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Related Concept Videos

RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
RNA Stability01:53

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Protein Engineering by Yeast Surface Display
05:49

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Evolution of protein stability using ribosome display.

Andrew Buchanan1

  • 1Department of Antibody Discovery and Protein Engineering, MedImmune Limited, Cambridge, UK. buchanana@medimmune.com

Methods in Molecular Biology (Clifton, N.J.)
|November 19, 2011
PubMed
Summary

Enhancing protein stability offers therapeutic benefits like longer shelf-life and reduced aggregation. Ribosome display technology can now be used to select for protein stability, improving drug development.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Biotechnology
  • Pharmaceutical Sciences

Background:

  • Protein stability is crucial for biological therapeutics, impacting half-life, shelf-life, aggregation, and expression.
  • Traditional methods for engineering protein stability include empirical, rational, and directed evolution approaches.
  • Phage display is a common directed evolution technique, but ribosome display offers a powerful alternative.

Purpose of the Study:

  • To extend the application of ribosome display technology beyond high-affinity protein selection.
  • To adapt ribosome display for the selection of proteins with enhanced stability.
  • To define and select for protein stability as the propensity to remain in a folded, active state.

Main Methods:

  • Utilizing ribosome display, an in vitro protein evolution system.
  • Adapting the selection criteria of ribosome display to target protein stability.
  • Defining protein stability as the molecule's ability to maintain its folded and active conformation.

Main Results:

  • Demonstrated the successful application of ribosome display for selecting protein stability.
  • Extended the utility of ribosome display to a new selection parameter beyond affinity.
  • Provided a method for identifying and engineering more stable protein variants.

Conclusions:

  • Ribosome display is a versatile tool that can be effectively employed for selecting enhanced protein stability.
  • This approach broadens the scope of directed evolution using ribosome display for therapeutic protein development.
  • Selecting for stability using ribosome display can lead to improved biological therapeutics with desirable characteristics.