Amyloid polypeptide aggregation is considered one of the factors involved in the pathogenesis of Alzheimer's disease (AD) and type 2 diabetes (T2D), and the number of affected patients increases as the population ages. Amyloid β (Aβ) found in the brain of patients with AD and human islet amyloid polypeptide (hIAPP) found in the pancreas of patients with T2D are thought to be cytotoxic during the aggregation process, especially the low-molecular-weight oligomers that are aggregation intermediates. In this study, meroterpenoids isolated and structurally determined from the brown alga Sargassum macrocarpum were evaluated for their ability to inhibit hIAPP aggregation.
View Article and Find Full Text PDFAmyloid β (Aβ) is thought to be involved in the pathogenesis of Alzheimer's disease (AD). Aβ aggregation in the brain is considered the cause of AD. Therefore, inhibiting Aβ aggregation and degrading existing Aβ aggregates is a promising approach for the treatment and prevention of the disease.
View Article and Find Full Text PDFThe structure and inhibitory activity of advanced glycation end products (AGEs) formation were studied using six model compounds and seven phlorotannins isolated from brown alga Ecklonia stolonifera. As a result, it was inferred that AGEs formation inhibitory activity was stronger when electron-rich groups were present because of the addition of many oxygen atoms to the phlorotannins.
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