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Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots

Amyloidosis refers to aggregates of protein that accumulate and are deposited as amyloid fibrils into plaques. When these are detected in organs, they are the main hallmark of Alzheimer’s disease, Parkinson’s disease, and other related diseases. Recent medical advances have shown that many precursor...

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Autores principales: Lin, Xuguang, Galaqin, Nuomin, Tainaka, Reina, Shimamori, Keiya, Kuragano, Masahiro, Noguchi, Taro Q. P., Tokuraku, Kiyotaka
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7139405/
https://www.ncbi.nlm.nih.gov/pubmed/32183170
http://dx.doi.org/10.3390/ijms21061978
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author Lin, Xuguang
Galaqin, Nuomin
Tainaka, Reina
Shimamori, Keiya
Kuragano, Masahiro
Noguchi, Taro Q. P.
Tokuraku, Kiyotaka
author_facet Lin, Xuguang
Galaqin, Nuomin
Tainaka, Reina
Shimamori, Keiya
Kuragano, Masahiro
Noguchi, Taro Q. P.
Tokuraku, Kiyotaka
author_sort Lin, Xuguang
collection PubMed
description Amyloidosis refers to aggregates of protein that accumulate and are deposited as amyloid fibrils into plaques. When these are detected in organs, they are the main hallmark of Alzheimer’s disease, Parkinson’s disease, and other related diseases. Recent medical advances have shown that many precursors and proteins can induce amyloidosis even though the mechanism of amyloid aggregation and the relationship of these proteins to amyloidosis remains mostly unclear. In this study, we report the real-time 3D-imaging and inhibition analysis of amyloid β (Aβ), tau, and α-synuclein aggregation utilizing the affinity between quantum dots (QD) and amyloid aggregates. We successfully visualized these amyloid aggregations in real-time using fluorescence microscopy and confocal microscopy simply by adding commercially available QD. The observation by transmission electron microscopy (TEM) showed that QD particles bound to all amyloid fibrils. The 3D-imaging with QD revealed differences between amyloid aggregates composed of different amyloid peptides that could not be detected by TEM. We were also able to quantify the inhibition activities of these proteins by rosmarinic acid, which has high activity for Aβ aggregation, from fluorescence micrographs as half-maximal effective concentrations. These imaging techniques with QD serve as quick, easy, and powerful tools to understand amyloidosis and to discover drugs for therapies.
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spelling pubmed-71394052020-04-10 Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots Lin, Xuguang Galaqin, Nuomin Tainaka, Reina Shimamori, Keiya Kuragano, Masahiro Noguchi, Taro Q. P. Tokuraku, Kiyotaka Int J Mol Sci Article Amyloidosis refers to aggregates of protein that accumulate and are deposited as amyloid fibrils into plaques. When these are detected in organs, they are the main hallmark of Alzheimer’s disease, Parkinson’s disease, and other related diseases. Recent medical advances have shown that many precursors and proteins can induce amyloidosis even though the mechanism of amyloid aggregation and the relationship of these proteins to amyloidosis remains mostly unclear. In this study, we report the real-time 3D-imaging and inhibition analysis of amyloid β (Aβ), tau, and α-synuclein aggregation utilizing the affinity between quantum dots (QD) and amyloid aggregates. We successfully visualized these amyloid aggregations in real-time using fluorescence microscopy and confocal microscopy simply by adding commercially available QD. The observation by transmission electron microscopy (TEM) showed that QD particles bound to all amyloid fibrils. The 3D-imaging with QD revealed differences between amyloid aggregates composed of different amyloid peptides that could not be detected by TEM. We were also able to quantify the inhibition activities of these proteins by rosmarinic acid, which has high activity for Aβ aggregation, from fluorescence micrographs as half-maximal effective concentrations. These imaging techniques with QD serve as quick, easy, and powerful tools to understand amyloidosis and to discover drugs for therapies. MDPI 2020-03-13 /pmc/articles/PMC7139405/ /pubmed/32183170 http://dx.doi.org/10.3390/ijms21061978 Text en © 2020 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
Lin, Xuguang
Galaqin, Nuomin
Tainaka, Reina
Shimamori, Keiya
Kuragano, Masahiro
Noguchi, Taro Q. P.
Tokuraku, Kiyotaka
Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots
title Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots
title_full Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots
title_fullStr Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots
title_full_unstemmed Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots
title_short Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots
title_sort real-time 3d imaging and inhibition analysis of various amyloid aggregations using quantum dots
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7139405/
https://www.ncbi.nlm.nih.gov/pubmed/32183170
http://dx.doi.org/10.3390/ijms21061978
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