David Needham, Duke University engineer and chemist, recently developed a process that dries proteins by turning them into glassy microbeads. The transformation occured when Needham's team used a micropipette to release droplets of water-dissolved protein into decanol, an organic solvent.
When water was restored to glassified test proteins, the proteins retained all or most of their original activity. The water that remained in the microbeads was not enough to allow bacteria or fungi to grow. These results suggest that glassification could be a good way to preserve biopharmaceuticals.The microbeads are not as viscous as lyophilized proteins, so they are unlikely to clog syringes, according to Needham's research. Also, like multiparticulates, the glassified proteins potentially could be covered with polymers for delayed release.
The glassification process takes minutes, while lyophilization sometimes takes days. The new process is cheaper than lyophilization, too, because it requires no specialized equipment.
If Needham's technique can work well in an industrial setting, it could save biopharmaceutical manufacturers money without harming proteins or posing risks to patients. Lyophilization is not the best process for every protein, but, thanks to Needham's team, the industry could soon have another trick up its sleeve.