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- W2515706561 abstract "There are synergistic effects of Aβ and tau protein in Alzheimer’s disease. Aβ1–42 protofibril seeds induce conversion of human tau protein into β-sheet-rich toxic tau oligomers. However, the molecular mechanisms underlying such a conformational conversion are unclear. Here, we use extensive all atom replica exchange molecular dynamics simulations to investigate the effects of preformed Aβ1–42 protofibril on two monomeric tau constructs: K18 and K19. We found that Aβ oligomer stretches tau conformation and drastically reduces the metastable secondary structures/hydrogen bonding/salt-bridge networks in tau monomers and exposes their fibril nucleating motifs 275VQIINK280 and 306VQIVYK311. Aβ interacting patches around Tyr10/Ile41 contribute significantly to the interactions with K18 and K19. Aβ cross-seeded tau aggregation can adopt a “stretching-and-packing” mechanism, paving the way for the next, prion-like growth step. The results provide a mechanism on the atomic level to experimental observations that tau pathogenesis is promoted by Aβ1–42 but not by Aβ1–40." @default.
- W2515706561 created "2016-09-16" @default.
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- W2515706561 date "2015-08-07" @default.
- W2515706561 modified "2023-10-18" @default.
- W2515706561 title "Aβ “Stretching-and-Packing” Cross-Seeding Mechanism Can Trigger Tau Protein Aggregation" @default.
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- W2515706561 doi "https://doi.org/10.1021/acs.jpclett.5b01447" @default.
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