In a comparison of protein filaments extracted from brain tissue donated by persons with FTD and other neurological disorders, scientists have revealed unique 3D structures of tau that vary by disease type. The research, which suggests each brain disease is associated with a unique 3D structure of protein filaments, could help to advance tools for early diagnosis and treatment.

Conducted by scientists from the United States, United Kingdom, and Japan, the study used cryogenic electron microscopy, which enables the discovery of 3D structures of proteins and other molecules, to analyze and compare protein filaments implicated in FTD and various neurodegenerative disorders. The technology allows scientists to better identify subtle differences in the building blocks of a proteins such as tau, which can cause the structure to bend, fold, or twist in a new way and thus contribute to neurodegeneration.

Published in a series of studies co-authored by AFTD Medical Advisory Council member Bernardino Ghetti, M.D., of Indiana University, the findings revealed unique 3D structures of tau associated with FTD, as well as tau structures unique to corticobasal degeneration (CBD), Alzheimer’s disease, and chronic traumatic encephalopathy (CTE), a condition associated with repeated head injuries from physical activity. Researchers also identified unique structures of the alpha-synuclein protein to be associated with Parkinson’s disease, Lewy body dementia, and multiple system atrophy.

By better understanding what causes the differences between protein filaments associated with brain diseases, researchers hope to find new ways to diagnose and treat FTD and other conditions. Similarly, understanding how rogue filaments bend, fold, and twist in structure can aid researchers in exploring the role that a specific structure plays in disease development and progression.

To read more about the research, click here. Individuals and families who are interested in learning more about brain donation can find information on the AFTD website.