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Related Concept Videos

Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Related Experiment Video

Updated: May 26, 2026

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)
09:35

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

A versatile method to measure the binding to basic proteins by surface plasmon resonance.

Shagufta H Khan1, Kriszta Farkas, Raj Kumar

  • 1Department of Basic Sciences, The Commonwealth Medical College, 525 Pine Street, Scranton, PA 18509, USA.

Analytical Biochemistry
|December 31, 2011
PubMed
Summary
This summary is machine-generated.

This study presents a novel Surface Plasmon Resonance (SPR) method for analyzing biomolecular interactions with basic proteins. The technique leverages natural protein charges for stable immobilization, enabling efficient kinetic assays under physiological conditions.

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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

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Last Updated: May 26, 2026

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)
09:35

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
15:27

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Biomolecular interactions are crucial for biological processes like gene transcription and cell signaling.
  • Basic proteins (histones, transcription factors, ribosomal proteins) are key players in these interactions.
  • Surface Plasmon Resonance (SPR) is a standard technique for measuring biomolecular interactions, but ligand immobilization can be challenging.

Purpose of the Study:

  • To develop a novel SPR method for measuring biomolecular interactions involving basic proteins.
  • To establish a method that immobilizes basic proteins without affecting their conformation or biological activity.
  • To enable efficient, fast, and reversible kinetic assays for basic protein interactions.

Main Methods:

  • Utilized the inherent positive charge of basic proteins for immobilization onto a negatively charged C1 chip surface.
  • Employed electrostatic interactions for specific and stable ligand immobilization without chemical modification.
  • Determined optimal regeneration conditions using sodium dodecyl sulfate for repeated binding cycles.

Main Results:

  • Achieved specific and stable immobilization of basic proteins via electrostatic interaction.
  • Demonstrated efficient regeneration of the SPR chip using sodium dodecyl sulfate.
  • Established a method for measuring binding kinetics of basic proteins under physiological conditions.

Conclusions:

  • The novel SPR method provides an efficient, fast, and reversible approach for studying basic protein interactions.
  • This technique is widely applicable to diverse biomolecular binding studies, including protein-protein, protein-DNA, and protein-RNA interactions.
  • The method overcomes limitations of traditional ligand immobilization in SPR assays for basic proteins.