Project information
Computational study of the tau protein aggregation

Information

This project doesn't include Faculty of Economics and Administration. It includes Faculty of Science. Official project website can be found on muni.cz.
Project Identification
MUNI/C/0059/2024
Project Period
3/2024 - 2/2025
Investor / Pogramme / Project type
Masaryk University
MU Faculty or unit
Faculty of Science

The aggregation of β-amyloid protein and the dissociation of tau protein from microtubules and its deposition into neurofibrillary tangles are the most prevalent pathological hallmarks of Alzheimer’s disease onset. Impaired cognitive and verbal abilities characterize the progression of the disease process. While the β-amyloid plaques used to be in the spotlight in the past, nowadays, the tau hypothesis has gained similar importance.
Phosphorylated tau protein dissociates from microtubules, and under specific conditions, it forms fibrils characteristic for different neurodegeneration diseases, so-called tauopathies (Alzheimer’s disease, Parkinson’s disease, Creutzfeldt-Jakob Disease, and others) via several pathological pathways.
The main aim of this project is to study the effect of various phosphorylation patterns on the fibrillization of tau protein and the stability of the resulting fibrils using molecular dynamics on atomistic or coarse-grained resolution and free energy calculations. To achieve this, the stability and behavior of paired helical filament isolated from a brain with Alzheimer’s disease obtained by cryo-electron microscopy will be explored, followed by finding possible fibrillization mechanisms.
The findings of this project can provide insight into pathological processes of tau protein, which can contribute to a better understanding of Alzheimer’s disease onset and progression, allowing earlier diagnostic and targeted treatment.

Publications

Total number of publications: 1


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