Probing Interfacial Charge Transfer between Amyloid-β and Graphene during Amyloid Fibrillization Using Raman Spectroscopy.

Abstract

Charge transfer plays a key role in the structural transformation of amyloid-β proteins (Aβs), as it fibrillizes from small monomers to intermediate oligomers and to ordered fibrils. While the protein fibrillization states have been identified using cryo-electron microscopy, X-ray diffraction, Raman, infrared, terahertz spectroscopies, <i>etc.</i>, there is little known about the electronic states during the fibrilization of Aβ protein. Here, we probe the charge transfer of Aβ₄₂ proteins at different aggregation stages adsorbed on monolayer graphene (Gr) and molybdenum disulfide (MoS₂) using Raman spectroscopy. Monomers, oligomers, and fibrils prepared in buffer solutions were deposited and dried separately on Gr and MoS₂ where well-established characteristic Raman modes (G, 2D for Gr and E_2g, A_1g for MoS₂) were monitored. The shifts in Raman parameters showed that the small Aβ monomers withdraw electrons, whereas fibrils donate electrons to Gr and MoS₂. Oligomers undergo transient charge states near the neutrality point. This is explained in terms of modulated carrier concentration in Gr and MoS₂. This finding provides insight into the electronic properties of Aβs that could be essential to identifying the onset of toxic fibril forms and developing a straightforward, label-free diagnosis using Gr and MoS₂.