Deformed proteins kept in line

A joint research group from Tokyo Medical and Dental and Kyoto Universities has developed a simple way to make deformed proteins return to their correct shapes. The new method could open doors to the treatment of disorders such as Alzheimer's disease, which are thought to be caused by abnormally shaped proteins. It appears that cells have specialised proteins, molecular chaperones, that assist them to fold into the correct three-dimensional shape to function properly.

Biochemists are also designing chaperones to boost the yield when synthesising proteins in the lab. This is necessary because at least half the proteins made synthetically fold abnormally and fail to function as desired. The new chaperone is unique in that it can be controlled using light, which greatly simplifies the control process.

It is made from a polymer complex taking a globular structure that naturally envelopes the abnormally folded protein. When this complex is exposed to light, one of its components becomes more water soluble and the complex changes structure, causing the protein to unfold and refold correctly. In a demonstration, the new chaperone molecule helped restore 80% of the protein molecules.