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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...
Drug-Receptor Bonds01:25

Drug-Receptor Bonds

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...
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:
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...

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Related Experiment Video

Updated: Jul 6, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

Ligand binding to nucleic acids and proteins: Does selectivity increase with strength?

Hans-Jörg Schneider1

  • 1FR Organische Chemie, Universität des Saarlandes, D 66041 Saarbrücken, Germany. ch12hs@rz.uni-sb.de

European Journal of Medicinal Chemistry
|April 12, 2008
PubMed
Summary

Ligand binding strength and selectivity to biomacromolecules are linked by thermodynamic principles. Multivalency enhances both affinity and selectivity, though deviations occur due to complex interactions.

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Area of Science:

  • Biochemistry
  • Chemical Thermodynamics
  • Molecular Biology

Background:

  • Understanding ligand-biomacromolecule interactions is crucial for drug design and molecular recognition.
  • The relationship between binding affinity and selectivity is complex and influenced by various molecular factors.

Purpose of the Study:

  • To explore the theoretical basis and practical implications of the relationship between ligand binding affinity and selectivity.
  • To investigate the role of multivalency and site-specific interactions in modulating binding characteristics.

Main Methods:

  • Theoretical analysis based on thermodynamic principles.
  • Illustration with examples from drug-receptor interactions, nucleic acids, and metalloproteins.

Main Results:

  • A linear correlation between selectivity and affinity is theoretically expected, with multivalency playing a key role.
  • Deviations from linearity are often due to complex, site-specific interactions that can dominate affinity.
  • Certain molecules, like etonitazene, demonstrate both high affinity and selectivity, aligning with theoretical predictions.

Conclusions:

  • Thermodynamic principles support a link between ligand binding affinity and selectivity, emphasizing the importance of multivalency.
  • While theoretical models predict linear correlations, real-world systems exhibit complexities due to diverse interaction sites.
  • The study highlights examples of successful ligand design and natural systems that achieve high affinity and selectivity.