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In situ monitored vortex fluidic-mediated protein refolding/unfolding using an aggregation-induced emission bioprobe

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journal contribution
posted on 10.08.2021, 00:48 by Q Hu, H Hu, X Zhang, K Fan, Yuning HongYuning Hong, CL Raston, Y Tang
Protein folding is important for protein homeostasis/proteostasis in the human body. We have established the ability to manipulate protein unfolding/refolding for β-lactoglobulin using the induced mechanical energy in the thin film microfluidic vortex fluidic device (VFD) with monitoring as such using an aggregation-induced emission luminogen (AIEgen), TPE-MI. When denaturant (guanidine hydrochloride) is present with β-lactoglobulin, the VFD accelerates the denaturation reaction in a controlled way. Conversely, rapid renaturation of the unfolded protein occurs in the VFD in the absence of the denaturant. The novel TPE-MI reacts with exposed cysteine thiol when the protein unfolds, as established with an increase in fluorescence intensity. TPE-MI provides an easy and accurate way to monitor the protein folding, with comparable results established using conventional circular dichroism. The controlled VFD-mediated protein folding coupled with in situ bioprobe AIEgen monitoring is a viable methodology for studying the denaturing of proteins.

Funding

Q. Hu is grateful for the financial support from Postgraduate Research Scholarships (International) for his study at Flinders University. Y. Hong and Y. Tang is grateful for the support from Australia-China Science and Research Fund-Joint Research Centre on Personal Health Technologies. This work is also supported by the Australia Research Council (DP200101106).

History

Publication Date

02/07/2021

Journal

Molecules

Volume

26

Issue

14

Article Number

4273

Pagination

(p. 1-11)

Publisher

MDPI

ISSN

1420-3049

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