Ultrasensitive capacitance sensor to detect amyloid-beta 1-40 in human serum using supramolecular recognition of β-CD/RGO/ITO micro-disk electrode

In this paper, we developed a new ultrasensitive capacitance sensor for detection of amyloid beta 1-40 (aβ40) protein (one of Alzheimer's disease core biomarkers) in human serum based on the high supramolecular recognition of the β-cyclodextrin/reduced graphene oxide (β-CD/RGO) nanohybrid toward the anti-aβ40 antibody molecule. The sensor was established by immobilizing specific anti-aβ40 antibody onto the β-CD/RGO nanohybrid functionalized on indium tin oxide micro-disk electrode (anti-aβ40/β-CD/RGO/ITO). Detection of aβ40 in the human serum (HS) using the sensor anti-aβ40/β-CD/RGO/ITO is carried out by capacitance measurement without a redox probe to prevent protein denaturation, serving as a convenient strategy for point-of-care diagnosis. In comparison with other studies, the sensor shows a very low limit of detection of 0.69 fg mL−1 in HS, demonstrating its ability for the ultrasensitive detection of aβ40. Using this sensor, the dissociation constant KD of the binding interaction between anti-aβ40 and aβ40 in HS is found to be 2.9 × 10−7 nM, indicating the high binding affinity of antibody–antigen and the suitability of the anti-aβ40/β-CD/RGO/ITO sensor for aβ40 protein detection. The good selectivity of the anti-aβ40/β-CD/RGO/ITO sensor in the presence of differential analytes was also performed in this paper. [Display omitted] •First development a capacitance sensor for ultrasensitive detection of aβ40 using supramolecular recognition.•The sensor (anti-aβ40/β-CD/RGO/ITO) was established through host–guest inclusion complex.•Avoiding the denaturation of protein during the detection using the capacitance sensor.•A very low LOD (0.69 fg mL-1) and low KD (2.9×10-7 nM) of aβ40 in human serum.