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Crown ethers are cyclic polyethers that contain multiple oxygen atoms, usually arranged in a regular pattern. The first crown ether was synthesized by Charles Pederson while working at DuPont in 1967. For this work, Pedersen was co-awarded the 1987 Nobel Prize in Chemistry. Crown ethers are named using the formula x-crown-y, where x is the total number of atoms in the ring and y is the number of ether oxygen atoms. The term 'crown' refers to the crown-like shape that these ether molecules take.
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Crowning proteins: modulating the protein surface properties using crown ethers.

Cheng-Chung Lee1, Manuel Maestre-Reyna, Kai-Cheng Hsu

  • 1Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 11529 (Taiwan); Core Facilities for Protein Structural Analysis, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 11529 (Taiwan).

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|October 8, 2014
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Crown ethers, cyclic polyethers, can alter protein surfaces by stabilizing interactions. This suggests their use in controlling protein behaviors like oligomerization and crystallization.

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crown compoundscrystal growthmolecular dynamicsprotein engineeringprotein surfaces

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Structural Biology

Background:

  • Crown ethers are cyclic polyethers utilized in phase-transfer catalysis and protein chemistry.
  • They exhibit cation-binding properties, interacting with metallic, organic cations, and charged amino acid residues.
  • Understanding crown ether interactions with proteins is crucial for novel applications.

Purpose of the Study:

  • To investigate the structural and functional effects of crown ethers on protein surfaces.
  • To explore the potential of crown ethers in modulating protein behavior and properties.
  • To compare protein-crown ether complexes with apoproteins and polyethylene glycol complexes.

Main Methods:

  • Co-crystallization of proteins with 18-crown-6.
  • X-ray crystallography to determine complex structures.
  • Biophysical assays and molecular dynamics simulations for comparative analysis.

Main Results:

  • Elucidation of crystal structures for several protein-crown ether co-crystals.
  • Demonstration that crown ethers significantly modify protein surface interactions.
  • Identification of stabilization of intra- and intermolecular interactions by crown ethers.

Conclusions:

  • Crown ethers can dramatically alter protein surface behavior.
  • Proposed application of crown ethers to modulate protein oligomerization, domain interactions, and stability.
  • Crown ethers show potential for enhancing protein crystallization and stabilization in organic solvents.