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Title: Unveiling the Interaction of Vanadium Compounds with Human Serum Albumin by Using 1H STD NMR and Computational Docking Studies
Authors: Dias, David M. 
Rodrigues, João P. G. L. M. 
Domingues, Neuza S. 
Bonvin, Alexandre M. J. J. 
Castro, M. M. C. A. 
Keywords: Proteins; Docking studies; Drug delivery; Vanadium; NMR spectroscopy
Issue Date: 2013
Publisher: Wiley-VCH Verlag
Serial title, monograph or event: European Journal of Inorganic Chemistry
Volume: 2013
Issue: 26
Abstract: The binding of the VV oxidation products of two vanadium( IV) compounds, [VO(dmpp)2] and [VO(maltolato)2], which have shown promising anti-diabetic properties, to human serum albumin (HSA) in aqueous aerobic solution has been studied by 1H saturation transfer difference (STD) NMR spectroscopy and computational docking studies. Group epitope mapping and docking simulations indicate a preference of HSA binding to the 1:1 [VO2(dmpp)(OH)(H2O)]– and 1:2 [VO2(maltol)2]– vanadium(V) species. By using known HSA binders, competition NMR experiments revealed that both complexes preferentially bind to drug site I. Docking simulations carried out with HADDOCK together with restraints derived from the STD results led to three-dimensional models that are in agreement with the NMR spectroscopic data, providing useful information on molecular interaction modes. These results indicate that the combination of STD NMR and data-driven docking is a good tool for elucidating the interactions in protein–vanadium compounds and thus for clarifying the mechanism of drug delivery as vanadium compounds have shown potential therapeutic properties.
DOI: 10.1002/ejic.201300419
Rights: openAccess
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais

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