Interaction between U-shaped amyloid beta fibril and semiconducting silicon nitride monolayer

Fuente: arXiv
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Main Authors: Shekaari, Ashkan, Jafari, Mahmoud
Format: Preprint
Published: 2024
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author Shekaari, Ashkan
Jafari, Mahmoud
author_facet Shekaari, Ashkan
Jafari, Mahmoud
contents Motivated by some recent works showing the ability of semiconducting monolayers to disintegrate the structures of biological fibrils, we have applied molecular dynamics (MD) simulations in both classical and quantum regimes to investigate whether semiconducting Si$_3$N$_4$ monolayer has the same ability on interaction with U-shaped amyloid beta (A$β$) fibril. In agreement with the literature, we found that disintegration began from the last chain (E) due to the rather strong interaction between the monolayer and the fibril residues numbered from 17 to 28 on the very chain, also engaging the next chain (D) over time. As a result, the $β$-sheet-rich content of chain E considerably decreases on interaction with the monolayer, turning into other secondary-structure types including turn and coil, in accordance with experimental findings. Results endorse the view that semiconducting Si$_3$N$_4$ monolayer has the potential of destabilizing the structure and conformation of U-shaped amyloid beta fibrils.
format Preprint
id arxiv_https___arxiv_org_abs_2403_10536
institution arXiv
publishDate 2024
record_format arxiv
spellingShingle Interaction between U-shaped amyloid beta fibril and semiconducting silicon nitride monolayer
Shekaari, Ashkan
Jafari, Mahmoud
Soft Condensed Matter
Materials Science
Motivated by some recent works showing the ability of semiconducting monolayers to disintegrate the structures of biological fibrils, we have applied molecular dynamics (MD) simulations in both classical and quantum regimes to investigate whether semiconducting Si$_3$N$_4$ monolayer has the same ability on interaction with U-shaped amyloid beta (A$β$) fibril. In agreement with the literature, we found that disintegration began from the last chain (E) due to the rather strong interaction between the monolayer and the fibril residues numbered from 17 to 28 on the very chain, also engaging the next chain (D) over time. As a result, the $β$-sheet-rich content of chain E considerably decreases on interaction with the monolayer, turning into other secondary-structure types including turn and coil, in accordance with experimental findings. Results endorse the view that semiconducting Si$_3$N$_4$ monolayer has the potential of destabilizing the structure and conformation of U-shaped amyloid beta fibrils.
title Interaction between U-shaped amyloid beta fibril and semiconducting silicon nitride monolayer
topic Soft Condensed Matter
Materials Science
url https://arxiv.org/abs/2403.10536