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A peptide switch developed by university scientists could offer a powerful way to prevent the build-up of alpha-synuclein, the protein strongly linked to Parkinson’s disease.
Alpha-synuclein is found in brain cells, where it regulates dopamine release and enables communication between neurons. In Parkinson’s, however, it clumps together, leading to cell death and the symptoms of the disease, including tremors and dementia.
A team from the University of Bath, working with Oxford and Bristol researchers, created a peptide fragment that locks the protein into its healthy, active shape. When in this state, alpha-synuclein folds into a helix to bind and transport dopamine, rather than forming toxic clumps.
Using a worm model of Parkinson’s, the researchers showed the fragment could prevent the damaging clumping, and even restore movement. Writing in JACS Au, they reported the peptide helped maintain protein stability in living systems.
Funded by Alzheimer’s Research UK, the project has sparked optimism. Dr Julia Dudley, the charity’s head of research, said:
“By stabilising alpha-synuclein in its healthy form, this could open the door to a new class of treatments that could slow progression in diseases like Parkinson’s and dementia with Lewy bodies.”
Professor Jody Mason of Bath’s Department of Life Sciences added:
“Our work shows it’s possible to rationally design small peptides that not only prevent harmful protein aggregation but also function inside living systems. This opens an exciting path towards new therapies for Parkinson’s and related diseases, where treatment options remain extremely limited.”
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