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Molecular Interaction between a Gadolinium–Polyoxometalate and Human Serum Albumin
Author(s) -
Zheng Li,
Ma Ying,
Zhang Guangjin,
Yao Jiannian,
Bassil Bassem S.,
Kortz Ulrich,
Keita Bineta,
de Oliveira Pedro,
Nadjo Louis,
Craescu Constantin T.,
Miron Simona
Publication year - 2009
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.200900610
Subject(s) - chemistry , isothermal titration calorimetry , human serum albumin , circular dichroism , gadolinium , polyoxometalate , tryptophan , protein secondary structure , fluorescence spectroscopy , fluorescence , stereochemistry , crystallography , biochemistry , organic chemistry , amino acid , physics , quantum mechanics , catalysis
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(β 2 ‐SiW 11 O 39 ) 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.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)