Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangement
M. Vigers, S. Lobo, S. Najafi, A. Dubose, K. Tsay, P. Ganguly, A. P. Longhini, Y. Jin, S. K. Buratto, K. S. Kosik, M. S. Shell, J.-E. Shea, S. Han
This paper identifies a tau peptide fragment that forms seeding-competent fibrils and shows how the P301L mutation facilitates its aggregation into 4R tauopathy-like structures.
bioRxiv · Nov 28, 2023 · PreprintBiophysics