First synthetic 'mini prion' shows how protein misfolding multiplies

Our pivotal work on understanding Tau protein misfolding in neurodegenerative disease has just been published and has been featured by both Northwestern University and Phys.org! Special congrats to Dr. Michael Vigers, Karen Tsay, and Austin DuBose from our group for their critical work in making this happen! We have created the first synthetic tau fragment that acts as a prion and have studied how it stacks and misfolds to better understand how Alzheimer's disease would unfold via their natural counterpart. We used Cryo-EM to study the structure of these synthetic fibrils, finding that the P301L mutation on the jR2R3 fragment of tau facilitates a specific type of misfolding that contributes to neurodegenerative disease. We are excited to continue building on our work by further characterizing these proteins!