Effect of heat shock protein 90 against ROS-induced phospholipid oxidation

Food Chem. 2018 Feb 1:240:642-647. doi: 10.1016/j.foodchem.2017.08.005. Epub 2017 Aug 2.

Abstract

The antioxidative role of Hsp90 purified from duck muscle on phospholipid was investigated in this study. Lipid oxidation was assessed by ferric thiocyanate method, and particle size, zeta potential measurements and transmission electron microscopy were employed to detect physical and chemical changes during oxidation of liposomes. Increase of the peroxidation products, decrease of the particle size and disruption of the spherical unity of the liposomes were detected when liposome was exposed to hydrogen peroxide (H2O2) oxidation, and Hsp90 was shown to protect liposome against oxidation. To further test the protection of Hsp90 on cell membrane, the Hsp90 transformed E. coli cell model was built. The Hsp90-containing E. coli showed higher survival and better membrane integrity as compared to the control upon H2O2 exposure. It is expected that Hsp90 plays an important role in the prevention of phospholipids oxidation in meat and has potential use as a food antioxidant.

Keywords: H(2)O(2); Hsp90; Lipid oxidation; Phospholipid.

MeSH terms

  • Escherichia coli
  • HSP90 Heat-Shock Proteins
  • Hydrogen Peroxide
  • Lipid Peroxidation
  • Liposomes
  • Phospholipids / metabolism*
  • Reactive Oxygen Species

Substances

  • HSP90 Heat-Shock Proteins
  • Liposomes
  • Phospholipids
  • Reactive Oxygen Species
  • Hydrogen Peroxide