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Refolding of recombinant proteins

Clark1

  • 1Department of Chemical Engineering Tufts University Medford, MA 02155, USA edeberna@tufts.edu

Current Opinion in Biotechnology
|July 17, 1998
PubMed
Summary

Recombinant protein production using bacterial inclusion bodies is efficient if refolding succeeds. New additives and chaperone-mimicking processes combat aggregation, improving protein refolding yields.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Bacterial expression systems are widely used for recombinant protein production.
  • Inclusion bodies facilitate high-yield production but require successful in vitro refolding.
  • Protein aggregation during refolding significantly reduces product yield.

Purpose of the Study:

  • To review recent advancements in understanding protein aggregation during in vitro refolding.
  • To highlight novel additives and strategies for preventing aggregation.
  • To explore the application of chaperone-inspired methods for improved refolding.

Main Methods:

  • Literature review of recent developments in protein refolding.
  • Analysis of aggregation mechanisms in vitro.
  • Evaluation of new additives and in vitro chaperone-mimicking processes.

Main Results:

  • Understanding of in vitro protein aggregation mechanisms has advanced.
  • Several new additives have been identified to mitigate aggregation.
  • Strategies mimicking in vivo chaperone activity show promise for enhancing refolding yields.

Conclusions:

  • Successful refolding of bacterial inclusion body proteins is crucial for efficient production.
  • Combating protein aggregation is key to improving refolding yields.
  • Emerging additives and chaperone-mimicking techniques offer promising solutions for recombinant protein production.

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