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Area of Science:

  • Biochemistry
  • Toxicology
  • Structural Biology

Background:

  • Per- and polyfluoroalkyl substances (PFAS) are persistent, toxic environmental contaminants due to strong carbon-fluorine bonds.
  • Beta-lactoglobulin (β-LG), a milk protein, is known to transport hydrophobic and amphiphilic molecules crucial for physiological functions.
  • Understanding β-LG's interaction with PFAS is significant due to the protein's transport role and PFAS toxicity.

Purpose of the Study:

  • To investigate the binding mechanism of PFAS with the milk protein β-lactoglobulin.
  • To elucidate the structural basis of PFAS-β-LG complex formation.
  • To assess the stability and energetics of PFAS binding within β-LG.

Main Methods:

  • X-ray crystallography was used to determine the structures of β-lactoglobulin complexed with PFOA, PFOS, and PFDA.
  • Bioinformatics analysis was performed on the crystal structures to identify key interactions.
  • Molecular dynamics (MD) simulations were employed to assess binding stability and calculate binding energies.

Main Results:

  • Crystal structures reveal high-affinity binding of PFOA, PFOS, and PFDA to the central calyx of β-lactoglobulin, the canonical binding site for retinol and fatty acids.
  • Hydrophobic interactions stabilize the binding of PFAS hydrophobic tails, while polar interactions involve Lys60, Lys69, and the PFAS polar head groups.
  • MD simulations confirm high binding stability, with PFDA exhibiting the strongest binding energy (-25 kcal/mol) due to favorable van der Waals interactions with its longer hydrophobic chain.

Conclusions:

  • Beta-lactoglobulin binds PFAS with high affinity in its hydrophobic calyx, utilizing similar mechanisms as for fatty acid and retinol transport.
  • The protein's structure undergoes conformational changes, including an open EF loop, upon PFAS complexation.
  • This study proposes a mechanism for β-lactoglobulin acting as a transporter for PFAS, potentially mediating their neurotoxic effects.