Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

14.3K
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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
14.3K
Ligand Binding Sites02:40

Ligand Binding Sites

8.2K
8.2K
Affinity and Avidity01:41

Affinity and Avidity

37.1K
Overview
37.1K
Quantitative Aspects of Drug-Receptor Interaction01:30

Quantitative Aspects of Drug-Receptor Interaction

1.4K
The receptor occupancy theory connects a drug's response to the number of occupied receptors. With higher drug concentrations, more receptors are occupied, leading to increased responses. The formation of drug-receptor complexes involves association and dissociation rates, which reach equilibrium when the forward and backward reactions are equal. The equilibrium association constant (Ka) and its inverse, the equilibrium dissociation constant (Kd), indicate drug affinity. Higher Ka and lower...
1.4K
Drug-Receptor Interactions01:29

Drug-Receptor Interactions

6.6K
Drug-receptor interaction describes the binding of receptors by drugs, but not all drug-receptor interactions result in activation and tissue response. For instance, the binding of agonists activates the receptor to generate a cellular reaction, while antagonists bind to receptors without causing their activation.
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue....
6.6K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

14.3K
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:
14.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Identification of Chronic Stress-Related Biomarkers for Potential Diagnosis and Treatment of Osteoporosis: An Integrated Multi-omic and Clinical Data Analysis.

Therapeutic innovation & regulatory science·2026
Same author

Modeling Reveals How Direct-Acting Antivirals Redirect HBV Capsid Assembly Pathways to Noninfectious Products.

bioRxiv : the preprint server for biology·2026
Same author

From shadows to light: navigating the rare complication of cerebral air embolism from a case report.

Frontiers in medicine·2026
Same author

Dual-symmetry-guided assembly of complex lattices.

Nature·2026
Same author

A DNA-encoded recipe to direct multistage colloidal assembly.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Impact of solvent forces and broken symmetry on the assembly of designed proteins at a liquid-solid interface.

Nature communications·2026
Same journal

5-Year advances in semisacrificial metal foam-derived materials for energy storage and electrocatalysis.

Nanoscale·2026
Same journal

Application of nanogenerators in oral and respiratory systems: a review.

Nanoscale·2026
Same journal

High-efficiency BCN quantum dots with enhanced carrier kinetics enabled by synergistic control of the atomic ratio and interface engineering.

Nanoscale·2026
Same journal

Fluorescence imaging for liver diseases: probe design strategies and diagnostic applications.

Nanoscale·2026
Same journal

Robust and well-structured graphene oxide membranes crosslinked by phenylboronic acid for efficient heavy metal ion sieving.

Nanoscale·2026
Same journal

Lasing characteristics and stress-tuning effects in GaN beam microcavities.

Nanoscale·2026
See all related articles

Related Experiment Video

Updated: Oct 29, 2025

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

21.8K

Avidity and surface mobility in multivalent ligand-receptor binding.

Simon Merminod1, John R Edison, Huang Fang

  • 1Martin A. Fisher School of Physics, Brandeis University, Waltham, MA 02453, USA. wrogers@brandeis.edu.

Nanoscale
|July 14, 2021
PubMed
Summary
This summary is machine-generated.

Membrane fluidity and receptor mobility are crucial for targeted drug delivery. These factors significantly influence particle binding (avidity) and movement on cell surfaces, validating theoretical models.

More Related Videos

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
13:22

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

Published on: November 2, 2011

15.1K
Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

7.4K

Related Experiment Videos

Last Updated: Oct 29, 2025

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

21.8K
Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
13:22

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

Published on: November 2, 2011

15.1K
Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

7.4K

Area of Science:

  • Biophysics
  • Materials Science
  • Nanotechnology

Background:

  • Targeted drug delivery requires particles to bind to cell receptors and cross membranes.
  • Controlling the thermodynamics and dynamics of these processes is challenging.
  • Multivalent ligand-receptor interactions are key to particle-membrane binding.

Purpose of the Study:

  • To characterize and model multivalent ligand-receptor binding between colloidal particles and lipid bilayers.
  • To understand the surface mobility of membrane-bound particles.
  • To investigate the influence of membrane receptor mobility on binding thermodynamics and dynamics.

Main Methods:

  • Combined experimental systems with statistical mechanical modeling.
  • Characterized multivalent ligand-receptor binding kinetics and thermodynamics.
  • Modeled particle-membrane interactions and surface mobility.

Main Results:

  • Membrane receptor mobility is critical for binding thermodynamics and dynamics.
  • Particle-membrane binding free energy (avidity) shows nonlinear dependence on ligand-receptor affinity due to multivalency and receptor recruitment.
  • Partial membrane wrapping of particles further enhances avidity.
  • Lateral diffusion of bound particles is dominated by hydrodynamic drag from recruited receptors.
  • The fluidity and elasticity of the membrane are as important as ligand-receptor affinity.

Conclusions:

  • Provides direct validation for theoretical frameworks of multivalent interactions.
  • Highlights the significant role of membrane fluidity and receptor dynamics in targeted particle delivery.
  • Suggests that optimizing membrane properties alongside ligand-receptor interactions is essential for effective drug delivery systems.