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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...
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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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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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An Allosterically Regulated, Four-State Macrocycle.

Andrea I d'Aquino1, Ho Fung Cheng1, Joaquín Barroso-Flores2

  • 1Department of Chemistry and International Institute for Nanotechnology , Northwestern University , 2145 Sheridan Road , Evanston , Illinois 60208 , United States.

Inorganic Chemistry
|January 6, 2018
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Summary
This summary is machine-generated.

Researchers developed a novel four-state macrocycle using coordination-driven supramolecular chemistry and the weak-link approach. This stimuli-responsive system mimics allosteric enzymes, enabling complex molecular switching for various applications.

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Area of Science:

  • Supramolecular Chemistry
  • Coordination Chemistry
  • Materials Science

Background:

  • Macrocycles are crucial for host-guest chemistry, enabling applications in separations, sensing, and drug delivery.
  • Designing and synthesizing complex macrocycles is challenging, hindering their widespread use.
  • Coordination-driven supramolecular chemistry offers a rapid route to synthesize macrocycles with tunable recognition properties.

Purpose of the Study:

  • To synthesize a novel, allosterically regulated four-state macrocycle using the weak-link approach (WLA).
  • To investigate the dynamic behavior and stimuli-responsive switching of the synthesized macrocycle.
  • To explore the potential of this system as a mimic of allosteric enzymes and for molecular logic systems.

Main Methods:

  • Stepwise assembly of ditopic bidentate hemilabile ligands (N-heterocyclic carbene thioether (NHC,S) and phosphino thioether (P,S)) at Platinum(II) metal nodes.
  • Utilizing the weak-link approach (WLA) for supramolecular coordination chemistry.
  • Characterization of each state using multinuclear Nuclear Magnetic Resonance (NMR) spectroscopy, single-crystal X-ray diffraction, and density functional theory (DFT) computations.

Main Results:

  • Successfully synthesized a new macrocyclic structure capable of existing in four distinct states.
  • Demonstrated that the macrocycle exhibits complex dynamic behavior and can be reversibly toggled between states using small-molecule effectors.
  • Confirmed structural switching with multiple distinct molecular cues, showcasing its responsiveness.

Conclusions:

  • The synthesized four-state macrocycle represents a significant advancement in stimuli-responsive supramolecular chemistry.
  • This system effectively mimics allosteric enzymes, offering tunable recognition and catalytic properties.
  • The ability for multicue switching opens possibilities for advanced chemoswitches, controlling chemical transformations and developing molecular logic systems.