2018/04/05 by Johannes Weickenmeier, Ellen Kuhl, Alain Goriely · 1 citation
Biochemistry, Genetics and Molecular Biology · #q-bio.NC #q-bio.TO
paper · pdf · doi:10.1103/physrevlett.121.158101
published as Phys. Rev. Lett. 121, 158101 (2018) · 5 pages/5 figures
arxiv created 2018/04/05 · arxiv updated 2018/10/17
Many neurodegenerative diseases are related to the propagation and accumulation of toxic proteins throughout the brain. The lesions created by aggregates of these toxic proteins further lead to cell death and accelerated tissue atrophy. A striking feature of some of these diseases is their characteristic pattern and evolution, leading to well-codified disease stages visible to neuropathology and associated with various cognitive deficits and pathologies. Here, we simulate the anisotropic propagation and accumulation of toxic proteins in full brain geometry. We show that the same model with different initial seeding zones reproduces the characteristic evolution of different prion-like diseases. We also recover the expected evolution of the total toxic protein load. Finally, we couple our transport model to a mechanical atrophy model to obtain the typical degeneration patterns found in neurodegenerative diseases.