Multifunctional Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-beta 40
- Multifunctional Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-beta 40
- 김승민; 양승훈; Dahye Jeong; Jinsik Kim; Myung-Sic Chae; Wonseok Lee; YoungSoo Kim; Jin San Lee; Jeong Hoon Lee; Jungkyu Choi; Dae Sung Yoon; Kyo Seon Hwang
- Issue Date
- VOL 18, NO 6-14
- Determination of the conformation (monomer, oligomer, or fibril) of amyloid peptide aggregates in the human brain is essential for the diagnosis and treatment of Alzheimer’s disease (AD). Accordingly, systematic investigation of amyloid conformation using analytical tools is essential for precisely quantifying the relative amounts of the three conformations of amyloid peptide. Here, we developed a reduced graphene oxide (rGO) based multiplexing biosensor that could be used to monitor the relative amounts of the three conformations of various amyloid-β 40 (Aβ40) fluids. The electrical rGO biosensor was composed of a multichannel sensor array capable of individual detection of monomers, oligomers, and fibrils in a single amyloid fluid sample. From the performance test of each sensor, we showed that this method had good analytical sensitivity (1 pg/mL) and a fairly wide dynamic range (1 pg/mL to 10 ng/mL) for each conformation of Aβ40. To verify whether the rGO biosensor could be used to evaluate the relative amounts of the three conformations, various amyloid solutions (monomeric Aβ40, aggregated Aβ40, and disaggregated Aβ40 solutions) were employed. Notably, different trends in the relative amounts of the three conformations were observed in each amyloid solution, indicating that this information could serve as an important parameter in the clinical setting. Accordingly, our analytical tool could precisely detect the relative amounts of the three conformations of Aβ40 and may have potential applications as a diagnostic system for AD.
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