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Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations.

Albert Solé-Daura1, Vincent Goovaerts2, Karen Stroobants2

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Chemistry (Weinheim an Der Bergstrasse, Germany)
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Summary

The cerium-substituted Keggin anion (CeK) shows strong interactions with hen egg-white lysozyme (HEWL). Its size, shape, and lower hydrophilicity enhance binding compared to other polyoxometalates.

Keywords:
DFT calculationsmolecular dynamicspeptide hydrolysispolyoxometalatesproteins

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Area of Science:

  • Inorganic Chemistry
  • Biochemistry
  • Computational Chemistry

Background:

  • Polyoxometalates (POMs) are versatile inorganic clusters with potential applications in biomaterials.
  • Understanding POM-protein interactions is crucial for designing novel functional materials.

Purpose of the Study:

  • To investigate the molecular interactions between a cerium-substituted Keggin anion (CeK) and hen egg-white lysozyme (HEWL).
  • To compare CeK with other POMs (CeK2, ZrL) to elucidate the influence of POM features on protein interactions.

Main Methods:

  • Molecular dynamics (MD) simulations were employed to model POM-protein interactions.
  • Analysis focused on electrostatic attraction and hydrogen bonding between POMs and protein residues.

Main Results:

  • The CeK anion strongly interacts with specific cationic sites (Arg21, Arg45, Arg68) on HEWL.
  • POMs primarily bind to positively charged and polar uncharged amino acid residues.
  • CeK exhibits higher protein affinity than CeK2 and ZrL due to optimal size, shape, and hydrophilicity.

Conclusions:

  • POM features like size, charge, and hydrophilicity significantly dictate POM-protein binding affinity.
  • CeK's characteristics make it a promising candidate for interacting with lysozyme and potentially other proteins.