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Related Experiment Video

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A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits
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Selection of Affibody Molecules Using Phage Display.

Linnea Charlotta Hjelm1, Charles Dahlsson Leitao1, Stefan Ståhl1

  • 1Department of Protein Science, KTH Royal Institute of Technology, 106 91 Stockholm, Sweden.

Cold Spring Harbor Protocols
|July 25, 2023
PubMed
Summary

This study details a protocol for amplifying affibody libraries and using phage display for biopanning. It enables the selection of novel affibody molecules with nanomolar affinities for specific targets.

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Protein Engineering

Background:

  • Affibody molecules are small, engineered proteins with high affinity for specific targets.
  • Directed evolution is a key method for generating these affinity proteins.
  • The selection and amplification of affibody libraries are crucial steps in their development.

Purpose of the Study:

  • To describe a detailed protocol for affibody library amplification.
  • To outline a biopanning method using phage display for affibody selection.
  • To enable the isolation of high-affinity affibody molecules.

Main Methods:

  • Generation and amplification of naive and affinity maturation affibody libraries.
  • Biopanning using phage display technology.
  • Analysis of selection output to identify affibody hits.

Main Results:

  • The protocol successfully yields first-generation affibody molecules.
  • Affibody hits with affinities in the low nanomolar range were obtained from naive libraries.
  • The method is adaptable for affinity maturation to isolate higher-affinity variants.

Conclusions:

  • This protocol provides a robust method for affibody molecule selection.
  • Phage display biopanning is effective for identifying novel affibody binders.
  • The described workflow facilitates the development of affibody-based research and therapeutic tools.