Israeli scientists discovered that the direction of magnetic fields can affect how Alzheimer’s-related proteins clump together and form harmful brain plaques.
- Magnetic surfaces can change the way amyloid-beta proteins clump in Alzheimer’s
- Electron spin direction affects the number, length, and shape of fibrils
- Discovery may lead to new treatments for neurodegenerative diseases
Israeli researchers have discovered that the spin orientation of electrons on magnetized surfaces can influence the way amyloid-beta proteins—which are central to Alzheimer’s disease—aggregate into harmful fibrils (1✔ ✔Trusted Source
Controlling Amyloid Assembly Dynamics Using Spin Interfaces
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The study, published in ACS Nano, was led by Yael Kapon, a Ph.D. student at the Hebrew University of Jerusalem’s Institute of Applied Physics, with Prof. Yossi Paltiel and Prof. Ehud Gazit of Tel Aviv University.
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The Role of Amyloid-Beta in Alzheimer’s
Amyloid-beta (Aβ₁–₄₂) peptides are known for forming sticky plaques in the brains of people with Alzheimer’s. The team examined how these peptides self-assemble on magnetized surfaces and whether electron spin orientation could alter the process.
When the surface magnetization pointed in one direction, the amyloid proteins formed nearly twice as many fibrils, some up to 20 times longer than when the magnetization was reversed.
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Chiral-Induced Spin Selectivity (CISS) Effect
The researchers linked this phenomenon to Chiral-Induced Spin Selectivity (CISS) , where chiral (asymmetric) molecules interact differently with electrons depending on their spin. While the CISS effect has been observed in chemistry and materials science, its role in biology is only beginning to be explored.
When a mirror-image (opposite chirality) version of the peptide was used, the fibril formation pattern also reversed—strong evidence for spin-dependent behavior.
Structural and Molecular Differences
Using electron microscopy and infrared spectroscopy, the team found that not only did fibrils vary in number and length, but their internal molecular arrangements also differed depending on electron spin alignment.
Prof. Paltiel said, “We’re beginning to see that biology may be more sensitive to spin than we thought. Our work shows that spin-related forces can directly influence the way proteins aggregate.”
Prof. Gazit added, “These findings suggest that physical properties like electron spin—not just biochemical interactions—can play a meaningful role in how harmful structures develop.”
Future Possibilities
Although the research is at a basic stage, it opens the door to potential new interventions. Future technologies could use spin-polarized nanoparticles or magnetized filters to disrupt harmful amyloid buildup—possibly benefiting not only Alzheimer’s patients but also those with other amyloidosis-related conditions.
Kapon noted, “This study gives us a new tool to probe how proteins come together. We hope it will guide future research into slowing, preventing, or redirecting these processes in a controlled way.”
Reference:
- Controlling Amyloid Assembly Dynamics Using Spin Interfaces – (https://pubs.acs.org/doi/10.1021/acsnano.5c06285)
Source-Medindia