Exploring the misfolding and self-assembly mechanism of TTR (105–115) peptides by all-atom molecular dynamics simulation

Exploring the misfolding and self-assembly mechanism of TTR (105–115) peptides by all-atom molecular dynamics simulation

Pathological aggregation of essentially dissociative Transthyretin (TTR) monomers protein, driven by misfolded and self-interaction, is connected with Amyloid Transthyretin amyloidosis (ATTR) disease. The TTR monomers protein contains several fragments that tend to self-aggregate, such as residue 10...

Full description

Bibliographic Details
Main Authors: Yuqi Zhang, Yanyan Zhu, Haiyan Yue, Qingjie Zhao, Huiyu Li
Format: Article
Language:English
Published: Frontiers Media S.A. 2022-08-01
Series:Frontiers in Molecular Biosciences
Subjects:
TTR(105–115)
peptide aggregation
β-Barrel
hydrophobic interaction
molecular dynamics simulation
ATTR
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2022.982276/full

Internet

https://www.frontiersin.org/articles/10.3389/fmolb.2022.982276/full

Similar Items