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Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
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Characterization of antibody-antigen interactions using biolayer interferometry.

Tal Noy-Porat1, Ron Alcalay1, Adva Mechaly1

  • 1Israel Institute for Biological Research, Ness-Ziona 7410001, Israel.

STAR Protocols
|September 27, 2021
PubMed
Summary

This protocol details using biolayer interferometry for antibody-antigen binding analysis. It enables rapid, real-time measurement of protein interactions without labeling molecules.

Keywords:
AntibodyImmunologyProtein Biochemistry

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Area of Science:

  • Biochemistry
  • Immunology
  • Biophysics

Background:

  • Assessing molecular interactions is crucial in drug discovery and diagnostics.
  • Label-free detection methods accelerate the study of biological interactions.
  • Biolayer interferometry (BLI) offers a robust platform for real-time interaction analysis.

Purpose of the Study:

  • To describe a protocol for utilizing biolayer interferometry.
  • To focus on affinity determination and epitope binning of antibody-antigen interactions.
  • To highlight the platform's utility for diverse protein-protein interaction studies.

Main Methods:

  • Utilizing a biolayer interferometry platform for real-time data collection.
  • Employing unlabeled molecules for interaction analysis.
  • Implementing careful experimental design, including sensor selection and controls.

Main Results:

  • Real-time readings enable fast and easy data acquisition.
  • The protocol facilitates accurate affinity determination.
  • Epitope binning experiments can be efficiently performed.

Conclusions:

  • Biolayer interferometry provides a rapid and accessible method for studying protein-protein interactions.
  • The described protocol allows for precise characterization of antibody-antigen binding kinetics.
  • Careful experimental planning is essential for successful application of the BLI technique.