Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor

Soheila Mohammadi,1 Maryam Nikkhah,1 Saman Hosseinkhani2 1Department of Nanobiotechnology, 2Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran Abstract: The aggregation of alpha-synuclein (αS), natively unstructured presynaptic protein, i...

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Autores principales: Mohammadi S, Nikkhah M, Hosseinkhani S
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Publicado: Dove Medical Press 2017
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spelling oai:doaj.org-article:2707528d23b64880a92716fa6051ac782021-12-02T05:10:25ZInvestigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor1178-2013https://doaj.org/article/2707528d23b64880a92716fa6051ac782017-12-01T00:00:00Zhttps://www.dovepress.com/investigation-of-the-effects-of-carbon-based-nanomaterials-on-a53t-alp-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Soheila Mohammadi,1 Maryam Nikkhah,1 Saman Hosseinkhani2 1Department of Nanobiotechnology, 2Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran Abstract: The aggregation of alpha-synuclein (αS), natively unstructured presynaptic protein, is a crucial factor leading to the pathogenesis of Parkinson’s disease (PD) and other related disorders. Recent studies have shown prefibrillar and oligomeric intermediates of αS as toxic to the cells. Herein, split-luciferase complementation assay is used to design a “signal-on” biosensor to monitor oligomerization of A53T αS inside the cells. Then, the effect of carbon-based nanomaterials, such as graphene quantum dots (GQDs) and graphene oxide quantum dots (GOQDs), on A53T αS oligomerization in vitro and in living cells is investigated. In this work, for the first time, it was found that GQDs at a concentration of 0.5 µg/mL can promote A53T αS aggregation by shortening the nucleation process, which is the key rate-determining step of fibrillation, thereby making a signal-on biosensor. While these nanomaterials may cross the blood–brain barrier because of their small sizes, the interaction between αS and GQDs may contribute to PD etiology. Keywords: αS, aggregation, split luciferase, luminescent biosensor, GQDs Mohammadi SNikkhah MHosseinkhani SDove Medical Pressarticleα-synuclein (αS)split luciferaseluminescent biosensorgraphene quantum dots (GQDs)Medicine (General)R5-920ENInternational Journal of Nanomedicine, Vol Volume 12, Pp 8831-8840 (2017)
institution DOAJ
collection DOAJ
language EN
topic α-synuclein (αS)
split luciferase
luminescent biosensor
graphene quantum dots (GQDs)
Medicine (General)
R5-920
spellingShingle α-synuclein (αS)
split luciferase
luminescent biosensor
graphene quantum dots (GQDs)
Medicine (General)
R5-920
Mohammadi S
Nikkhah M
Hosseinkhani S
Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor
description Soheila Mohammadi,1 Maryam Nikkhah,1 Saman Hosseinkhani2 1Department of Nanobiotechnology, 2Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran Abstract: The aggregation of alpha-synuclein (αS), natively unstructured presynaptic protein, is a crucial factor leading to the pathogenesis of Parkinson’s disease (PD) and other related disorders. Recent studies have shown prefibrillar and oligomeric intermediates of αS as toxic to the cells. Herein, split-luciferase complementation assay is used to design a “signal-on” biosensor to monitor oligomerization of A53T αS inside the cells. Then, the effect of carbon-based nanomaterials, such as graphene quantum dots (GQDs) and graphene oxide quantum dots (GOQDs), on A53T αS oligomerization in vitro and in living cells is investigated. In this work, for the first time, it was found that GQDs at a concentration of 0.5 µg/mL can promote A53T αS aggregation by shortening the nucleation process, which is the key rate-determining step of fibrillation, thereby making a signal-on biosensor. While these nanomaterials may cross the blood–brain barrier because of their small sizes, the interaction between αS and GQDs may contribute to PD etiology. Keywords: αS, aggregation, split luciferase, luminescent biosensor, GQDs 
format article
author Mohammadi S
Nikkhah M
Hosseinkhani S
author_facet Mohammadi S
Nikkhah M
Hosseinkhani S
author_sort Mohammadi S
title Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor
title_short Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor
title_full Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor
title_fullStr Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor
title_full_unstemmed Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor
title_sort investigation of the effects of carbon-based nanomaterials on a53t alpha-synuclein aggregation using a whole-cell recombinant biosensor
publisher Dove Medical Press
publishDate 2017
url https://doaj.org/article/2707528d23b64880a92716fa6051ac78
work_keys_str_mv AT mohammadis investigationoftheeffectsofcarbonbasednanomaterialsona53talphasynucleinaggregationusingawholecellrecombinantbiosensor
AT nikkhahm investigationoftheeffectsofcarbonbasednanomaterialsona53talphasynucleinaggregationusingawholecellrecombinantbiosensor
AT hosseinkhanis investigationoftheeffectsofcarbonbasednanomaterialsona53talphasynucleinaggregationusingawholecellrecombinantbiosensor
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