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Note: Model identification and analysis of bivalent analyte surface plasmon resonance data.
Purushottam Babu Tiwari1, Aykut Üren1, Jin He2
1Department of Oncology, Georgetown University, Washington, District of Columbia 20057, USA.
The Review of Scientific Instruments
|November 2, 2015
Summary
This study introduces a unique signature to identify the bivalent analyte model in surface plasmon resonance (SPR) experiments. This method accurately distinguishes the bivalent binding mechanism from other biphasic models using SPR sensorgrams.
Area of Science:
- Biophysics
- Biochemistry
- Analytical Chemistry
Background:
- Surface plasmon resonance (SPR) is a label-free technique for studying biomolecular interactions.
- Accurate kinetic analysis requires precise identification of binding models.
- The bivalent analyte model, involving complex differential equations, lacks a clear identification procedure.
Purpose of the Study:
- To propose a unique signature for the bivalent analyte model in SPR.
- To develop a method for distinguishing the bivalent analyte model from other biphasic models.
- To validate the proposed signature using experimental SPR data.
Main Methods:
- Development of a novel signature specific to the bivalent analyte binding model.
- Application of the signature to differentiate between various biphasic binding models.
- Experimental validation using sensorgrams obtained from SPR measurements.
Main Results:
- A distinct signature capable of identifying the bivalent analyte model was successfully proposed.
- The signature effectively differentiated the bivalent analyte model from other biphasic models.
- Experimental SPR sensorgrams confirmed the utility of the proposed signature.
Conclusions:
- The proposed signature provides a clear procedure for identifying the bivalent analyte model in SPR.
- This advancement facilitates more accurate kinetic analysis of biomolecular interactions.
- The method enhances the reliability of SPR data interpretation for complex binding events.

