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Binding of Per- and Polyfluoroalkyl Substances to β-Lactoglobulin from Bovine Milk. | LitMetric

AI Article Synopsis

  • PFAS are persistent environmental pollutants found in dairy products, but their accumulation mechanisms are not fully understood.
  • Research involved using mass spectrometry and simulations to examine how PFAS interact with bovine whey protein β-lactoglobulin (β-LG), revealing that several PFAS bind to this protein.
  • The study indicates that β-cyclodextrin can help reduce PFAS binding to β-LG, which could lead to strategies for minimizing PFAS levels in dairy and other biological systems.

Article Abstract

Per- and polyfluoroalkyl substances (PFAS) are known for their high environmental persistence and potential toxicity. The presence of PFAS has been reported in many dairy products. However, the mechanisms underlying the accumulation of PFAS in these products remain unclear. Here, we used native mass spectrometry and molecular dynamics simulations to probe the interactions between 19 PFAS of environmental concern and two isoforms of the major bovine whey protein β-lactoglobulin (β-LG). We observed that six of these PFAS bound to both protein isoforms with low- to mid-micromolar dissociation constants. Based on quantitative, competitive binding experiments with endogenous ligands, PFAS can bind orthosterically and preferentially to β-LG's hydrophobic ligand-binding calyx. β-Cyclodextrin can also suppress binding of PFAS to β-LG owing to the ability of β-cyclodextrin to directly sequester PFAS from solution. This research sheds light on PFAS-β-LG binding, suggesting that such interactions could impact lipid-fatty acid transport in bovine mammary glands at high PFAS concentrations. Furthermore, our results highlight the potential use of β-cyclodextrin in mitigating PFAS binding, providing insights toward the development of strategies to reduce PFAS accumulation in dairy products and other biological systems.

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Source
http://dx.doi.org/10.1021/acs.chemrestox.4c00021DOI Listing

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