Oligomers imaging of amyloid-β_(1-42) by scanning tunneling microscopy

摘要

Amyloid-beta(1-42) (A beta 42) peptide, identified as more toxic than beta(1-40), rapidly aggregates to form oligomers. The information of the detailed oligomer structures should play a pivotal role to understand the process en route to the deposition of amyloid plaques associated with Alzheimer's disease. Due to the diversity of the A beta 42 aggregates and the instability, the A beta 42 oligomeric structures still remain under discussion. We have discussed the structure models of A beta 42 oligomers and fibrils using the topographic imaging of atomic force microscopy and scanning tunneling microscopy, with visualizing oligomer species by native gel electrophoresis. The obtained images with the height profiles reveal the structural features of A beta 42 oligomers, based on proposed A beta 42 fibril atomic structures having a dimeric feature. (C) 2019 The Japan Society of Applied Physics