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Preferential solvent interactions between proteins and polyethylene glycols

J C Lee, L L Lee

    The Journal of Biological Chemistry
    |January 25, 1981
    PubMed
    Summary
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    Proteins are preferentially hydrated, with polyethylene glycol excluded from their domain, leading to thermodynamic instability and phase separation in solutions. Higher polymer molecular weight and protein hydrophobicity increase this destabilization.

    Area of Science:

    • Biophysical Chemistry
    • Solution Thermodynamics
    • Protein-Polymer Interactions

    Background:

    • Understanding protein-solvent interactions is crucial for bioprocessing and drug formulation.
    • Polyethylene glycols (PEGs) are widely used polymers in biological applications.
    • Preferential solvation phenomena influence protein stability and behavior in solution.

    Purpose of the Study:

    • To investigate preferential solvent interactions between polyethylene glycols (PEGs) and proteins.
    • To analyze the thermodynamic consequences of these interactions.
    • To elucidate the factors driving protein phase separation in PEG solutions.

    Main Methods:

    • Density measurements of PEG-protein systems across varying concentrations and molecular weights.

    Related Experiment Videos

  • Analysis using multicomponent theory.
  • Investigation at different pH values to assess ionic effects.

    • Main Results:

    • Proteins exhibit preferential hydration, with PEGs excluded from the protein domain.
    • Protein presence thermodynamically destabilizes the PEG solution, increasing with PEG concentration and molecular weight.
    • Destabilization correlates with protein hydrophobicity and hydrophilic/ionic residue content, with negative charges being more destabilizing.

    Conclusions:

    • Unfavorable thermodynamic interactions between PEGs and proteins, influenced by protein charge and mass, lead to phase separation.
    • PEG exclusion from the protein domain is a key factor driving this phenomenon.
    • Protein surface properties significantly impact solution stability.