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A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits
Published on: February 16, 2014
Rescuing recombinant proteins by sequestration into the P22 VLP
Dustin P Patterson1, Benjamin LaFrance, Trevor Douglas
1Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
Chemical Communications (Cambridge, England)
|October 1, 2013
Summary
Protein cages can rescue difficult-to-produce soluble proteins. This self-assembling protein technology offers a novel solution for protein production challenges.
Area of Science:
- Biochemistry
- Protein Engineering
- Molecular Biology
Background:
- Recombinant proteins often form insoluble inclusion bodies during production.
- This limits the yield and utility of many valuable proteins.
Purpose of the Study:
- To investigate the use of self-assembling protein cages for sequestering and solubilizing recombinant proteins.
- To establish protein cages as a viable method for producing otherwise intractable proteins.
Main Methods:
- Utilized self-assembling protein cages as a delivery vehicle.
- Applied protein cage technology to capture and maintain protein solubility.
Main Results:
- Successfully sequestered and solubilized recombinant proteins.
- Demonstrated the ability of protein cages to prevent aggregation into inclusion bodies.
- Obtained soluble proteins that are typically difficult to produce.
Conclusions:
- Self-assembling protein cages are effective vehicles for rescuing and producing soluble recombinant proteins.
- This approach offers a novel strategy to overcome challenges in protein production and enhance protein yields.
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