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Fluorescent Silicon Nanoparticles Inhibit the Amyloid Fibrillation of Insulin


Amyloid fibrillation of proteins is likely a key factor leading to the development of amyloidosis-associated diseases. Inhibiting amyloid fibrillation has become a crucial therapeutic strategy. Water-soluble, fluorescent silicon nanoparticles (SiNPs) have great potential in biomedicine for various therapeutic and diagnostic purposes, however, it is unclear whether SiNPs have the ability to inhibit amyloid fibrillation. Herein, insulin was chosen as a protein model, and SiNPs of varying size were synthesized by UV irradiation. The influence of size and concentration of SiNPs on insulin fibrillation was investigated, and it was observed that these variables were crucial in regulating insulin fibrillation. Using an average particle size of 6.6 nm and increasing the concentration of SiNPs to 5 g/mL, the Thioflavin T (ThT) fluorescence intensity decreased significantly by 90%, with an increased lag time of 76.8 h, compared to that of the control. Insulin aggregates were short, thin fibrils or clusters when incubated with SiNPs, compared to the long, thick fibrils formed for insulin alone. Additionally, we found that SiNPs prevent the conformational transition of insulin from its initial structure to β-sheets, and thus inhibit nucleation, which is necessary to form large fibrils. The inhibitory activity is attributed to the interactions between SiNPs and insulin during the nucleation period. Our results demonstrate that SiNPs disrupt insulin amyloid fibrillation, and thus, may serve a useful role in new therapeutic and diagnostic strategies for amyloid-related disorders.

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Publication details

The article was received on 09 Nov 2018, accepted on 09 Jan 2019 and first published on 10 Jan 2019

Article type: Paper
DOI: 10.1039/C8TB02964D
Citation: J. Mater. Chem. B, 2019, Accepted Manuscript
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    Fluorescent Silicon Nanoparticles Inhibit the Amyloid Fibrillation of Insulin

    Y. Ma, R. Huang, W. Qi, R. Su and Z. He, J. Mater. Chem. B, 2019, Accepted Manuscript , DOI: 10.1039/C8TB02964D

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