Tel Aviv [Israel], August 1 (ANI/TPS): Israeli scientists have uncovered a surprising physical mechanism that may influence the development of Alzheimer's disease, which raises new possibilities for the treatment of neurodegenerative diseases.
The research found that the orientation of magnetic fields on surfaces can steer the way amyloid-beta proteins key contributors to Alzheimer's assemble into harmful fibrils in the brain.
The study, led by Yael Kapon, a PhD student at the Hebrew University of Jerusalem's Institute of Applied Physics, was recently published in the peer-reviewed ACS Nano. The research was carried out under the guidance of Prof. Yossi Paltiel and in collaboration with Prof. Ehud Gazit of Tel Aviv University.
The findings suggest that electron spin orientation which is determined by the magnetisation of a surface can significantly affect the quantity, length, and structure of amyloid fibrils.
"We're beginning to see that biology may be more sensitive to spin than we thought," said Paltiel. "Our work shows that spin-related forces can directly influence the way proteins aggregate. That's a new dimension to consider when thinking about diseases like Alzheimer's, which involve the buildup of these kinds of fibrils."
At the centre of the study is the amyloid-beta (Ab₁-₄₂) peptide, known for its role in forming sticky plaques in the brains of Alzheimer's patients. The researchers examined how these peptides self-assemble on magnetised surfaces, discovering that the spin direction of electronsaligned by the magnetic fieldaltered the formation process dramatically.
When the magnetisation of the surface pointed in one direction, the amyloid proteins formed nearly twice as many fibrils some as much as 20 times longer than when the magnetisation was reversed. When a version of the peptide with opposite chirality was used, the pattern also reversed, indicating a robust spin-dependent effect.
The phenomenon behind these results is known as Chiral-Induced Spin Selectivity (CISS). This effect describes how chiral molecules those with a specific "handedness" interact differently with electrons depending on their spin. While previously studied in chemistry and materials science, CISS is only now gaining attention for its potential role in biological processes.
"These findings add a new layer to our understanding of amyloid formation," said Gazit, an expert in protein self-assembly. "They suggest that physical properties like electron spinnot just biochemical interactionscan play a meaningful role in how these harmful structures develop. This opens up new possibilities for designing technologies that influence protein behaviour in targeted and non-invasive ways."
Using electron microscopy and infrared spectroscopy, the team found that not only did the fibrils differ in number and length, but their internal molecular arrangement also varied depending on the spin alignment of the surface. The implication is that spin polarisation could be a controllable factor in the prevention or manipulation of amyloid structures linked to neurodegeneration.
While the research remains at a fundamental stage, it could pave the way for novel approaches to controlling protein aggregation. The team envisions future applications such as spin-polarised nanoparticles or magnetised filters that might disrupt or redirect harmful protein buildup, with potential uses in treating Alzheimer's and related disorders.
"This study gives us a new tool to probe how proteins come together," said Kapon. "We hope it will help guide future research into how to slow, prevent, or redirect these processes in a controlled way." (ANI/TPS)
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