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Related Experiment Videos

Conformational changes in SP-B as a function of surface pressure.

Wilfred K Fullagar1, Karen A Aberdeen, David G Bucknall

  • 1School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia.

Biophysical Journal
|September 26, 2003
PubMed
Summary

Surfactant-associated protein B (SP-B) changes structure at the air/water interface under pressure, influencing protein squeeze-out and lipid exchange. Neutron reflectivity reveals water and proton exchange within SP-B monolayers.

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Area of Science:

  • Biophysics
  • Surface Chemistry
  • Structural Biology

Background:

  • Surfactant-associated protein B (SP-B) plays a crucial role in lung function.
  • Understanding protein behavior at interfaces is vital for biological and medical applications.

Purpose of the Study:

  • To investigate the structural changes of bovine and sheep SP-B at the air/water interface.
  • To correlate structural changes with phenomena like protein squeeze-out and lipid exchange.
  • To develop and apply an algorithm for analyzing reflectivity data.

Main Methods:

  • X-ray and neutron reflectivity measurements.
  • Pressure-area isotherm analysis.
  • Application of box/layer models for scattering-length density profile fitting.

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  • Inclusion of instrumental resolution in data analysis.

    • Main Results:

    • SP-B undergoes tertiary structural changes at the air/water interface influenced by surface pressure.
    • These changes are linked to protein squeeze-out and lipid exchange dynamics.
    • Neutron reflectivity indicates significant water and labile proton exchange within bovine SP-B monolayers.
    • Water is partially expelled from the monolayer at higher surface pressures.

    Conclusions:

    • Surface pressure induces conformational changes in SP-B, impacting its interfacial behavior.
    • The developed algorithm aids in accurate characterization of interfacial protein structures.
    • SP-B's interaction with water and protons is dynamic and pressure-dependent.