Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles
Abstract The advancement of neuroprotective pharmacological agents to proficiently avert amyloid-β (Aβ) clustering persists as a significant obstacle in Alzheimer’s disease (AD) management. This analysis focuses on the inhibitory characteristics related to amyloid formation of selenium nanoparticles...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-06-01
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| Series: | Scientific Reports |
| Subjects: | |
| Online Access: | https://doi.org/10.1038/s41598-025-03962-0 |
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| Summary: | Abstract The advancement of neuroprotective pharmacological agents to proficiently avert amyloid-β (Aβ) clustering persists as a significant obstacle in Alzheimer’s disease (AD) management. This analysis focuses on the inhibitory characteristics related to amyloid formation of selenium nanoparticles (SeNPs) enveloped in 5-caffeoylquinic acid (CQA), which are biosynthesized using violet sweet potato (PSP) extract. Engineered SeNPs revealed an absorption peak at 260 nm, were spherical and non-crystalline (50–60 nm), and had a zeta potential measured at 24.3 ± 2.1 mV. The antioxidant traits of SeNPs were showcased (IC50 = 8.01 ± 1.21 µg/mL), by obstructing AChE (IC50 = 3.70 ± 0.02 µg/mL) and BChE (IC50 = 72 ± 0.5 µg/mL), while also diminishing Aβ fibrillation, thereby emphasizing their function in the modulation of amyloid clustering. Molecular dynamics simulations elucidated that CQA-SeNPs preferentially associate with hydrophobic residues (e.g., Leu34 and Phe19) of the Aβ peptide, obstructing β-sheet formation. These findings suggest that CQA-SeNPs interfere with Aβ aggregation, offering a potential therapeutic strategy for AD. |
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| ISSN: | 2045-2322 |