Figure 6
From: Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β1–42 fibril formation
Aβ1-42 monomer adsorbing on the surface of few-layer Bi2Se3. (a) CD spectra of Aβ1-42 with and without few-layer Bi2Se3. (1): Aβ1-42 monomer, (2-4): Aβ1-42 was incubated at 37°C for 3 h in the presence of few-layer Bi2Se3 with different concentrations (2: 0, 3: 120 and 4: 2400 ng mL-1, respectively). (b) Nyquist diagrams of few-layer Bi2Se3-modified GCE before and after adsorption of freshly prepared Aβ1-42 monomer. Inset: equivalent circuit used to model impedance data in the presence of redox couples. Rs, electrolyte solution resistance; Rct, interfacial electron transfer resistance; C, capacitance of the electric double layer between electrolyte and interface of electrode. The concentrations of few-layer Bi2Se3 and Aβ1-42 monomer were 10 μg mL-1 and 10 μM, respectively. (c) Impedance at 10 Hz with time for few-layer Bi2Se3-modified GCE immersed in modified Krebs-Henseliet buffer. Buffer was added twice at 30 and 90 min, respectively. Aβ1-42 monomer was added at 60 min. (d) Weight increment (ΔWt) with time was measured for few-layer Bi2Se3 coating silicon slice which was immersed in modified Krebs-Henseliet buffer containing 10 μM freshly-prepared Aβ1-42 monomers.
