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Current Medicinal Chemistry

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Review Article

Molecular Mechanism of Tau Misfolding and Aggregation: Insights from Molecular Dynamics Simulation

Author(s): Haiyang Zhong, Hongli Liu and Huanxiang Liu*

Volume 31, Issue 20, 2024

Published on: 21 June, 2023

Page: [2855 - 2871] Pages: 17

DOI: 10.2174/0929867330666230409145247

Price: $65

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Abstract

Tau dysfunction has a close association with many neurodegenerative diseases, which are collectively referred to as tauopathies. Neurofibrillary tangles (NFTs) formed by misfolding and aggregation of tau are the main pathological process of tauopathy. Therefore, uncovering the misfolding and aggregation mechanism of tau protein will help to reveal the pathogenic mechanism of tauopathies. Molecular dynamics (MD) simulation is well suited for studying the dynamic process of protein structure changes. It provides detailed information on protein structure changes over time at the atomic resolution. At the same time, MD simulation can also simulate various conditions conveniently. Based on these advantages, MD simulations are widely used to study conformational transition problems such as protein misfolding and aggregation. Here, we summarized the structural features of tau, the factors affecting its misfolding and aggregation, and the applications of MD simulations in the study of tau misfolding and aggregation.

Keywords: Tau protein, aggregation, misfolding, molecular dynamics simulation, post-translational modifications, mutation.

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