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

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$\beta$) 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 $\beta$-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.