Researchers at Kumamoto University have discovered a compound in pomegranate leaves and branches that can effectively break apart protein aggregates linked to transthyretin amyloidosis, a condition that can cause serious damage to nerves and the heart. This discovery highlights a potential new avenue for medical treatment.
The compound, named 1,2,3,4,6-penta-O-galloyl-?-D-glucose (PGG), was identified as an “amyloid disruptor.” In transthyretin amyloidosis, the transthyretin protein can misfold, forming amyloid fibrils that accumulate in organs. Most current treatments aim to stabilise the protein or reduce its production, but once these fibrils form, it is challenging to remove them.
To find effective solutions, the research team screened over 1,500 plant extracts. They found that extracts from pomegranate clearly stood out for their ability to disrupt existing TTR fibrils. They focused specifically on the compound PGG, which showed remarkable efficacy.
In lab experiments, PGG broke down amyloid fibrils from both normal and mutated forms of TTR without affecting amyloid-? fibrils related to Alzheimer’s disease. This specificity suggests that PGG works by targeting TTR aggregates selectively.
When tested in a model organism, C. elegans, engineered to produce TTR fragments, those treated with PGG showed fewer protein deposits and a notable increase in both lifespan and healthspan. Furthermore, PGG was also effective against amyloid fibrils obtained from a patient’s heart tissue, confirming its potential in practical applications.
Despite the need for further research on safety and effectiveness in humans, these findings suggest that PGG could be a promising candidate for future treatments, helping to remove harmful amyloid deposits in transthyretin amyloidosis.
Test Your Understanding
How much do you know?
