Companies freeze-dry proteins for storage and transport, but risk damaging them at each stage of freeze-drying. Researchers at the University of Oxford have developed a new method for identifying changes to protein structure during a freeze-drying process used by the biopharmaceutical industry to improve the shelf life of therapeutic proteins.
The researchers, led by Professor Zhanfeng Cui and funded through BBSRC’s Bioprocessing Research Industry Club (BRIC), have already used the process to characterise proteins from industry members Novozymes and Lonza plc.
|15||Number of BRIC members in June 2012|
|£13.7M||First phase BRIC funding to 25 projects|
|£10M||Second phase BRIC funding to run five years|
Cui’s aim was to develop a method to observe the behaviour and structure of protein molecules as they were freeze-dried. The researchers first looked at a technique commonly used in chemistry laboratories called Fourier transform infrared spectroscopy (FTIR). Uniquely, they were able to adapt the technique to produce a two-dimensional map of the protein in solution, showing where and how much protein is denatured [changed]. “This is a useful tool, we can do it in liquid, partly-frozen, fully frozen, or dried states, so right through the process,” says Cui.
They then combined FTIR with a modern 3D microscopy method called multi-photon microscopy (MPM). By using both imaging techniques, the researchers could build up a detailed picture of how process conditions affected protein structure during freeze-drying at each stage of the process, making it easier for companies to formulate drugs that can survive freeze-drying intact.
BRIC was established in 2005 by BBSRC, EPSRC and industry to support and develop the UK bioprocessing research community, and enable knowledge transfer between the science and engineering base and industry.
Read the full impact evidence report:
You may need to download additional plug-ins to open this file.