Multiscale simulations reveal the driving forces underlying V337M-induced Tau core fragment aggregation

Pengxuan Xia; Yujie Chen; Jiaxing Tang; Lulu Guan; Dushuo Feng; Yu Zou

doi:10.1039/d5nr05519a

January 1, 2026Nanoscale

Multiscale simulations reveal the driving forces underlying V337M-induced Tau core fragment aggregation

View Full Paper

Ask AI

Bookmark

Share

Key Points

The aim is to understand how the V337M mutation influences Tau aggregation, a key factor in tauopathies.
Multiscale simulations were conducted to analyze the structural changes in Tau due to the V337M mutation.
Focus was on the aggregation-prone PHF6** motif of Tau.
Interactions between Tau fragments were assessed to reveal driving forces of aggregation.
Simulations showed significant alterations in the aggregation pathway due to the V337M mutation.
Increased probability of Tau core fragment aggregation was observed compared to wild-type Tau.
Key driving forces identified include structural changes induced by the mutation, affecting Tau dynamics.

Implication

Multiscale simulations demonstrate how the V337M mutation affects Tau aggregation in tauopathies.

Abstract

Pathogenic microtubule-associated protein tau (MAPT) mutations play an important role in tauopathies by altering Tau assembly and early aggregation. The V337M mutation, located within the aggregation-prone PHF6** motif of Tau,...

Discussion

No takes yet. Share an insight, caveat, or question.

Cite This Study

Xia et al. (2026) studied this question.

synapsesocial.com/papers/6a0567a8a550a87e60a1fd29 https://doi.org/10.1039/d5nr05519a

View Full Paper

Ask AI

Bookmark

Share

Multiscale simulations reveal the driving forces underlying V337M-induced Tau core fragment aggregation

Key Points

Implication

Abstract

Discussion

Cite This Study

Multiscale simulations reveal the driving forces underlying V337M-induced Tau core fragment aggregation

Key Points

Implication

Abstract

Discussion

Cite This Study

Keep reading

Keep reading