$\alpha$-Tocopherol's Antioxidant Role: A Biophysical Perspective (bibtex)
by Drew T.C. Marquardt
Abstract:
I present evidence of an antioxidant mechanism for vitamin E that correlates strongly with its physical location in a model lipid bilayer. These data address the overlooked problem of the physical distance between the vitamin's reducing hydrogen and lipid acyl chain radicals. The combined data from neutron diffraction, NMR and UV spectroscopy experiments, all suggest that reduction of reactive oxygen species and lipid radicals occurs specifically at the membrane's hydrophobic-hydrophilic interface. The latter is possible when the acyl chain adopts conformations in which they snorkel to the interface from the hydrocarbon matrix. Moreover, not all model lipids are equal in this regard, as indicated by the small differences in the vitamin's location. The present result is a clear example of the importance of lipid diversity in controlling the dynamic structural properties of biological membranes. Importantly, these results suggest that measurements of alpha-tocopherol oxidation kinetics, and its products, should be revisited by taking into consideration the physical properties of the membrane in which the vitamin resides.
Reference:
Drew T.C. Marquardt, "$\alpha$-Tocopherol's Antioxidant Role: A Biophysical Perspective", PhD thesis, Brock University, 2014.
Bibtex Entry:
@phdthesis{2014-Marquardt,
  author={Drew T.C. Marquardt},
  title={$\alpha$-Tocopherol's Antioxidant Role: A Biophysical Perspective},
  year={2014},
  school={Brock University},
  note={Supervised by Thad A. Harroun},
  abstract={I present evidence of an antioxidant mechanism for vitamin E that correlates strongly with its physical location in a model lipid bilayer. These data address the overlooked problem of the physical distance between the vitamin's reducing hydrogen and lipid acyl chain radicals. The combined data from neutron diffraction, NMR and UV spectroscopy experiments, all suggest that reduction of reactive oxygen species and lipid radicals occurs specifically at the membrane's hydrophobic-hydrophilic interface. The latter is possible when the acyl chain adopts conformations in which they snorkel to the interface from the hydrocarbon matrix. Moreover, not all model lipids are equal in this regard, as indicated by the small differences in the vitamin's location. The present result is a clear example of the importance of lipid diversity in controlling the dynamic structural properties of biological membranes. Importantly, these results suggest that measurements of alpha-tocopherol oxidation kinetics, and its products, should be revisited by taking into consideration the physical properties of the membrane in which the vitamin resides.},
  url={http://hdl.handle.net/10464/5817}
}
Powered by bibtexbrowser