摘要 : Charge transfer plays a key role in the structural transformation of amyloid-ss proteins (A ss s), as it fibrillizes from small monomers to intermediate oligomers and to ordered fibrils. While the protein fibrillization states hav... 展开 Charge transfer plays a key role in the structural transformation of amyloid-ss proteins (A ss s), 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, etc., there is little known about the electronic states during the fibrilization of A ss protein. Here, we probe the charge transfer of A ss(42) 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 A ss 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 A ss s that could be essential to identifying the onset of toxic fibril forms and developing a straightforward, label-free diagnosis using Gr and MoS2. 收起