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Related Experiment Video

Updated: Jan 28, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Flow-Induced Dispersion Analysis (FIDA) for Protein Quantification and Characterization.

Morten E Pedersen1, Jesper Østergaard1,2, Henrik Jensen3,4

  • 1FIDA-Tech Aps, C/O University of Copenhagen, Copenhagen, Denmark.

Methods in Molecular Biology (Clifton, N.J.)
|March 9, 2019
PubMed
Summary

Flow-Induced Dispersion Analysis (FIDA) quantifies proteins in solution by measuring ligand size changes upon binding. This method offers straightforward assay development and reliable quantification in complex samples like plasma.

Keywords:
Auto-antibody detectionBinding analysisDissociation constantFIDAFlow-induced dispersion analysisLigand-binding assayMolecular interactionsPlasmaProtein-protein interactionSerumTaylor dispersion analysis

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Protein Analysis

Background:

  • Characterizing protein interactions is crucial for understanding biological processes.
  • Existing ligand-binding assays like ELISA, SPR, and BLI have limitations, including complex assay development and surface chemistry issues.
  • There is a need for robust, in-solution methods for protein quantification and characterization.

Purpose of the Study:

  • To introduce and describe Flow-Induced Dispersion Analysis (FIDA) as a novel method for protein characterization and quantification.
  • To highlight the advantages of FIDA over existing techniques, particularly its in-solution nature and straightforward assay development.
  • To demonstrate the utility of FIDA for determining binding affinities (Kd) and analyte concentrations.

Main Methods:

  • FIDA utilizes Taylor dispersion analysis (TDA) in fused silica capillaries to measure the apparent hydrodynamic radius of a ligand.
  • The change in ligand size is monitored as it binds to a target protein in solution.
  • Titration experiments are performed to determine the dissociation constant (Kd) and quantify analyte concentration based on size measurements.

Main Results:

  • FIDA accurately measures the apparent molecular size of ligands, which increases upon binding to target analytes.
  • The method allows for straightforward determination of Kd values from titration experiments.
  • Absolute size measurements provide built-in quality control for the assay.
  • FIDA minimizes issues related to non-specific adsorption, enabling direct measurements in complex biological matrices such as plasma and serum.

Conclusions:

  • FIDA is a powerful ligand-binding assay for characterizing and quantifying proteins under native, in-solution conditions.
  • Its straightforward assay development, built-in quality control, and minimized non-specific binding make it advantageous over traditional methods.
  • FIDA offers a reliable approach for protein analysis in various biological samples, including serum and plasma.