Electrical characteristics of amyloid beta peptides in vertical junctions

Abstract Assembled amyloid beta (Aβ) peptides have been considered pathological assemblies involved in human brain diseases, and the electron transfer or transport characteristics of Aβ are important for formation structured assemblies. Here, we report electrical surface-assembled similar to those observed Alzheimer’s patients. These correlate their characteristics. Electrical current–voltage plots vertical junction devices show sequence dependence current densities at both monomers ( mono -Aβs) oligomers oli -Aβs), while is not clearly planar field effect transistors (FETs). In particular, surface oligomerization drastically decreases activity transfer, which presents a change pathway junctions. Electron oli- junctions symmetric (tunneling/tunneling) due weak voltage-independent coupling less redox-reactive -Aβ contacts, that asymmetric (hopping/tunneling) redox levels voltage-dependently coupled with contact electrodes. Consequently, through junctions, sequence- conformation-dependent Aβs can reveal activities.