"By studying animal models, human neurons and brain tissue from high-risk patients, the team discovered a particularly toxic protein fragment, called amyloid-beta 42, accumulates inside neurons' synaptic vesicles - the tiny packets that neurons use to send signals. But, when the scientists administered levetiracetam (an inexpensive, decades‑old anti‑seizure drug) to the animals and human neurons, the drug prevented neurons from forming amyloid-beta 42."
""While many of the Alzheimer's drugs currently on the market, such as lecanemab and donanemab, are approved to clear existing amyloid plaques, we've identified this mechanism that prevents the production of the amyloid‑beta 42 peptides and amyloid plaques," said corresponding author Jeffrey Savas, PhD, associate professor in the Ken and Ruth Davee Department of Neurology's Division of Behavioral Neurology at Northwestern University Feinberg School of Medicine."
""Our new results uncovered new biology while also opening doors for new drug targets.""
Amyloid-beta 42 accumulates inside neurons' synaptic vesicles, the tiny packets that neurons use to send signals. Abnormal processing of amyloid precursor protein (APP) generates amyloid-beta peptides linked to Alzheimer's pathology. Levetiracetam, an FDA-approved anti-seizure drug, prevents intracellular formation of amyloid-beta 42 in animal models, human neurons, and high-risk brain tissue. Existing therapies such as lecanemab and donanemab clear extracellular plaques, whereas levetiracetam blocks production of toxic peptides before plaque formation. Preventing intracellular amyloid-beta 42 production identifies new drug targets and suggests a preventative strategy complementary to plaque-clearing approaches.
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