Computational study of intermolecular interactions between α-synuclein fibrils and Tau protein propagating Tau aggregation

Abstract

α-Synuclein is the principal component responsible for the onset of Parkinson's disease, a neurodegenerative disorder. It has been recently suggested that α- synuclein fibrils probably interact with Tau protein, inhibit its function to stabilize microtubules, and also promote Tau aggregation, leading to dysfunction of neuronal cells. Here, we have studied the interactions between α-synuclein fibrils and Tau protein. The results show that the basic region of Tau protein strongly interacts with the C-terminal acidic regions of α-synuclein fibrils, and undergoes conformational change resulting in the formation of seed for assembly of Tau into amyloid-like fibrils.