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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
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A Rapid Method for Refolding Cell Surface Receptors and Ligands.
Lu Zhai1,2, Ling Wu1, Feng Li1
1Department of Biochemistry, Virginia Polytechnic Institute &State University, Blacksburg, VA 24061, USA.
Scientific Reports
|May 25, 2016
Summary
Researchers developed a rapid, one-day method for refolding cell surface receptors and ligands from inclusion bodies. This technique streamlines protein production, enabling faster structural and functional studies of these vital proteins.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Producing membrane-associated cell surface receptors and ligands is complex, costly, and slow.
- This difficulty hinders detailed structural and functional protein characterization.
Purpose of the Study:
- To develop a rapid method for refolding recombinant cell surface receptors and ligands.
- To enable faster production of these proteins for research.
Main Methods:
- Coupling on-column immobilized metal ion affinity purification with solid-phase protein refolding.
- Refolding inclusion-body-based proteins in a single day.
Main Results:
- Successfully produced functional immunoreceptors, ligands, and viral decoys.
- Demonstrated utility for challenging cell surface proteins.
- Achieved production speeds comparable to soluble proteins.
Conclusions:
- The new method significantly accelerates the production of cell surface receptors and ligands.
- This approach overcomes limitations of traditional refolding techniques.
- Facilitates broader structural and functional analysis of cell surface proteins.
