Abstract
Inorganic functionalization of the decavanadate anion promotes a different type of interaction with model proteins thaumatin, lysozyme, proteinase K, human serum albumin and transferrin.
Highlights
The decavanadate anion, HxV10O28(6Àx)À (V10), is one of the most studied vanadium polyoxometalate species
To the best of our knowledge, the work of Schwendt et al.[61] presenting the synthesis and characterization of (2-hepH)2[{Cu(H2O)2(2-hep)}2V10O28]Á6H2O is the only one reporting a coordination compound of decavanadate that stays intact in aqueous solution
A reversed addition of the individual reaction components and stepwise acidification of the solution prevented formation of heavy precipitates that were described in the original procedure[61] and such an approach resulted in successful isolation of V10Cu containing the [{Cu(H2O)2(2-hep)}2V10O28]2À complex anion and a new compound V10Co composed of the purely inorganic complex anion [{Co(H2O)5}2V10O28]2À
Summary
The decavanadate anion, HxV10O28(6Àx)À (V10), is one of the most studied vanadium polyoxometalate species. It has been shown that V10Co is stable in the presence of proteins and for the first time it was possible to study the interaction of decavanadate with proteins without the interference of lower vanadate oligomers. This allowed comparison of interactions of V10 and V10Co with the model proteins thaumatin, lysozyme, proteinase K, human serum albumin and transferrin under conditions close to biological ones (0.1 M 2-(N-morpholino)ethanesulfonic acid, 0.5 M NaCl, pH = 5.8). The oxygen atoms OB and OC are potential sites for protonation, and the atoms OC, OF, OG and OD are the most potential sites for ligation to transition metal ions.[31,32]
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