Week 6: Prion Disease

 As we’ve learned in our previous science classes, and in the Susan Lindquist lecture, proteins are capable of folding in an infinite number of ways. Proteins contain chains of nucleic acids and thus can have infinite combinations – by folding in a certain way, the protein can give us haemoglobin; by folding using a different set of combinations, we get the Prion protein.

Thus I found this weeks materials fascinating – it seems that the way a protein folds is its identity. Thus by impacting the molecular folding of the Prion protein, this disease has a profound biological consequence which makes this disease so hard to cure. The research from Zurich is so important because it identifies a specific part of the prion protein, namely the tail, that induces death. By isolating a specific part of the protein, we have a better idea of where to focus research. Thus the hypothesis of binding the ‘flexible tail’ with antibodies in order to stop death is worth investigating.

While these new discoveries are paramount for finding a cure, we need to still keep in mind that these experiments were conducted on animals (mice). As animal brains are very different from humans, we cannot be sure that what works with mice will work with humans. Nonetheless, this is certainly a big step in the right direction and I look forward to seeing what results such research yields.