Our research: Studying the structure and interactions of Tau protein to understand Alzheimer's disease
The research group of assoc. prof. Jozef Hritz working at the Department of Chemistry, the National Centre for Biomolecular Research and CEITEC of Masaryk University has long been studying proteins involved in neurodegenerative diseases, especially Alzheimer's disease. In a recent publication, they focused on the structure and interactions of phosphorylated Tau protein, a key player in this disease.
They investigated the interactions between Tau protein and 14-3-3ζ proteins, which are abundant in the human brain, using atomic-resolution biophysical methods such as nuclear magnetic resonance (NMR) spectroscopy, chemical cross-linking, and mass spectrometry. They found out how phosphorylation of the Tau protein affects its structure and binding properties (binding affinity, ratio, and site) to the 14-3-3ζ protein in two forms – dimeric and monomeric. The results of this work could contribute to a better understanding of the molecular mechanism of Tau protein aggregation, which is one of the typical manifestations of Alzheimer's disease in the brain, but which has not yet been fully elucidated.