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Nanoscopic surfactant behavior of the porin MspA in aqueous media

Ayomi S Perera1, Hongwang Wang, Tej B Shrestha

  • 1Kansas State University, Department of Chemistry, CBC Building 201, Manhattan, KS 66506, USA.

Beilstein Journal of Nanotechnology
|June 15, 2013
PubMed

Insights

Mycobacterial porin MspA, a highly stable protein, forms nanoscale vesicles acting as a surfactant. This behavior deviates from classical surface chemistry principles, especially at high temperatures.

Area of Science:

  • Biophysics
  • Materials Science
  • Protein Chemistry

Background:

  • Mycobacterial porin MspA is exceptionally stable, retaining structure at high temperatures.
  • MspA forms vesicles in aqueous solutions, suggesting surfactant-like properties.

Purpose of the Study:

  • To investigate the principles and thermodynamic factors governing MspA vesicle formation.
  • To explore MspA's behavior as a nanoscale surfactant at elevated temperatures.

Main Methods:

  • Dynamic light scattering (DLS)
  • Transmission electron microscopy (TEM)
  • Electrophoretic light scattering (ELS) for zeta-potential measurements

Main Results:

  • MspA exhibits nanoscale surfactant behavior, forming vesicles in aqueous buffers.
  • Vesicle formation is temperature-dependent, studied up to 343 K.
  • MspA's stability allows investigation at temperatures where most proteins denature.

Conclusions:

  • MspA vesicle formation deviates from classical surface chemistry principles.
  • Nanoscale surfactant behavior of MspA is confirmed.
  • Thermodynamic factors influencing MspA vesicle formation are elucidated.
Keywords:
charge-interactionhydrophobic interactionliposome-type clusterprotein clustersupramoleculartemperature influencezeta potential

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