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In certain chromatographic separations, solutes transfer between the mobile phase and the stationary phase via sorption, which typically refers to the process of adsorption. For many chromatographic systems, the sorption process often depends on the polarity of the compounds—an expression of the overall dipole moment within the molecule. During the separation process, there is competition between the solute and solvent for adsorption to the stationary phase. Highly polar compounds and...
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Enhanced protein adsorption upon bulk phase separation.

Madeleine R Fries1, Daniel Stopper2, Maximilian W A Skoda3

  • 1Institute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany.

Scientific Reports
|June 27, 2020
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Summary
This summary is machine-generated.

Multivalent ions can induce protein adsorption or a wetting layer in protein solutions, depending on concentration and temperature. This wetting phenomenon is linked to liquid-liquid phase separation and ion-activated substrates.

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Area of Science:

  • Protein adsorption
  • Biotechnology
  • Heterogeneous nucleation
  • Liquid-liquid phase separation (LLPS)

Background:

  • Understanding protein adsorption forces is crucial across medicine, biotechnology, and nucleation science.
  • Protein behavior at interfaces is complex and influenced by solution conditions.

Purpose of the Study:

  • To investigate the mechanism of wetting transitions in protein solutions.
  • To understand the role of multivalent ions and liquid-liquid phase separation (LLPS) in protein adsorption.

Main Methods:

  • Ellipsometry
  • Quartz-crystal microbalance with dissipation (QCM-D)
  • Density-functional theory (DFT)
  • Modeling proteins as limited-valence (patchy) particles

Main Results:

  • Multivalent ions induced either simple adsorption or a wetting layer for bovine serum albumin (BSA) on a negatively charged interface.
  • Wetting layer formation was observed near liquid-liquid phase separation (LLPS) conditions, influenced by protein concentration (cp) and temperature (T).
  • The water-to-protein ratio was significantly higher in the wetting layer compared to simple adsorption.

Conclusions:

  • A wetting transition mechanism was identified for complex protein systems.
  • Ion-activated attractive substrates and bulk instability from metastable LLPS drive this wetting phenomenon.