Molecular dynamics method for targeting α-synuclein aggregation induced Parkinson's disease using boron nitride nanostructures

Parkinson's disease (PD) is a brain disorder connected with the abnormal aggregation and disposition of α-synuclein proteins. It has been suggested that nanoparticles (NPs) can be used to treat PD by inhibiting the formation of amyloids. In this study, boron nitride nanotube (BNNT) and boron nitride nanolayer (BNNL) were studied as inhibitor of α-synuclein protein aggregation. The interactions of α-synuclein and BN nanostructures have been simulated using molecular dynamics. Due to the tunable properties of boron-nitride structures, these structures can be designed and optimized for the treatment of PD using molecular simulations. To evaluate the effects of NPs, the interaction energies, compactness, and durability of α-synuclein protein in the attendance of NPs were investigated by atomistic analyzes. The results show that BN nanostructures destabilize α-synuclein by changing the structure of it. As a result, the interaction of amyloid with each other and their aggregation in the presence of nanostructures is weakened. Regarding the results, hexagonal two-dimensional (2D) structures, such as BNNL, are highly capable of causing structural conversions in a α-synuclein protein. The computational studies of this work would offer interesting implications for the use of BN nanostructures in the treatment of PD.