The grant worth in excess of £350,000 will fund a project involving the measurement of ultrafast excited state chemistry in newly discovered ‘second generation’ photoactive proteins, their mutants and in a series of synthetic analogs of the fluorescent protein chromophore.  The project is a collaboration between the ultrafast spectroscopy group of Steve Meech and the synthesis group of Prof Phil Page, with input from biophysics and protein scientists in Japan and the USA.

The first generation of fluorescent proteins, based around the Green Fluorescent Protein (GFP), was responsible for revolutionary advances in bioimaging. The second generation are photoactive proteins. The first examples exhibit photoswitching – the capacity to change their optical properties, but mutant forms may exhibit a variety of photo-induced structural changes, photoreactivity, etc.; the range of potential applications for such spatially localised photoaddressable proteins in living cells is enormous. Some of the new proteins may exhibit phototoxicity, permitting the selective destruction of cells expressing the photoprotein. Other examples might include spatially localised drug release due to photoinduced structure changes, allowing drugs to be delivered to specific cells in the body.