Our research

Targeting tau, naturally

Most of today’s Alzheimer’s drugs go after amyloid. We focus on tau, the protein that forms toxic tangles inside neurons in Alzheimer’s disease, frontotemporal dementia, CTE and other tauopathies. Our question is simple: can natural, plant-derived compounds help keep tau from clumping together?

Why tau?

A shared thread across dementias

In healthy neurons, tau stabilizes the microtubules that give the cell its shape and carry nutrients along the axon. In disease, tau becomes chemically altered, detaches, and aggregates into fibrils and tangles. Misfolded tau can then act as a “seed” that corrupts normal tau in neighboring cells, spreading pathology through connected brain regions.

Tau pathology tracks closely with symptoms and neurodegeneration, and it is common to many forms of dementia. That makes tau aggregation a compelling point to intervene.

Read the biology
Our pipeline

Four stages of evidence

Candidate compounds must pass each stage before moving to the next, from simple, high-throughput tests to complex living systems.

Screen in biosensor cells

We screen natural compounds in tau biosensor cells. These engineered cells glow with a FRET signal when tau aggregates, so we can see quickly which compounds reduce aggregation.

Test fibril formation

Leading candidates, primarily flavonoids, are tested directly for their ability to inhibit the formation of tau fibrils, the building blocks of tangles.

Challenge with patient-derived tau

Selected plant extracts are applied to an Alzheimer’s cell model in which aggregation is triggered by tau “seeds” derived from brain tissue.

Validate in vivo

Extracts are given orally over 10 months in the 3xTg-AD mouse, a widely used model that develops both amyloid and tau pathology. We examine the hippocampus and cortex, and test memory with the Y-maze.

Method spotlight

How a tau biosensor works

Biosensor cells produce tau tagged with two fluorescent proteins, CFP and YFP. While tau floats freely, the tags are too far apart to interact. When tau aggregates, the tags are pulled within about 10 nanometers of each other. Energy then transfers from one to the other (FRET), producing a bright green dot under the microscope.

Counting those dots lets us measure aggregation, and whether a compound prevents it.

How a tau biosensor cell reports aggregation Tau tagged with CFP and YFP floats freely and emits no FRET signal. When seeded tau aggregates, the tags come within 10 nanometers, producing a bright FRET signal. An effective inhibitor keeps tau apart, so the signal stays low. Resting tagged tau floats freely · no signal + seed Aggregated tags within 10 nm · bright FRET signal + inhibitor Inhibited tau kept apart · signal stays low
Schematic. Green fluorescent dots indicate aggregated tau protein.

Plant-based

We work with naturally occurring flavonoids and plant extracts, selected for tolerability and suitability as dietary ingredients.

Mechanism-first

Every candidate is chosen for a specific, testable mechanism: interfering with tau aggregation.

Transparent

Our work so far is preclinical. We will share findings as they are published, and we will be clear about what they do and don’t show.

Stay current

Follow tau research as it’s published

Our live feed tracks new tau papers from PubMed-indexed journals, updated continuously.

Latest tau research