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

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...
Ligand Binding Sites02:40

Ligand Binding Sites

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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
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:
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

You might also read

Related Articles

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

Sort by
Same author

Optimized Sample Handling Minimizes Peptide Adsorption to Plastics to Enable High Sensitivity Evosep Based Chemical Proteomics.

Proteomics·2026
Same author

Towards supramolecular regenerative medicine using low-molecular-weight gelator hydrogels for stem cell growth.

Biomaterials science·2026
Same author

Biomechanics of the plesiomorphic forelimb of the basal therizinosaur Falcarius.

Anatomical record (Hoboken, N.J. : 2007)·2026
Same author

When Reality Defies Prediction: Polymorphism, Twinning, and Accordion Crystals.

Journal of the American Chemical Society·2026
Same author

Genomic features associated with sustained mammalian transmission of avian influenza A viruses.

Nature microbiology·2026
Same author

Molecular-Scale Tuning of Low-Molecular-Weight Gelators Controls Supramolecular Assembly and Directs Human Mesenchymal Stem Cell Growth.

Angewandte Chemie (International ed. in English)·2026
Same journal

A Domino-Synthesized Dicoordinate Copper(I) Bis-imidazopyridine Complex Triggering Cuproptosis/Ferroptosis for Enhanced Cancer Immunotherapy.

Angewandte Chemie (International ed. in English)·2026
Same journal

Mirror-Symmetric Organic Two-Dimensional Crystals for Alternative Photon Transport Pathways.

Angewandte Chemie (International ed. in English)·2026
Same journal

Cobalt-Catalyzed Migratory E-Selective Asymmetric Aza-Nozaki-Hiyama-Kishi Coupling.

Angewandte Chemie (International ed. in English)·2026
Same journal

Facile Synthesis of α,ω-Dihydroxy Telechelic Macromonomers From Ethylene and α-Olefins for Recyclable Alternating Block Copolymers.

Angewandte Chemie (International ed. in English)·2026
Same journal

Multi-Atom Sub-Nanometer Assemblies on Interpenetrating Multi-Chambered N/C Nanospheres.

Angewandte Chemie (International ed. in English)·2026
Same journal

A Synergistic C<sub>2+</sub> Alcohols/Olefins-Intermediated Pathway Boosts CO<sub>2</sub> Hydrogenation to Aromatics.

Angewandte Chemie (International ed. in English)·2026
See all related articles

Related Experiment Video

Updated: May 21, 2026

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

Self-assembled multivalency: dynamic ligand arrays for high-affinity binding.

Anna Barnard1, David K Smith

  • 1Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.

Angewandte Chemie (International Ed. in English)
|June 13, 2012
PubMed
Summary
This summary is machine-generated.

Self-assembled multivalency uses biological self-assembly to create high-affinity molecular interactions. This approach offers advantages for designing synthetic nanosystems for nanomedicine applications.

More Related Videos

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

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

Related Experiment Videos

Last Updated: May 21, 2026

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

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

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

Area of Science:

  • Biochemistry
  • Nanotechnology
  • Materials Science

Background:

  • Multivalency enhances molecular recognition and binding affinity in biological systems.
  • Traditional methods involve covalent synthesis of scaffolds to organize ligands.
  • Emerging strategies explore self-assembly for organizing multivalent ligands.

Purpose of the Study:

  • To highlight the significance of self-assembled multivalency as a design strategy.
  • To explore the advantages of self-assembly over covalent synthesis for multivalent systems.
  • To discuss the potential applications of self-assembled multivalency in nanomedicine.

Main Methods:

  • Review of self-assembly principles in organizing multivalent ligands.
  • Analysis of advantages including ease of synthesis, tunability, and responsiveness.
  • Conceptualization of self-assembled nanostructures for biological intervention.

Main Results:

  • Self-assembly offers a flexible and tunable approach to creating multivalent systems.
  • Advantages include simplified synthesis, control over nanostructure morphology, and ligand presentation.
  • The responsive nature of self-assembly allows for dynamic control of molecular interactions.

Conclusions:

  • Self-assembled multivalency is a fundamental strategy for designing synthetic nanosystems.
  • This approach facilitates high-affinity molecular recognition for biological intervention.
  • Significant potential exists for applications in nanomedicine and beyond.