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Computational Study of Intermolecular Interactions between α-Synuclein Fibrils and Tau Protein Propagating Tau Aggregation


Affiliations
1 Molecular Modelling and Simulation Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784 028, India
 

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.

Keywords

Fibrils, Microtubules, Intermolecular Interactions, Neurodegenerative Disorders.
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  • Computational Study of Intermolecular Interactions between α-Synuclein Fibrils and Tau Protein Propagating Tau Aggregation

Abstract Views: 394  |  PDF Views: 128

Authors

Airy Sanjeev
Molecular Modelling and Simulation Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784 028, India
Venkata Satish Kumar Mattaparthi
Molecular Modelling and Simulation Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784 028, India

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.

Keywords


Fibrils, Microtubules, Intermolecular Interactions, Neurodegenerative Disorders.

References





DOI: https://doi.org/10.18520/cs%2Fv112%2Fi11%2F2219-2225