Journal
EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
Volume -, Issue 34, Pages 5189-5193Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ejic.200900610
Keywords
Gadolinium; Polyoxometalates; Fluorescence; Energy transfer; Protein structures
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Funding
- European Community [040487]
- Chinese Academy of Science
- National Natural Science Foundation of China [20733006, 50720145202]
- Jacobs University [2006CB806200]
- German Science Foundation (DFG) [KO-2288/8-1]
- Fonds der Chemischen Industrie
- Centre National de la Recherche Scientifique (CNRS) [UMR 8000]
- Universite Paris-Sud 11, France
- INSERM U 759/Institut Curie-Recherche
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Polyoxometalates (POMs) show promising antibacterial, antiviral (particularly anti-HIV), antitumor, and anticancer activities, but the mechanism of these potential therapeutic effects remains to be elucidated at the molecular level. The interaction between the Gd-containing tungstosilicate [Gd(beta(2)-SiW11O39)(2)](13-) and human serum albumin (HSA) was studied by several techniques. Fluorescence spectroscopy showed an energy transfer between the single tryptophan residue of HSA and the POM. Circular dichroism led to the conclusion that the POM significantly altered the secondary structure of HSA. Isothermal titration calorimetry revealed an enthalpy-driven binding reaction between HSA and the POM, resulting in the formation of a 1:1 complex. ((C) Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)
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