Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites
Amyloid-beta proteins that form cytotoxic aggregates called amyloid-β derived diffusible ligands are responsible for various neurodegenerative diseases like Alzheimer’s and Parkinson’s disease. Novel methods for the early detection of such aggregates and inhibition of further fibrillation are highly...
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sg-ntu-dr.10356-1486022023-10-21T16:48:10Z Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites Nair, Radhika Vadakkini Padmanabhan, Parasuraman Gulyás, Balázs Murukeshan, Vadakke Matham School of Mechanical and Aerospace Engineering Lee Kong Chian School of Medicine (LKCMedicine) Centre for Optical and Laser Engineering Science::Physics::Optics and light Alzheimer’s Disease Plasmonics Amyloid-beta proteins that form cytotoxic aggregates called amyloid-β derived diffusible ligands are responsible for various neurodegenerative diseases like Alzheimer’s and Parkinson’s disease. Novel methods for the early detection of such aggregates and inhibition of further fibrillation are highly important and need in the current situation. In this paper, we present a novel method based on fluorescence resonance energy transfer (FRET) between carbon dots and Ag nanoparticle for sensing various fibrillation stages of beta-amyloid proteins. The addition of Ag nanoparticles to carbon dot colloid is found to significantly enhance the inhibition of beta-amyloid fibrillation due to the modified hydrophobic and electrostatic interactions introduced by Ag nanoparticles and is monitored using thioflavin T (ThT) assay. Further, fluorescence quenching of carbon dots in the presence of Ag particles is found to get reduced with the increase in the incubation time of beta-amyloid fibrils. We could observe a linear trend in the variation of Stern–Volmer constants calculated based on FRET between carbon dots and Ag nanoparticles with the incubation time of beta-amyloid, indicating the potential of using the proposed FRET-based method for sensing beta-amyloid fibrillation. Economic Development Board (EDB) Ministry of Education (MOE) Submitted/Accepted version The authors acknowledge NTU, COLE-EDB, and Ministry of Education, MoE Singapore (RG 192/17) for financial support. B.G. and P.P. thank the support from Lee Kong Chian School of Medicine Imaging Probe Development Platform and the support from the Cognitive Neuro Imaging Centre (CONIC) at NTU 2021-06-03T05:54:57Z 2021-06-03T05:54:57Z 2021 Journal Article Nair, R. V., Padmanabhan, P., Gulyás, B. & Murukeshan, V. M. (2021). Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites. Plasmonics, 16(3), 863-872. https://dx.doi.org/10.1007/s11468-020-01338-w 1557-1963 0000-0002-4370-2112 https://hdl.handle.net/10356/148602 10.1007/s11468-020-01338-w 2-s2.0-85099030196 3 16 863 872 en RG192/17 Plasmonics © 2021 Springer Science Business Media, LLC, part of Springer Nature. All rights reserved. This article may be downloaded for personal use only. Any other use requires prior permission of the copyright holder. The Version of Record is available online at http://doi.org/10.1007/s11468-020-01338-w. application/pdf application/pdf |
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Science::Physics::Optics and light Alzheimer’s Disease Plasmonics Nair, Radhika Vadakkini Padmanabhan, Parasuraman Gulyás, Balázs Murukeshan, Vadakke Matham Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites |
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Amyloid-beta proteins that form cytotoxic aggregates called amyloid-β derived diffusible ligands are responsible for various neurodegenerative diseases like Alzheimer’s and Parkinson’s disease. Novel methods for the early detection of such aggregates and inhibition of further fibrillation are highly important and need in the current situation. In this paper, we present a novel method based on fluorescence resonance energy transfer (FRET) between carbon dots and Ag nanoparticle for sensing various fibrillation stages of beta-amyloid proteins. The addition of Ag nanoparticles to carbon dot colloid is found to significantly enhance the inhibition of beta-amyloid fibrillation due to the modified hydrophobic and electrostatic interactions introduced by Ag nanoparticles and is monitored using thioflavin T (ThT) assay. Further, fluorescence quenching of carbon dots in the presence of Ag particles is found to get reduced with the increase in the incubation time of beta-amyloid fibrils. We could observe a linear trend in the variation of Stern–Volmer constants calculated based on FRET between carbon dots and Ag nanoparticles with the incubation time of beta-amyloid, indicating the potential of using the proposed FRET-based method for sensing beta-amyloid fibrillation. |
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School of Mechanical and Aerospace Engineering |
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School of Mechanical and Aerospace Engineering Nair, Radhika Vadakkini Padmanabhan, Parasuraman Gulyás, Balázs Murukeshan, Vadakke Matham |
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Article |
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Nair, Radhika Vadakkini Padmanabhan, Parasuraman Gulyás, Balázs Murukeshan, Vadakke Matham |
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Nair, Radhika Vadakkini |
title |
Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites |
title_short |
Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites |
title_full |
Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites |
title_fullStr |
Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites |
title_full_unstemmed |
Fluorescence resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites |
title_sort |
fluorescence resonance energy transfer (fret)-based tht free sensing of beta-amyloid fibrillation by carbon dot-ag composites |
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2021 |
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https://hdl.handle.net/10356/148602 |
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