@article {1176,
	title = {New insights into the interactions of serum proteins with bis(maltolato)oxovanadium(IV): Transport and biotransformation of insulin-enhancing vanadium pharmaceuticals},
	journal = {Journal of the American Chemical Society},
	volume = {127},
	number = {14},
	year = {2005},
	note = {ISI Document Delivery No.: 914LQTimes Cited: 39Cited Reference Count: 66},
	month = {Apr},
	pages = {5104-5115},
	type = {Article},
	abstract = {Significant new insights into the interactions of the potent insulin-enhancing compound bis(maltolato)oxovanadium(IV) (BMOV) with the serum proteins, apo-transferrin and albumin, are presented. Identical reaction products are observed by electron paramagnetic resonance (EPR) with either BMOV or vanadyl sulfate (VOSO4) in solutions of human serum apo-transferrin. Further detailed study rules out the presence of a ternary ligand-vanadyl-transferrin complex proposed previously. By contrast, differences in reaction products are observed for the interactions of BMOV and VOSO4 with human serum albumin (HSA), wherein adduct formation between albumin and BMOV is detected. In BMOV-albumin solutions, vanadyl ions are bound in a unique manner not observed in comparable solutions Of VOSO4 and albumin. Presentation of chelated vanadyl ions precludes binding at the numerous nonspecific sites and produces a unique EPR spectrum which is assigned to a BMOV-HSA adduct. The adduct species cannot be produced, however, from a solution Of VOSO4 and HSA titrated with maltol. Addition of maltol to a VOSO4-HSA solution instead results in formation of a different end product which has been assigned as a ternary complex, VO(ma)(HSA). Furthermore, analysis of solution equilibria using a model system of BMOV with 1-methylimidazole (formation constant log K = 4.5(1), by difference electronic absorption spectroscopy) lends support to an adduct binding mode (VO(ma)(2)-HSA) proposed herein for BMOV and HSA. This detailed report of an in vitro reactivity difference between VOSO4 and BMOV may have bearing on the form of active vanadium metabolites delivered to target tissues. Albumin binding of vanadium chelates is seen to have a potentially dramatic effect on pharmacokinetics, transport, and efficacy of these antidiabetic chelates.},
	keywords = {BINDING CONSTANTS, COMPLEXES, DEPENDENT DIABETES-MELLITUS, ELECTRON-PARAMAGNETIC RESONANCE, HUMAN SEROTRANSFERRIN, IN-VIVO, IRON REMOVAL, METALLOKINETIC ANALYSIS, MIMETIC AGENT, TRANSFERRIN},
	isbn = {0002-7863},
	url = {<Go to ISI>://000228229600036},
	author = {Liboiron, B. D. and Thompson, K. H. and Hanson, G. R. and Lam, E. and Aebischer, N. and Orvig, Chris}
}
@inbook {1012,
	title = {Vanadium compounds in the treatment of diabetes},
	booktitle = {Metal Ions in Biological Systems, Vol 41: Metal Ions and Their Complexes in Medication},
	series = {Metal Ions in Biological Systems},
	volume = {41},
	year = {2004},
	note = {ISI Document Delivery No.: BBZ13Times Cited: 38Cited Reference Count: 148Review270 MADISON AVE, NEW YORK, NY 10016 USA},
	pages = {221-252},
	publisher = {Marcel Dekker},
	organization = {Marcel Dekker},
	address = {New York},
	keywords = {ELECTRON-PARAMAGNETIC-RESONANCE, GLUCOSE-HOMEOSTASIS, IMPROVES GLYCEMIC CONTROL, IN-VIVO, INSULIN-RESISTANCE, ISOLATED, METALLOKINETIC ANALYSIS, OXYGEN-BRIDGED DIMER, PEROXOVANADIUM COMPOUNDS, PHOSPHOTYROSINE PHOSPHATASE INHIBITORS, RAT ADIPOCYTES},
	isbn = {0161-5149},
	url = {<Go to ISI>://000228348900007},
	author = {Thompson, K. H. and Orvig, Chris}
}
