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

Qi Hu, Haozhen Hu, Xinyi Zhang, Kyle Fan, Yuning Hong, Colin L. Raston, Youhong Tang

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Article number4273
Number of pages11
JournalMolecules
Volume26
Issue number14
DOIs
Publication statusPublished - 2 Jul 2021

Keywords

  • Aggregation induced emission
  • Protein folding/unfolding
  • Vortex fluidic device

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