Although diseases caused by prions are very rare, until recently they were all fatal. Together with a team of biochemists, I changed that. After almost 15 years of research full of setbacks, we have managed to synthesize a molecular machine that can recognize a prion and then render it harmless. This method relies on enclosing the prion protein with a network polymer. This prevents the prion from misfolding other proteins. In addition, we have succeeded in making the mutated PRNP gene inactive and using gene therapy to insert a healthy gene into the DNA so that no new prions are made during protein synthesis. These developments enable us to combat an early stage prion disease in a very effective manner.

The biggest challenge of our research was to differentiate between the normal PrP proteins and the prions. After all, no normal PrP proteins should be inactivated. After years of research in the lab, we finally managed to develop a molecular machine that can distinguish between the tertiary structure of a PrP protein and that of a prion in cattle. Not much later we also managed to treat a prion disease (vCJD, variant Creutzveldt-Jacob disease) in a human. Someone who actually only had a few months to live could now pick up her life again.

I would have liked our research to have been completed earlier, due to a lack of financial resources this was not possible. However, I am satisfied with our result. Diseases such as Creutzveldt-Jacob disease and Fatal Familial Insomnia (fatal insomnia) can now be treated at an early stage. Dozens of people are cured every year with this method.