From pinworms to proteins: How a surprising old drug is inspiring new ideas for Alzheimer’s
- research2693
- Oct 16
- 4 min read
A new study reveals an unexpected mechanism that could reshape how we understand Alzheimer’s, Parkinson’s, and the science of brain resilience.
Researchers at the University of California, San Diego, together with the University of Pittsburgh, have uncovered surprising findings about an old antiparasitic drug called pyrvinium pamoate, traditionally used to treat intestinal worm infections.
In laboratory models, this compound appeared to restore key protein-regulation systems inside brain cells, dramatically reducing the buildup of toxic proteins linked to neurodegenerative diseases such as Alzheimer’s and Parkinson’s.
While still in the research phase, these results provide an exciting glimpse into how our cells might maintain balance and resilience, and how nutrition and lifestyle may one day support similar pathways naturally.
Understanding the cellular challenge
In most neurodegenerative diseases, proteins that normally support brain-cell function start to misfold and aggregate.
In Alzheimer’s disease, this protein is tau.
In Parkinson’s disease, it’s alpha-synuclein.
When these proteins clump together, they interfere with communication between neurons, damage mitochondria, and trigger inflammation. Over time, this leads to cell death and the symptoms associated with cognitive or motor decline.
Healthy brain cells rely on finely tuned internal systems — molecular chaperones, autophagy, and proteasomal clearance — to keep protein balance in check. This overall process is known as proteostasis.
However, when these systems are disrupted by oxidative stress, poor energy metabolism, or ageing, protein waste accumulates faster than the cell can manage, setting the stage for disease progression.
The role of nuclear speckles: The brain cell’s hidden regulators
Within every neuron lies a nucleus that manages genetic expression. Inside that nucleus are nuclear speckles — tiny, droplet-like structures that control how genetic instructions are processed into functional proteins.
They operate through a process called liquid–liquid phase separation, meaning they form and move like liquid droplets rather than fixed organelles.
This flexibility allows them to continuously regulate gene expression and coordinate the cell’s stress response.
When exposed to chronic stress, these droplets can become rigid and less functional, disrupting how the cell produces and repairs proteins.
Recent studies have linked this loss of flexibility to several neurodegenerative diseases — but until now, no known drug had been shown to reverse it.
What the UC San Diego Study found
The researchers discovered that pyrvinium pamoate restored the flexibility of nuclear speckles in both cell and animal models of tau pathology.
When the drug was introduced, the droplets regained their normal liquid-like properties, improving communication between the nucleus and the rest of the cell.
This allowed neurons to re-establish healthy protein-control mechanisms, and tau accumulation dropped by about 70 percent.
The team used advanced imaging tools, including optical tweezers, to measure how pyrvinium pamoate changed the physical properties of these nuclear structures.
They confirmed that the compound reduced surface tension within the droplets, helping them move and function normally again.
Importantly, the effect occurred without damaging healthy cells, suggesting the improvement was due to restored regulation, not toxicity.
Why this discovery matters
This research introduces a new idea: that the physical organisation of the cell, not just its chemical reactions, may play a central role in neurodegenerative disease.
By restoring the environment in which genes and proteins are regulated, it may be possible to influence how the brain protects and repairs itself.
This represents a shift from traditional drug approaches that target one specific molecule or receptor. Instead, it focuses on supporting the cell’s inherent ability to maintain homeostasis an approach closely aligned with the principles of functional medicine and nutritional therapy.
How this connects to nutritional science
Although pyrvinium pamoate itself is not suitable for clinical use in brain health, its underlying mechanism reflects biological processes that nutritional therapy seeks to support naturally.
At You Nutrition Clinic, we focus on helping clients support the body’s own ability to maintain cellular balance and repair by:
• Optimising mitochondrial function – sustaining healthy energy metabolism that underpins all cellular renewal
• Reducing oxidative stress and inflammation – both central to the processes of protein misfolding and neuronal injury
• Supporting natural proteostasis – the body’s capacity to fold, recycle, and clear damaged proteins efficiently
• Prioritising restorative sleep and circadian health – as these processes are essential for autophagy and waste clearance in the brain
While the UCSD study explored a pharmacological compound, it underscores a broader truth: when we restore cellular balance and resilience, the nervous system is often better equipped to repair, adapt, and protect itself.
The Future of Brain Research
These findings open a new field of investigation into biophysical neurobiology — how the physical state of cell structures influences function and disease.
Future studies may explore:
• Small molecules that can safely modulate nuclear-phase behaviour in humans
• Nutritional or metabolic factors that help maintain condensate fluidity
• The role of systemic metabolic health in regulating intracellular organisation
For individuals living with or at risk of neurodegenerative conditions, this research offers reassurance that science is moving beyond symptom management toward understanding the root mechanisms of cellular resilience.
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References
UC San Diego Today (2025, August 11). Antiparasitic drug shows power against Alzheimer’s and dementia. https://today.ucsd.edu/story/antiparasitic-drug-shows-power-against-alzheimers-and-dementia
Ramaswami M., & Alberti S. (2023). Protein phase separation in neurodegeneration. Nature Reviews Neuroscience, 24(1), 1–17. https://doi.org/10.1038/s41583-022-00704-y
Hipp M. S., Kasturi P., & Hartl F. U. (2019). The proteostasis network and its decline in ageing. Nature Reviews Molecular Cell Biology, 20(7), 421–435. https://doi.org/10.1038/s41580-019-0108-y
Alberti S., & Hyman A. A. (2021). Biomolecular condensates at the nexus of cellular stress, protein aggregation, and neurodegeneration. Nature Reviews Molecular Cell Biology, 22(3), 196–213. https://doi.org/10.1038/s41580-020-00326-6
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