Wang, Shih Ting, Lin, Yiyang, Hsu, Chia Chen et al. (3 more authors) (2017) Probing amylin fibrillation at an early stage via a tetracysteine-recognising fluorophore. Talanta. pp. 44-50. ISSN 0039-9140
Abstract
Amyloid fibrillation is a nucleation-dependent process known be involved in the development of more than 20 progressive and chronic diseases. The detection of amyloid formation at the nucleation stage can greatly advance early diagnoses and treatment of diseases. In this work, we developed a new assay for the early detection of amylin fibrillation using the biarsenical dye 4,5-bis(1,3,2-dithiarsolan-2-yl)fluorescein (FlAsH), which could recognise tetracysteine motifs and transform from non-fluorescent form into strongly fluorescent complexes. Due to the close proximity of two cysteine residues within the hydrophilic domain of amylin, a non-contiguous tetracysteine motif can form upon amylin dimerisation or oligomerisation, which can be recognised by FlAsH and emit strong fluorescence. This enables us to report the nucleation-growth process of amylin without modification of the protein sequence. We showed that the use of this assay not only allowed the tracking of initial nucleation events, but also enabled imaging of amyloid fibrils and investigation of the effects of amyloid inhibitor/modulator toward amylin fibrillation.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 The Author(s). Published by Elsevier B.V. |
Keywords: | Amylin,Amyloid inhibitor,Early detection,Fibrillation,FlAsH,Glycosaminoglycan |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 07 Sep 2018 09:30 |
Last Modified: | 26 Nov 2024 00:39 |
Published Version: | https://doi.org/10.1016/j.talanta.2017.05.015 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.talanta.2017.05.015 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:135439 |
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