作者: Michal Baram , Yoav Atsmon-Raz , Buyong Ma , Ruth Nussinov , Yifat Miller
DOI: 10.1039/C5CP03338A
关键词: Biochemistry 、 Aβ oligomers 、 Extramural 、 Single layer 、 Alzheimer's disease 、 Molecular dynamics 、 Chemistry 、 Double layer (biology) 、 Amylin 、 Atomic resolution 、 Biophysics
摘要: Clinical studies have identified Type 2 diabetes (T2D) as a risk factor of Alzheimer's disease (AD). One the potential mechanisms that link T2D and AD is loss cells associated with degenerative changes. Amylin1-37 aggregates (the pathological species in T2D) were found to be co-localized those Aβ1-42 AD) form Amylin1-37-Aβ1-42 plaques, promoting aggregation thus contributing etiology AD. However, by which co-aggregates are still elusive. This work presents interactions between oligomers at atomic resolution applying extensive molecular dynamics simulations for relatively large ensemble cross-seeding oligomers. The main conclusions this study first, prefer interact single layer conformations (in-register interactions) rather than double conformations; second, some oligomers, destabilize inhibit aggregation, while other conformations, stabilize promote aggregation.