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Mattaparthi, Venkata Satish Kumar
- Computational Study of Intermolecular Interactions between α-Synuclein Fibrils and Tau Protein Propagating Tau Aggregation
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1 Molecular Modelling and Simulation Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784 028, IN
1 Molecular Modelling and Simulation Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784 028, IN
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Current Science, Vol 112, No 11 (2017), Pagination: 2219-2225Abstract
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
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- A Comparative Study to Elucidate the Inhibitory Mechanism of a 6-Mer Fragment of Amyloid-Beta 42 Peptide as a Potential Therapeutic in Alzheimer’s Disease:Insights from Molecular Dynamics Simulations
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Authors
Affiliations
1 Department of Molecular Biology and Biotechnology, Tezpur University, Sonitpur 784 028, IN
1 Department of Molecular Biology and Biotechnology, Tezpur University, Sonitpur 784 028, IN
Source
Current Science, Vol 114, No 06 (2018), Pagination: 1207-1213Abstract
Alzheimer’s disease is a neurodegenerative and incurable disease that is associated with the amyloid beta (Aβ) aggregation. We have carried out comparative molecular dynamics simulations of a 6-mer peptide and its analogues to elucidate the inhibitory mechanism on Aβ aggregation. The top analogue screened after refinement via docking exhibited significant inhibitory activities on both Aβ17–42 fibril as well as Aβ1–42 monomer, leading to disassembly of β-strands of Aβ1–42 peptide and fibril by interacting with C-terminal residues via hydrogen bonds and hydrophobic contacts. Binding of the analogue to the C-terminal region proves to be significant.Keywords
Alzheimer’s Disease, Aggregation, Docking, Hydrophobic Interaction, Inhibitor Peptide.References
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