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

Smida, Kamel; Albedah, M. A.; Rashid, Rzgar Farooq; Al‐Qawasmi, Abdel‐Rahman

doi:10.1016/j.enganabound.2022.10.016

Cited by 10 publications

(8 citation statements)

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“…The planar surface of BNNS leads to superior stacking orientation with hIAPP, making it most favorable as an inhibitor of hIAPP dimerization. The better performance of BNNS over BNNT is also detected in their inhibition toward α-syn aggregation . These BN nanoparticles also display the potential to destabilize the ordered protofibrillar structure of hIAPP by interacting with the N-terminal side of protofibrils.…”

Section: Discussionmentioning

confidence: 97%

“…63 The destabilization effect of BNNT and BNNS on amyloid aggregation of α-synuclein, which is associated with PD, is also reported. 64 Here, BNNS demonstrates better inhibitory potential against α-syn aggregation than BNNT. 64 These studies suggest that the curvature of nanoparticles influences peptide− nanoparticle interactions.…”

Section: Introductionmentioning

confidence: 82%

“…64 Here, BNNS demonstrates better inhibitory potential against α-syn aggregation than BNNT. 64 These studies suggest that the curvature of nanoparticles influences peptide− nanoparticle interactions. 65,66,43 In addition, the polar nature of the B−N bonds results in variation of interaction between BN nanoparticles and amino acids of different polarities.…”

Section: Introductionmentioning

confidence: 82%

“…The better performance of BNNS over BNNT is also detected in their inhibition toward α-syn aggregation. 64 These BN nanoparticles also display the potential to destabilize the ordered protofibrillar structure of hIAPP by interacting with the N-terminal side of protofibrils. The destabilization effect is more pronounced for (5,5)BNNT and BNNS.…”

Section: Discussionmentioning

confidence: 99%

“…BNNTs have also been used to deliver anticancer drugs in brain and also DNA oligomers . Recently, the application of boron nitride (BN) nanoparticles in the inhibition of aggregation of amyloid peptides has also been explored. − Sorout et al discovered that (3,3)BNNT stabilizes helical Aβ trimers and inhibits their conformational transition to β-sheet rich aggregates, thus preventing Aβ self-assembly . Furthermore, they have also observed that, with variation in curvature of BN nanoparticles, structural changes of Aβ and its interactions with the nanoparticle differs .…”

Section: Introductionmentioning

confidence: 99%

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Exploring the Curvature-Dependence of Boron Nitride Nanoparticles on the Inhibition of hIAPP Aggregation

Roy,

Paul

2023

J. Phys. Chem. B

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Nanoparticles, particularly carbon nanoparticles, have gathered significant interest in the field of anti-aggregation research. However, due to their cytotoxicity, the exploration of biocompatible nanoparticles has become a new frontier in the quest for drugs against human amyloid diseases. The application of non-cytotoxic and biocompatible boron nitride (BN) nanoparticles against amyloid aggregation has been probed to tackle this issue. BN nanoparticles displayed inhibitory activity against the aggregation of Aβ and α-syn peptides. In this work, the effect of BN nanoparticles on the dimerization of hIAPP, which is associated with the pathogenesis of type 2 diabetes, is studied. BN nanoparticles prevent the misfolding of hIAPP into β-sheet-rich aggregates. On varying the curvature, the nanoparticles display variation in the interaction preference with hIAPP. Interestingly, as the hydrophobicity of the nanoparticles increases from (5,5) BN nanotube to BN nanosheet, the interaction propensity shifts from N-terminal to the amyloid prone C-terminal of hIAPP. The hydrophobic and aromatic stacking interactions are a contributing factor toward the binding between hIAPP and BN. Due to this, the flat surface of the nanosheet shows better interaction potential toward hIAPP, compared to the nanotubes. Further, the nanoparticles can also disassemble preformed hIAPP fibrils, and the effect is more pronounced for (5,5) nanotube and the nanosheet. This study provides insight into the inhibitory mechanism of hIAPP aggregation by boron nitride nanoparticles and also an understanding of the significance of the curvature of nanoparticles in their interaction with amyloid peptides, which is valuable for the design of antiamyloid drugs.

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Section: Discussionmentioning

confidence: 97%