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| Main Authors: | , , , , , , , , , , , |
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| Format: | Preprint |
| Published: |
2025
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| Subjects: | |
| Online Access: | https://arxiv.org/abs/2503.06265 |
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| _version_ | 1866915188038434816 |
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| author | Kapon, Yael Merhav, Dror Finkelstein-Zuta, Gal Blumen, Omer Book, Naomi Melamed Levi-Kalisman, Yael Torchinsky, Ilya Yochelis, Shira Sharon, Daniel Baczewski, Lech Tomasz Gazit, Ehud Paltiel, Yossi |
| author_facet | Kapon, Yael Merhav, Dror Finkelstein-Zuta, Gal Blumen, Omer Book, Naomi Melamed Levi-Kalisman, Yael Torchinsky, Ilya Yochelis, Shira Sharon, Daniel Baczewski, Lech Tomasz Gazit, Ehud Paltiel, Yossi |
| contents | Protein aggregation into insoluble amyloid-like fibrils is implicated in a wide range of diseases and understanding its nucleation process is a key for mechanistic insights and advancing therapeutics. The electronic charge of the amyloidogenic monomers significantly influences their self-assembly process. However, the impact of electron spin interactions between monomers on amyloid nucleation has not been considered yet. Here, we studied amyloid formation on magnetic substrates using Scanning Electron Microscopy (SEM), fluorescence microscopy, and Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) Spectroscopy. We observed a preferred magnetization orientation of the ferromagnetic layer for fibril formation, leading to twice as many and significantly longer fibrils (up to 20 times) compared to the opposite magnetization orientation. This preference is related to monomer chirality. Additionally, fibril structure varied with substrate magnetization orientation. Our findings suggest a transient spin polarization in monomers during self-assembly, driven by the Chiral Induced Spin Selectivity (CISS) effect. These effects are consistent for various molecule length scales, from A-beta polypeptide to dipeptides and single amino acids, indicating a fundamental spin-based dependence on biomolecular aggregation that could be applied in novel therapeutic interventions targeted for amyloid-related diseases. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2503_06265 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | Spin-Dependent Amyloid Self-Assembly on Magnetic Substrates Kapon, Yael Merhav, Dror Finkelstein-Zuta, Gal Blumen, Omer Book, Naomi Melamed Levi-Kalisman, Yael Torchinsky, Ilya Yochelis, Shira Sharon, Daniel Baczewski, Lech Tomasz Gazit, Ehud Paltiel, Yossi Chemical Physics Biological Physics Protein aggregation into insoluble amyloid-like fibrils is implicated in a wide range of diseases and understanding its nucleation process is a key for mechanistic insights and advancing therapeutics. The electronic charge of the amyloidogenic monomers significantly influences their self-assembly process. However, the impact of electron spin interactions between monomers on amyloid nucleation has not been considered yet. Here, we studied amyloid formation on magnetic substrates using Scanning Electron Microscopy (SEM), fluorescence microscopy, and Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) Spectroscopy. We observed a preferred magnetization orientation of the ferromagnetic layer for fibril formation, leading to twice as many and significantly longer fibrils (up to 20 times) compared to the opposite magnetization orientation. This preference is related to monomer chirality. Additionally, fibril structure varied with substrate magnetization orientation. Our findings suggest a transient spin polarization in monomers during self-assembly, driven by the Chiral Induced Spin Selectivity (CISS) effect. These effects are consistent for various molecule length scales, from A-beta polypeptide to dipeptides and single amino acids, indicating a fundamental spin-based dependence on biomolecular aggregation that could be applied in novel therapeutic interventions targeted for amyloid-related diseases. |
| title | Spin-Dependent Amyloid Self-Assembly on Magnetic Substrates |
| topic | Chemical Physics Biological Physics |
| url | https://arxiv.org/abs/2503.06265 |