Folding of proteins in neurodegenerative diseases
Abstract
In Alzheimer’s diesease and Parkinson’s disease it is known that the proteins amyloid beta and alpha synuclein aggregates and that this causes the disease. Previously it have been thought that the big aggregates causes the disease, but now a lot point to that is is the small oligomers that are the most neurotoxic. Very little is known about these smaller oligomers and since they are just an intermediate in the aggregation process it is difficult to analyse them. A lot of knowledge about the disease could be learned if one can create a stable oligomeric amyloid beta and alpha synuclein. The accuracy of predicting protein structures have vastly been increased in the last years and with alphafold one are able to predict structures with quite high accuracy, which is of extra high benefit when wanting to look at structures that are difficult to produce in a stable way in the lab. We want to analyse the structure of these oligomeric species to better create therapies to these two diseases.
Claudio Mirabello is helping us running Alpha fold efficently on Berzelius.
