Scientific Foundation
Understanding disease at its molecular origin.
We combine protein biophysics, structural biology, and Al to uncover how protein condensation and misfolding initiate neurodegenerative and metabolic.
Protein Misfolding & LLPS
We study LLPS-driven protein condensation, misfolding, and aggregation to reveal the earliest molecular origins of neurodegenerative and metabolic diseases.
Our research shows that disruptions in biomolecular phase separation can initiate pathological protein assemblies, including TDP-43 proteinopathies.
View our TDP-43 research published in Nature Communications →
Disease OriginTM Al Platform
We integrate biofluid protein signals with clinical context to reconstruct pathophysiological
pathways and deliver ultra-early, actionable risk insights.
pathways and deliver ultra-early, actionable risk insights.
TDP-43 contains an aggregation-prone domain that enables LLPS dynamic, membrane-less assemblies for cellular maintenance. Disease converts this reversible organization into misfolded aggregates, leading to oxidative stress and loss of function.
Pilot Clinical Trial
- Focus: Dementia with Lewy Bodies
- Trial Results:
- 50% reduction in plasma α-synuclein levels after 4 weeks.
- 100% reduction after 16 weeks.
- Significant cognitive and behavioral improvements.
- Future Plans:
- Phase I/II Reprofold® Treatment Clinical Trial of DLB
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