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Oligomers imaging of amyloid-β1-42 by scanning tunneling microscopy

Amyloid-β1-42 (Aβ42) peptide, identified as more toxic than β1-40, 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 Aβ42 aggregates and the instability, the Aβ42 oligomeric structures still remain under discussion. We have discussed the structure models of Aβ42 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 Aβ42 oligomers, based on proposed Aβ42 fibril atomic structures having a dimeric feature.