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Using folding promoting agents in recombinant protein production: a review
1Cardiff School of Biosciences, Cardiff University, Wales, UK. FahnertB@cardiff.ac.uk
Methods in Molecular Biology (Clifton, N.J.)
|December 14, 2011
Summary
Using folding promoting agents enhances the production of functional recombinant proteins. Optimization is key, as strategies must be tailored to specific target proteins for successful in vivo application.
Area of Science:
- Biotechnology and Protein Engineering
- Molecular Biology
- Biochemistry
Background:
- Recombinant protein production is vital for research and therapeutics.
- Achieving soluble and correctly folded proteins remains a challenge.
- Various strategies, including host selection and cultivation conditions, are employed.
Purpose of the Study:
- To review and discuss the successful application of folding promoting agents in recombinant protein production.
- To highlight the importance of analyzing and optimizing these strategies for specific target proteins.
- To provide an overview of technologies for deciding on in vivo use of folding promoting agents.
Main Methods:
- Co-expression of chaperones and foldases.
- Optimization of cultivation conditions.
- Application of modern systems approaches and folding/activity screening assays.
- In vitro and in vivo analysis of folding promoting agents.
Main Results:
- Significant increase and success in using folding promoting agents for functional recombinant protein yield.
- In vivo effects of agents are comparable to in vitro actions.
- Data generated can inform experimental planning and knowledge-based modeling.
Conclusions:
- Folding promoting agents are effective tools for improving recombinant protein production.
- Tailored optimization is essential for successful application.
- Systematic analysis aids in the decision-making process for in vivo use.
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