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David M. Dias, João P. G. L. M. Rodrigues, Neuza S. Domingues, Alexandre M. J. J. Bonvin and M. Margarida C. A. Castro Unveiling the Interaction of Vanadium Compounds with Human Serum Albumin by Using 1H STD NMR and Computational Docking Studies European Journal of Inorganic Chemistry 2013

Version of Record online: 19 JUL 2013 | DOI: 10.1002/ejic.201300419

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1H STD NMR analysis complemented by HADDOCK studies have revealed that the [VO2(dmpp)(H2O)(OH)] species, resulting from the oxidation of the potential insulin mimetic VO(dmpp)2, binds preferentially to HSA site I. These findings corroborate the involvement of this serum protein in the transport of vanadium species in the blood stream and their delivery to target cells.

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