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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Spare Receptors01:30

Spare Receptors

Some receptors remain unoccupied even when an agonist produces a maximal response. Such empty ones are called spare receptors. In presence of spare receptors the maximum effect of an agonist drug is achieved with fewer than 100% of the receptors being occupied. To determine the presence of spare receptors, scientists often compare the concentration of the drug needed to produce 50% of the maximum effect (EC50) with the concentration of the drug needed to occupy 50% of the receptors (Kd). If the...
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...
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...
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...

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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

Artificial allosteric receptors.

Christopher Kremer1, Arne Lützen

  • 1Universität Bonn, Kekulé-Institut für Organische Chemie und Biochemie, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|March 7, 2013
PubMed
Summary
This summary is machine-generated.

Allosteric effects, where one molecule binding influences another, are crucial in biology. This review explores artificial systems mimicking these effects for molecular control in supramolecular chemistry.

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Area of Science:

  • Supramolecular Chemistry
  • Chemical Biology

Background:

  • Allosteric effects describe cooperative binding influenced by conformational changes, a key regulatory mechanism in biological systems.
  • This biological principle inspires the design of artificial systems in supramolecular chemistry.

Purpose of the Study:

  • To provide an updated overview of artificial systems designed to mimic allosteric effects.
  • To cover various approaches and effector types used in supramolecular chemistry.

Main Methods:

  • Review of literature on artificial allosteric systems since the late 1970s/early 1980s.
  • Categorization of systems based on effector type (cationic, anionic, neutral) and combinations.
  • Inclusion of both homotropic and heterotropic allosteric examples.

Main Results:

  • Numerous artificial systems have been developed to replicate biological allosteric regulation.
  • These systems demonstrate control over molecular recognition, signal amplification, reactivity, and catalysis.
  • A comprehensive classification of existing approaches based on effector properties is presented.

Conclusions:

  • Allosteric principles from biology are successfully translated into artificial supramolecular systems.
  • These artificial systems offer novel avenues for precise functional control in chemistry.
  • The review highlights the diversity and evolution of allosteric systems in supramolecular chemistry.