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Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40

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...

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Autores principales: Jeong, Dahye, Kim, Jinsik, Chae, Myung-Sic, Lee, Wonseok, Yang, Seung-Hoon, Kim, YoungSoo, Kim, Seung Min, Lee, Jin San, Lee, Jeong Hoon, Choi, Jungkyu, Yoon, Dae Sung, Hwang, Kyo Seon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6022081/
https://www.ncbi.nlm.nih.gov/pubmed/29843431
http://dx.doi.org/10.3390/s18061738
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author Jeong, Dahye
Kim, Jinsik
Chae, Myung-Sic
Lee, Wonseok
Yang, Seung-Hoon
Kim, YoungSoo
Kim, Seung Min
Lee, Jin San
Lee, Jeong Hoon
Choi, Jungkyu
Yoon, Dae Sung
Hwang, Kyo Seon
author_facet Jeong, Dahye
Kim, Jinsik
Chae, Myung-Sic
Lee, Wonseok
Yang, Seung-Hoon
Kim, YoungSoo
Kim, Seung Min
Lee, Jin San
Lee, Jeong Hoon
Choi, Jungkyu
Yoon, Dae Sung
Hwang, Kyo Seon
author_sort Jeong, Dahye
collection PubMed
description 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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spelling pubmed-60220812018-07-02 Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40 Jeong, Dahye Kim, Jinsik Chae, Myung-Sic Lee, Wonseok Yang, Seung-Hoon Kim, YoungSoo Kim, Seung Min Lee, Jin San Lee, Jeong Hoon Choi, Jungkyu Yoon, Dae Sung Hwang, Kyo Seon Sensors (Basel) Article 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. MDPI 2018-05-28 /pmc/articles/PMC6022081/ /pubmed/29843431 http://dx.doi.org/10.3390/s18061738 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Jeong, Dahye
Kim, Jinsik
Chae, Myung-Sic
Lee, Wonseok
Yang, Seung-Hoon
Kim, YoungSoo
Kim, Seung Min
Lee, Jin San
Lee, Jeong Hoon
Choi, Jungkyu
Yoon, Dae Sung
Hwang, Kyo Seon
Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40
title Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40
title_full Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40
title_fullStr Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40
title_full_unstemmed Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40
title_short Multifunctionalized Reduced Graphene Oxide Biosensors for Simultaneous Monitoring of Structural Changes in Amyloid-β 40
title_sort multifunctionalized reduced graphene oxide biosensors for simultaneous monitoring of structural changes in amyloid-β 40
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6022081/
https://www.ncbi.nlm.nih.gov/pubmed/29843431
http://dx.doi.org/10.3390/s18061738
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