Formation and Characterization of Stable Human Serum Albumin−Tris-malonic Acid [C60]Fullerene Complex

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 an...

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Veröffentlicht in:	Bioconjugate chemistry 2005-09, Vol.16 (5), p.1058-1062
Hauptverfasser:	Belgorodsky, Bogdan, Fadeev, Ludmila, Ittah, Varda, Benyamini, Hadar, Zelner, Stanislav, Huppert, Dan, Kotlyar, Alexander B, Gozin, Michael
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids Biochemistry Chromatography, Gel Cytochromes c - chemistry Cytochromes c - metabolism Fullerenes - chemistry Humans Immunoglobulins Malonates - chemistry Models, Molecular Protein Structure, Tertiary Proteins Serum Albumin - chemistry Spectrometry, Fluorescence Spectrometry, Mass, Electrospray Ionization Superoxide Dismutase - chemistry Superoxide Dismutase - metabolism Tromethamine - chemistry Xanthine Oxidase - chemistry Xanthine Oxidase - metabolism
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Zusammenfassung:	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.
ISSN:	1043-1802 1520-4812
DOI:	10.1021/bc050103c