Researchers at Kumamoto University have discovered a natural compound from pomegranate leaves and branches that has the capability to dismantle protein aggregates linked to transthyretin amyloidosis (TTR). This condition can severely impair nerve and heart function, making effective treatments critical.
The scientists identified a specific compound, known as 1,2,3,4,6-penta-O-galloyl-?-D-glucose (PGG), in a study published in the journal iScience. In TTR amyloidosis, the transthyretin protein changes shape and forms insoluble aggregates called amyloid fibrils, which accumulate in organs. Current treatment approaches primarily aim to stabilize the protein or reduce its production, yet none effectively eliminate existing deposits.
To find alternatives, the research team screened 1,509 plant extracts for their ability to disrupt existing TTR fibrils. Extracts from pomegranate leaves and branches proved particularly promising. After extensive analysis, they confirmed that PGG was the pivotal component responsible for this disruptive action.
Experimental findings indicated that PGG could effectively dismantle amyloid fibrils from both normal and mutated forms of the TTR protein without affecting amyloid-? fibrils associated with Alzheimer’s disease. This selectivity suggests that PGG interacts specifically with TTR aggregates, which could limit side effects.
Further investigations in a model organism, the nematode C. elegans, demonstrated that PGG treatment resulted in reduced protein deposits and enhanced lifespan and healthspan. Additionally, PGG was effective on fibrils derived from the heart tissue of patients with hereditary TTR amyloidosis, reinforcing its potential clinical relevance.
While additional research is necessary to assess safety and efficacy in humans, these findings suggest that PGG and similar plant-derived compounds may eventually lead to innovative treatments targeting TTR amyloidosis.
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