for laboratory analysis.

The method will give scientists access to previously ignored proteins deemed too unstable to work with.

Prof Michael Overduin, from Birmingham University, said: ‘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.’

BBSRC chief executive, Prof Doug Kell, said: ‘The attrition rate in developing new drugs is phenomenal. Only a tiny fraction make it into the clinic to benefit patients. Research such as this that can help to understand the chemical biology of membrane proteins and thereby increase the number of potential targets will mean a larger pipeline for scientists to develop new drugs from and, ultimately more, better drugs for patients.’