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Reliable Strategy for Analysis of Complex Biosensor Data.

Patrik Forssén1, Evgen Multia2, Jörgen Samuelsson1

  • 1Department of Engineering and Chemical Sciences , Karlstad University , SE-651 88 Karlstad , Sweden.

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|March 29, 2018
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Summary
This summary is machine-generated.

This study introduces a novel four-step strategy for analyzing biosensor kinetic binding data, improving the accuracy of complex formation analysis, especially for slow dissociation kinetics and handling system drift.

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Area of Science:

  • Biomolecular Interaction Analysis
  • Biosensor Technology
  • Quantitative Kinetics

Background:

  • Biosensors analyze biomolecular interactions using sensorgrams, but steady-state complex formation is often not reached.
  • Standard global fitting procedures can be unreliable for complex kinetic binding data, especially with antibody interactions.

Purpose of the Study:

  • To present and validate a new four-step strategy for reliable processing of complex kinetic binding data from biosensors.
  • To compare the new strategy against standard global fitting for accuracy and robustness.

Main Methods:

  • A four-step strategy involving dissociation graph calculation, a numerical algorithm (AIDA) for reaction identification, individual sensorgram fitting, and rate constant clustering.
  • Evaluation using synthetic and experimental data from QCM biosensor systems with varying kinetics (fast, moderate, slow).

Main Results:

  • The new strategy reliably estimates the number of complex formations, particularly for complex and slow dissociation kinetics.
  • The strategy demonstrates robustness in handling system drift and deteriorating biosensor chip data.
  • Improved accuracy in estimating complex formation rate constants compared to standard global fitting.

Conclusions:

  • The proposed four-step strategy offers a more reliable and robust method for analyzing complex biosensor kinetic binding data.
  • This approach enhances the understanding of biomolecular interactions, especially when steady-state is not achieved.