Event:

Protein misfolding and aggregation are implicated in neurodegenerative disorders. While the kinetics of fiber formation and high-resolution structure of fibrils and their polymorphic nature have been well investigated, obtaining structural information on the most toxic intermediate species of amyloid proteins has been a major challenge. My research group has been investigating the high-resolution structures of early amyloid intermediates, amyloid-membrane interaction and membrane disruption, and the interaction of polyphenols with amyloid peptides.[1,2] In my presentation, kinetics of formation and NMR structures of early intermediates of amyloid peptides, mechanisms of amyloid-induced membrane disruption, and amyloid inhibition by small molecule compounds will be discussed. Particularly, our recent
studies on the membrane interaction and cell toxicity of amyloid-beta, implicated in Alzheimer’s Disease, and islet amyloid polypeptide (IAPP, or also known as amylin), implicated in Type-2 diabetes, will be discussed.