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

Drug-Receptor Bonds01:25

Drug-Receptor Bonds

4.0K
Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
4.0K
Van der Waals Interactions01:24

Van der Waals Interactions

69.4K
Atoms and molecules interact with each other through intermolecular forces. These electrostatic forces arise from attractive or repulsive interactions between particles with permanent, partial, or temporary charges. The intermolecular forces between neutral atoms and molecules are ion–dipole, dipole–dipole, and dispersion forces, collectively known as van der Waals forces.
69.4K
Ligand Binding Sites02:40

Ligand Binding Sites

14.7K
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...
14.7K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

14.6K
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:
14.6K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

9.7K
9.7K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

62.3K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
62.3K

You might also read

Related Articles

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

Sort by
Same author

Single-molecule readout of reversible nanoswitches enables continuous monitoring of low biomarker concentrations.

Nature communications·2026
Same author

Continuous Sensing of Lactate Dehydrogenase with a Competitive Particle-Based Sensor for Monitoring Cell Death.

ACS sensors·2026
Same author

Simulation-guided exploration of PAINT parameter space for accurate molecular quantification.

Nanoscale·2025
Same author

Reversible Sandwich-Based Particle Nanoswitch for Continuous Protein Monitoring at Picomolar Concentrations with Automated Calibration.

Angewandte Chemie (International ed. in English)·2025
Same author

Spatial Molecular Heterogeneity on Biofunctionalized Particles Quantified by Three-Dimensional Single-Molecule DNA-PAINT.

Langmuir : the ACS journal of surfaces and colloids·2025
Same author

Understanding Fast and Slow Signal Changes in a Competitive Particle-Based Continuous Biosensor.

Analytical chemistry·2025
Same journal

Tau protein as a regulator of mitochondrial function and dynamics.

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

A scalable, dividing cell model for the robust propagation and quantification of human sporadic Creutzfeldt-Jakob disease prions.

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

Epigenetic regulation of mesenchymal BMP signaling directs postnatal organ innervation.

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

Single-shot wide-field biochemical imaging at 1 kHz frame rate.

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

Morphogenesis and topological evolution of a frustrated nematic liquid crystal under confinement.

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

B cell-intrinsic CXCR3 drives efficient generation of ectopic pulmonary germinal center responses to influenza A virus infection.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Related Experiment Video

Updated: Dec 10, 2025

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.1K

Multivalent weak interactions enhance selectivity of interparticle binding.

M R W Scheepers1,2, L J van IJzendoorn1,2, M W J Prins3,2,4

  • 1Department of Applied Physics, Eindhoven University of Technology, 5600 MB Eindhoven, The Netherlands.

Proceedings of the National Academy of Sciences of the United States of America
|August 30, 2020
PubMed
Summary
This summary is machine-generated.

Multivalent weak interactions enhance binding selectivity for targeted drug delivery. Shorter DNA interactions between particles and cells improve selectivity, as confirmed by experiments and simulations.

Keywords:
multivalencyparticlesselectivity

More Related Videos

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

12.5K
Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

377

Related Experiment Videos

Last Updated: Dec 10, 2025

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.1K
Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST

Published on: November 2, 2018

12.5K
Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

377

Area of Science:

  • Colloidal science
  • Biophysics
  • Nanotechnology

Background:

  • Targeted drug delivery relies on selective binding of colloidal particles to cells.
  • Theoretical models indicate multivalency and weak interactions are key for high selectivity.
  • Ligand-receptor interactions are crucial for particle-cell binding specificity.

Purpose of the Study:

  • To investigate the role of multivalent weak interactions in enhancing binding selectivity.
  • To model ligand-receptor interactions using DNA-coated particles.
  • To experimentally validate theoretical predictions on selectivity.

Main Methods:

  • Optomagnetic cluster experiments were used to measure particle aggregation rates.
  • Particle aggregation was studied as a function of ligand and receptor densities.
  • Computational simulations were performed to confirm experimental findings.

Main Results:

  • Binding selectivity increased with shorter DNA ligand-receptor pairs.
  • Multivalent weak interactions were shown to enhance interparticle binding selectivity.
  • Simulations highlighted the importance of ligand-receptor dissociation in selectivity.

Conclusions:

  • Experimental and simulation results confirm that multivalent weak interactions improve binding selectivity.
  • The findings provide a foundation for designing more effective targeted drug delivery systems.
  • Understanding ligand-receptor dissociation is critical for optimizing colloidal particle selectivity.