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

Authors Mohammadi S, Nikkhah M, Hosseinkhani S

Received 24 June 2017

Accepted for publication 29 September 2017

Published 14 December 2017 Volume 2017:12 Pages 8831—8840


Checked for plagiarism Yes

Review by Single anonymous peer review

Peer reviewer comments 2

Editor who approved publication: Dr Thomas Webster

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

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