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Vanadium and proteins: Uptake, transport, structure, activity and function
Ternary complex formation between VO(IV)-picolinic acid or VO(IV)-6-methylpicolinic acid and small blood serum bioligands.
Interaction of antidiabetic vanadium compounds with hemoglobin and red blood cells and their distribution between plasma and erythrocytes.
The results indicate that, in the studies on the transport of a potential pharmacologically active V species, the interaction with red blood cells and Hb cannot be neglected, that a distribution between the erythrocytes and plasma is achieved, and that these processes can significantly influence the effectiveness of a V drug.
Oxovanadium(IV) complexes of quinoline derivatives
Structural and redox requirements for the action of anti-diabetic vanadium compounds.
- Y. Yoshikawa, H. Sakurai, D. Crans, G. Micera, E. Garribba
- ChemistryDalton transactions
- 15 April 2014
The results suggest that a V(IV)O functionality is necessary for vanadium complexes to exhibit anti-diabetic effects, which agrees with the notion that the biotransformations of V compounds in the organism are more important than the nature of the species.
Polyoxovanadates with emerging biomedical activities
Antitumoral effect of vanadium compounds in malignant melanoma cell lines.
Physicochemical, antioxidant, DNA cleaving properties and antimicrobial activity of fisetin-copper chelates.
Potentiometric, spectroscopic, electrochemical and DFT characterization of oxovanadium(IV) complexes formed by citrate and tartrates in aqueous solution at high ligand to metal molar ratios: the…
A discussion on the possible form of VO(IV)-citrate complexes in blood serum is presented, where it is found that the most relevant species under physiological conditions should be [VO(citrH(-1))]2-.
Binding of VIVO2+ to the Fe binding sites of human serum transferrin. A theoretical study
- G. Justino, E. Garribba, J. Pessoa
- Chemistry, PhysicsJBIC Journal of Biological Inorganic Chemistry
- 20 August 2013
The binding of VIVO2+ to human serum transferrin (hTF) at the FeIII binding sites is addressed and the one that yields the lowest calculated heats of formation and minimum deviations from the experimental values of the 51V and 14N A tensor components is the structure that includes CO32− as a synergistic anion.