Alzheimer’s research: Culprit of deadly tau aggregation found

Understanding tau behavior in Alzheimer’s disease could alter the course of diagnostics and therapy development. Research conducted in part by scientists at the Technische Universitat Munchen (TUM) has revealed an essential mechanism of tau deposition and neurodegenerative disease, the institution announced today.

Researchers from TUM and the Helmholtz Zentrum Munchen, including Tobias Madl, PhD, head of the BioSysNet Working Group and a junior fellow at TUM, used diverse imaging methods including MR spectroscopy and computer modeling to understand the dynamic and interchange between tau protein and proteins like the “heat shock” chaperone protein known as HSP90 as they relate to the development of neurodegenerative disease and other illnesses.

“Deposits of tau proteins can cause Alzheimer’s disease,” commented Madl via press release. “We have discovered the protein regions in which the proteins interact. This is a novel and important starting point for influencing structural formation and for developing future therapies for Alzheimer’s disease.”

The scientists found that HSP90 ordinarily unites with proteins that have already been folded while tau proteins resemble elongated chains. The research led to the discovery that HSP90 mistake tau proteins for folded larger proteins. Additionally this protein causes a particular formation of tau that is related to nerve damage and onset of neurodegeneration. These chaperones are also implicated in cystic fibrosis and tumor development. The knowledge is certain to be instrumental in future drug development.

The research was funded by a handful of international institutions, including the National Institutes of Health, and the computer modeling phase was conducted at the Leibniz Supercomputing Center of the Bavarian Academy of Sciences.