Protein adsorption on supported phospholipid bilayers

Karin Glasmästar1, Charlotte Larsson, Fredrik Höök

  • 1Department of Applied Physics, Chalmers University of Technology and Göteborg University, SE-412 96 Göteborg, Sweden. karing@fy.chalmers.se

Insights

Supported lipid bilayers made of egg-phosphatidylcholine (eggPC) lipids demonstrate significant protein resistance. Quartz crystal microbalance with dissipation (QCM-D) and surface plasmon resonance (SPR) confirmed minimal protein adsorption for various biomolecules.

Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Biophysics

Background:

  • Supported lipid bilayers (SLBs) are crucial for biomimetic interfaces.
  • Understanding protein adsorption onto SLBs is vital for biosensor and biomedical applications.
  • Egg-phosphatidylcholine (eggPC) is a common lipid for forming stable SLBs.

Purpose of the Study:

  • To investigate the protein resistance of supported eggPC lipid bilayers.
  • To quantify protein adsorption using Quartz Crystal Microbalance with Dissipation (QCM-D) and Surface Plasmon Resonance (SPR).
  • To compare protein adsorption of various biomolecules including fibrinogen, albumin, hemoglobin, cytochrome c, and immunoglobulin G (IgG).

Main Methods:

  • Formation of supported eggPC lipid bilayers on SiO(2) surfaces via vesicle adhesion and fusion.
  • Adsorption measurements using QCM-D for multiple proteins and 10% fetal bovine serum.
  • Comparative adsorption studies using SPR for fibrinogen and hIgG.

Main Results:

  • EggPC lipid bilayers exhibited high protein resistance, with irreversible adsorption below detection limits.
  • Reversible protein adsorption was observed, ranging from 0.3-4% of saturation coverage on a gold thiol monolayer.
  • SPR measurements indicated slightly higher adsorbed amounts compared to QCM-D.

Conclusions:

  • Supported eggPC lipid bilayers demonstrate excellent protein-repellent properties.
  • The findings suggest potential for using eggPC bilayers in applications requiring resistance to non-specific protein binding.
  • Further investigation into the mechanisms underlying this protein resistance is warranted.

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