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Related Experiment Videos

Lysozyme adsorption studies at the silica/water interface using dual polarization interferometry.

Jian R Lu1, Marcus J Swann, Louise L Peel

  • 1Biological Physics Group, Department of Physics, UMIST, PO Box 88, Manchester M60 1QD, United Kingdom.

Langmuir : the ACS Journal of Surfaces and Colloids
|April 2, 2005
PubMed
Summary

Dual polarization interferometry reveals how lysozyme protein adsorbs to silica surfaces. Adsorption behavior changes with pH and concentration, forming deformed monolayers and bilayers, with largely reversible adsorption upon pH cycling.

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Area of Science:

  • Surface science
  • Biophysics
  • Analytical chemistry

Background:

  • Understanding protein adsorption at interfaces is crucial for biomaterials and biosensors.
  • Lysozyme is a model protein frequently studied for its adsorption behavior.
  • Previous studies used techniques like neutron reflection, but lacked real-time molecular layer information.

Purpose of the Study:

  • To investigate lysozyme adsorption dynamics at the silica/water interface using dual polarization interferometry.
  • To quantify layer thickness and mass coverage under varying pH and concentration conditions.
  • To assess the reversibility of lysozyme adsorption upon pH changes.

Main Methods:

  • Utilized dual polarization interferometry (DPI) for real-time monitoring of molecular layer changes.

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  • Studied lysozyme adsorption at concentrations ranging from 0.03 to 4.0 g dm⁻³.
  • Investigated adsorption at pH 4 and pH 7, including pH cycling experiments.

    • Main Results:

    • Observed adsorbed layer thicknesses from 14 to 54 ± 1 Å and mass coverages from 0.21 to 3.29 ± 0.05 mg m⁻².
    • Identified significant structural deformation of lysozyme monolayers at low concentrations and formation of bilayers at high concentrations.
    • Demonstrated broadly reversible lysozyme adsorption upon pH cycling between 4 and 7.

    Conclusions:

    • Dual polarization interferometry provides detailed insights into lysozyme adsorption kinetics and layer structure.
    • Lysozyme adsorption is concentration and pH-dependent, involving monolayer deformation and bilayer formation.
    • The adsorption process is largely reversible, indicating potential for controlled surface functionalization.