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Related Experiment Video

Updated: Sep 9, 2025

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

In-Solution Characterization of Biomolecular Interaction Kinetics under Native Conditions.

Philipp Willmer^1,2, Emil G P Stender¹, Kritika Sahni Ray¹

¹FIDA Biosystems ApS, Soborg 2860, Denmark.

Analytical Chemistry

|August 29, 2025

Summary

This summary is machine-generated.

A new flow-induced dispersion analysis method, C-Jump, measures biomolecular interaction kinetics in solution without surface immobilization. This technique accurately determines binding rates for protein-protein and protein-small molecule interactions under native conditions.

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Area of Science:

Biochemistry
Biophysics
Chemical Kinetics

Background:

Accurate characterization of biomolecular interaction kinetics is crucial for drug discovery, protein engineering, and understanding biological mechanisms.
Current surface-based methods for studying kinetics require sample immobilization, which can alter molecular behavior and limit applicability under native conditions.
There is a need for methods that can measure interaction kinetics in solution, preserving native molecular states and mobility.

Purpose of the Study:

To introduce a novel method, flow-induced dispersion analysis (C-Jump), for studying biomolecular interaction kinetics in solution.
To eliminate the need for surface immobilization, thereby preserving molecular mobility and avoiding structural constraints.
To demonstrate the method's capability in accurately determining association and dissociation rates for various biomolecular interactions.

Main Methods:

Utilizing flow-induced dispersion analysis with a rapid concentration change technique (C-Jump) in a microfluidic environment.
Examining reactions outside equilibrium conditions by inducing a concentration jump in one binding partner.
Operating without buffer restrictions and requiring minimal sample quantities.

Main Results:

Accurately determined association and dissociation rates for protein-protein and protein-small molecule interactions.
Demonstrated robustness by measuring interaction kinetics in human serum and in-solution, label-free.
Validated C-Jump's broad applicability for studying biomolecular interactions under native conditions.

Conclusions:

C-Jump offers a paradigm shift in studying biomolecular interaction kinetics by keeping molecules in solution.
The method provides a powerful tool for advancing protein engineering and drug discovery.
C-Jump enables the characterization of previously inaccessible biomolecular interactions under native conditions.