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Related Concept Videos

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Internal Receptors01:31

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Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
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The Equilibrium Binding Constant and Binding Strength02:18

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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: Feb 3, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
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Ligand-Receptor Binding on Cell Membrane: Dynamic Force Spectroscopy Applications.

Jianli Liu1, Wenhui Li1,2, Xuejie Zhang1

  • 1Key Laboratory of Molecular Nanostructures and Nanotechnology, Institute of Chemistry, Chinese Academy of Sciences, Beijing, China.

Methods in Molecular Biology (Clifton, N.J.)
|October 31, 2018
PubMed
Summary

This study uses atomic force microscopy to analyze cell surface receptor binding. It investigates how epidermal growth factor (EGF) binds to its receptor (EGFR) and the impact of Pertuzumab and Trastuzumab drugs on this interaction.

Keywords:
AFM force spectroscopyAtomic force microscopy (AFM)Dynamic force spectroscopy (DFS)Ligand-receptor interaction

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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
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Area of Science:

  • Cellular biology
  • Biophysics
  • Pharmacology

Background:

  • Cell membrane ligand-receptor interactions are crucial for intercellular communication.
  • Atomic force microscopy (AFM) offers a powerful method for studying these interactions in a near-physiological state.
  • Understanding these interactions is vital for disease research and drug development.

Purpose of the Study:

  • To demonstrate the application of single-molecule dynamic force spectroscopy in studying ligand-receptor binding.
  • To investigate the binding dynamics between epidermal growth factor (EGF) and its receptor (EGFR).
  • To assess the influence of Pertuzumab and Trastuzumab on the EGF-EGFR interaction.

Main Methods:

  • Single-molecule dynamic force spectroscopy utilizing Atomic Force Microscopy (AFM).
  • Direct measurement of binding forces and kinetics between EGF and EGFR.
  • Analysis of drug effects on the molecular binding events.

Main Results:

  • Successfully applied AFM-based single-molecule force spectroscopy to quantify EGF-EGFR binding.
  • Characterized the binding forces and dissociation rates of the EGF-EGFR complex.
  • Observed and quantified the modulatory effects of Pertuzumab and Trastuzumab on EGF-EGFR binding.

Conclusions:

  • AFM single-molecule force spectroscopy is a valuable tool for dissecting ligand-receptor dynamics.
  • The study provides insights into the molecular mechanisms underlying EGF-EGFR interactions.
  • Pertuzumab and Trastuzumab demonstrate specific effects on the EGF-EGFR pathway, relevant for therapeutic strategies.