Invited lectures-Effects of membrane and metal ion interactions with amyloidogenic proteins

摘要

Neurodegenerative disorders such as Alzheimer Disease (AD), Parkinson Disease (PD) and Transmisible Spongform Encelapthaties (TSEs) are increasingly widespread and highly debilitating diseases, characterized by the progressive loss of neuron structure and function, which ultimately leads to neuronal death. The major hallmark of AD, PD and TSEs pathologies is the presence of inclusion bodies mainly made of protein aggregates in the brain, consisting of fibers assembled by misfolded proteins with β-sheet conformation. Amyloid β (Aβ), α- Synuclein (aS) and human Prion Protein (hPrP) are the amyloidogenic proteins associated to AD, PD and TSEs respectively. They are native unfolded but, after misfolding aggregate and accumulate as deposits in the brain. Aβ, αS also share the ability to undergo to α-helix structural transition in presence of membrane mimicking environments [see for example 1, 2].