Zhiyuan is a 6th-year graduate student working with his advisor, Dr. Feng Ding, in Biophysics.. Check out his paper here.
“Proteins like amyloid-beta (Aβ) and islet amyloid polypeptide (IAPP) can misfold and form structures called amyloid fibrils, which are linked to diseases like Alzheimer’s (AD) and type 2 diabetes (T2D). We used physics-based molecular dynamics simulations to study how preformed IAPP fibrils interact with Aβ, potentially explaining why having T2D increases the risk of AD. We found that IAPP fibrils can speed up Aβ aggregation by providing surfaces that encourage Aβ molecules to bind and form initial clusters, a process called “cross-seeding.” However, Aβ and IAPP do not easily form stable hybrid fibrils, meaning their interactions likely involve temporary binding rather than permanent mixing. The study also showed that these interactions depend on where Aβ binds to the IAPP fibril—different surfaces influence how Aβ molecules group together. This research helps explain how diseases like AD and T2D might be biologically connected, offering insights for understanding disease mechanisms and designing new treatments.”
