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Related Concept Videos

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...
Targets for Drug Action: Overview01:26

Targets for Drug Action: Overview

Drugs target macromolecules to modify ongoing cellular processes. Primary drug targets include receptors, ion channels, transporters, and enzymes.
Receptors are either membrane-spanning or intracellular proteins, which upon binding a ligand, get activated and transmit the signal downstream to elicit a response. Drugs bind receptors, either mimicking the action of endogenous ligands or blocking the receptor activity to bring about a modified response. Nearly 35% of approved drugs target the G...
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...
ATP and Macromolecule Synthesis01:28

ATP and Macromolecule Synthesis

Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, nitrogen, and other minor elements. There are four major biological macromolecule classes: carbohydrates, lipids, proteins, and nucleic acids.
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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:
Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...

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Related Experiment Video

Updated: Jul 12, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

Ion binding by synthetic macrocyclic compounds.

J J Christensen, J O Hill, R M Izatt

    Science (New York, N.Y.)
    |October 29, 1971
    PubMed
    Summary

    Synthetic macrocycles offer tunable ion binding properties. Researchers can design these molecules for specific cation and anion interactions, opening new avenues in coordination chemistry and solution metal complexation.

    Area of Science:

    • Coordination Chemistry
    • Supramolecular Chemistry

    Background:

    • Synthetic macrocyclic molecules possess unique hydrophilic cavities and hydrophobic exteriors.
    • Recent advances have focused on synthesizing novel macrocyclic compounds, yet practical applications remain largely unexplored.

    Purpose of the Study:

    • To explore the potential of synthetic macrocycles for designing specific cation and anion binding properties.
    • To investigate how structural modifications influence ion selectivity and binding characteristics.

    Main Methods:

    • Systematic variation of macrocycle cavity size to achieve size-selective ion accommodation.
    • Tailoring the number and type of coordinating atoms (e.g., oxygen, sulfur, nitrogen) to control electrostatic and covalent interactions.
    • Modifying hydrophobic exteriors with side chains to enhance solubility of ion complexes in organic solvents.

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    Published on: June 23, 2026

    Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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    Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

    Published on: October 26, 2015

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    Last Updated: Jul 12, 2026

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    Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
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    Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
    10:33

    Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

    Published on: October 26, 2015

    Main Results:

    • Demonstrated ability to synthesize macrocycles with pre-selected ion binding specificities.
    • Established correlations between coordinating atom type and the ionic/covalent character of metal-ligand bonds.
    • Showcased structural mimicry of natural molecules like cyclic polyethers and cyclic polyamines.

    Conclusions:

    • Synthetic macrocycles represent a versatile platform for selective metal complexation in solution.
    • Structural tunability allows for precise control over ion binding, mimicking biological systems and enabling new chemical applications.