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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:
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: Jun 5, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

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Published on: January 7, 2017

Methods for measuring aptamer-protein equilibria: a review.

Meng Jing1, Michael T Bowser

  • 1University of Minnesota, Department of Chemistry, 207 Pleasant St. SE, Minneapolis, MN 55455-0431, USA.

Analytica Chimica Acta
|January 18, 2011
PubMed
Summary
This summary is machine-generated.

Aptamers, which rival antibodies, require precise binding analysis. This review details various methods for assessing aptamer-protein interactions, crucial for research and clinical uses.

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Last Updated: Jun 5, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Analytical Chemistry

Background:

  • Aptamers are single-stranded DNA or RNA molecules selected for high-affinity binding to targets.
  • Understanding aptamer-protein binding is essential for their research and clinical applications.
  • Aptamers offer an alternative to antibodies in many biological applications.

Purpose of the Study:

  • To review and compare methods for assessing aptamer-protein binding.
  • To provide a comprehensive overview of available techniques for aptamer characterization.
  • To guide researchers in selecting appropriate methods for aptamer-target interaction studies.

Main Methods:

  • Separation-based techniques: Dialysis, ultrafiltration, electrophoresis (gel and capillary), and HPLC.
  • Mixture-based techniques: Fluorescence intensity and anisotropy, UV-Vis absorption, circular dichroism, surface plasmon resonance, and isothermal titration calorimetry.
  • Comparison of methods based on principle, application range, sample consumption, time, and complexity.

Main Results:

  • Summarizes various methods for aptamer-protein binding assessment.
  • Compares the strengths and weaknesses of different techniques.
  • Provides a comparative overview of key features for each method.

Conclusions:

  • A thorough understanding of aptamer-target binding is necessary for aptamer utility.
  • A variety of methods exist, each with specific advantages and limitations.
  • This review aids in selecting optimal techniques for aptamer-protein interaction analysis.