Bath scientists design peptide ‘switch’ that keeps Parkinson’s protein in its healthy form

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On Oct. 6, 2025, Researchers at the University of Bath, in collaboration with the Universities of Oxford and Bristol, announced they have developed a molecule that prevents the clumping and build-up of a protein linked to Parkinson’s disease and related dementias. The team has successfully demonstrated it works in an animal model of Parkinson’s and hopes that in the future this could lead to a treatment that slows the progression of the disease.

Alpha-synuclein is a protein naturally found mainly in brain cells (neurons) where it regulates the release of neurotransmitters such as dopamine, allowing communication between the neurons.

In Parkinson’s disease, this protein sticks together into toxic clumps that cause nerve cell death and leads to patients suffering from symptoms such as tremors, difficulties moving and muscle stiffness. Whilst there are treatments available to relieve symptoms, there is currently no cure. Normally, alpha-synuclein’s natural or “native state” is like a flexible strand, but when active it shapes itself into a helix, which is critical for its function in binding and transporting parcels of dopamine.

The team engineered a peptide fragment that locks alpha-synuclein into its healthy shape, blocking its conversion into the toxic clumps that cause nerve cell death. Laboratory tests showed the peptide is stable, penetrates brain-like cells, and restores movement while reducing protein deposits in a worm model of Parkinson’s.

This breakthrough, published in the journal JACS Au, demonstrates the potential of rational peptide design to transform large, unstable proteins into compact drug-like molecules. The findings mark a significant step towards developing new peptide-based treatments for currently untreatable neurodegenerative conditions.

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Source: University of Bath
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