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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Nature Portfolio
2025-06-01
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| Series: | Scientific Reports |
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| Online Access: | https://doi.org/10.1038/s41598-025-03962-0 |
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| author | Shubhangi D. Shirsat Chunyi Li Zhipeng Liu Varenyam Achal Olivier Habimana |
| author_facet | Shubhangi D. Shirsat Chunyi Li Zhipeng Liu Varenyam Achal Olivier Habimana |
| author_sort | Shubhangi D. Shirsat |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-e16cb3d1c68d47aa84ecfb75ab8cfc93 |
| institution | Kabale University |
| issn | 2045-2322 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Nature Portfolio |
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| series | Scientific Reports |
| spelling | doaj-art-e16cb3d1c68d47aa84ecfb75ab8cfc932025-08-20T03:26:44ZengNature PortfolioScientific Reports2045-23222025-06-0115111310.1038/s41598-025-03962-0Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticlesShubhangi D. Shirsat0Chunyi Li1Zhipeng Liu2Varenyam Achal3Olivier Habimana4Biotechnology and Food Engineering Program, Guangdong Technion-Israel Institute of TechnologyBiotechnology and Food Engineering Program, Guangdong Technion-Israel Institute of TechnologyBiotechnology and Food Engineering Program, Guangdong Technion-Israel Institute of TechnologyEnvironmental Engineering Program, Guangdong Technion-Israel Institute of TechnologyBiotechnology and Food Engineering Program, Guangdong Technion-Israel Institute of TechnologyAbstract 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.https://doi.org/10.1038/s41598-025-03962-0Selenium nanoparticles5‑caffeoylquinic acidAntioxidantCholinesteraseβ-Amyloid peptideMolecular dynamic simulation |
| spellingShingle | Shubhangi D. Shirsat Chunyi Li Zhipeng Liu Varenyam Achal Olivier Habimana Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles Scientific Reports Selenium nanoparticles 5‑caffeoylquinic acid Antioxidant Cholinesterase β-Amyloid peptide Molecular dynamic simulation |
| title | Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles |
| title_full | Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles |
| title_fullStr | Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles |
| title_full_unstemmed | Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles |
| title_short | Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles |
| title_sort | anti amyloidogenic properties of 5 caffeoylquinic acid capped selenium nanoparticles |
| topic | Selenium nanoparticles 5‑caffeoylquinic acid Antioxidant Cholinesterase β-Amyloid peptide Molecular dynamic simulation |
| url | https://doi.org/10.1038/s41598-025-03962-0 |
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