Formation and characterization of stable human serum albumin-tris-malonic acid [C60]fullerene complex

Bioconjug Chem. 2005 Sep-Oct;16(5):1058-62. doi: 10.1021/bc050103c.

Abstract

The preparation and characterization of the stable human serum albumin (HSA)-C3 isomer of tris-malonic acid [C60]fullerene complex is reported. Other than the anti-fullerene antibody, a stable protein-fullerene complex with a native protein has never been observed. This study may provide valuable answers to the growing concern regarding the effects of carbonaceous nanomaterials on human health on one hand and, on the other, may lead to the development of novel antioxidant therapeutic agents, radiopharmaceuticals, and components for bioelectronic devices.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, Gel
  • Cytochromes c / chemistry
  • Cytochromes c / metabolism
  • Fullerenes / chemistry*
  • Humans
  • Malonates / chemistry*
  • Models, Molecular
  • Protein Structure, Tertiary
  • Serum Albumin / chemistry*
  • Spectrometry, Fluorescence
  • Spectrometry, Mass, Electrospray Ionization
  • Superoxide Dismutase / chemistry
  • Superoxide Dismutase / metabolism
  • Tromethamine / chemistry*
  • Xanthine Oxidase / chemistry
  • Xanthine Oxidase / metabolism

Substances

  • Fullerenes
  • Malonates
  • Serum Albumin
  • Tromethamine
  • Cytochromes c
  • malonic acid
  • Superoxide Dismutase
  • Xanthine Oxidase
  • fullerene C60