@article {1600,
	title = {Metal complexes in medicinal chemistry: new vistas and challenges in drug design},
	journal = {Dalton Transactions},
	number = {6},
	year = {2006},
	note = {ISI Document Delivery No.: 014YVTimes Cited: 60Cited Reference Count: 44},
	month = {Feb},
	pages = {761-764},
	type = {Article},
	abstract = {An overview is presented of selected metal-bases! pharmaceuticals, either diagnostic or therapeutic, with emphasis on specific attributes and in vivo interactions of these compounds relevant to their use in medicinal applications. Both the advantages and the challenges of this approach are outlined, with possibilities for future developments accentuated.},
	keywords = {AGENTS, BINDING CONSTANTS, BIS(MALTOLATO)OXOVANADIUM(IV), GLUCOSE, HUMAN-SERUM TRANSFERRIN, MODULATION, therapy, TRANSPORT},
	isbn = {1477-9226},
	url = {<Go to ISI>://000235520000001},
	author = {Thompson, K. H. and Orvig, Chris}
}
@article {3927,
	title = {Tripodal aminophenolate ligand complexes of aluminum(III), gallium(III), and indium(III) in water},
	journal = {Inorganic Chemistry},
	volume = {36},
	number = {2},
	year = {1997},
	note = {ISI Document Delivery No.: WC887Times Cited: 34Cited Reference Count: 53},
	month = {Jan},
	pages = {236-248},
	type = {Article},
	abstract = {Four water-soluble amine phenols have been prepared: tris(((2-hydroxy-5-sulfobenzyl)amino)ethyl)amine (H(6)TRNS), 1,1,1-tris(((2-hydroxy-5-sulfobenzyl)amino)methyl)ethane (H(6)TAMS), 1,2,3-tris((2-hydroxy-5-sulfobenzyl)amino)propane (H(6)TAPS), and cis,cis-1,3,5-tris((2-hydroxy-5-sulfobenzyl)amino)cyclohexane (H(6)TACS). Complex formation constants have been measured at 25 degrees C (mu = 0.16 M NaCl): log K [M(TRNS)](3-) ([M(HTRNS)](2-)) M = Ga 28.55 (36.90), In 29.3 (34.9); log K [M(TAMS)](3-) ([M(HTAMS)](2-)) M = Al 22.5 (29.3), Ga 31.53, In 28.49; log K [M(TAPS)](3-) ([M(HTAPS)](2-)) M = Al 22.8 (29.0), Ga 31.54 (35.15), In 27.56 (31.93). The order of stability is Ga(III) > In(III) > Al(III) for H(6)TAMS and H(6)TAPS, while far H(6)TRNS it is Ga(III) approximate to In(lII) > Al(III). The solution structures of the complexes have been probed by multinuclear NMR (H-1, C-13, Al-27, Ga-71, In-115) and UV spectroscopic studies, and these solution structures are compared with solid state structures for analogous complexes. The H-1 NMR spectrum in D2O establishes TAPS to be preorganized for metal ion binding. H(6)TACS exists in the wrong conformation for metal ion binding, and this results in slow complexation kinetics and relatively weaker binding.},
	keywords = {ACID, BINDING, EQUILIBRIUM-CONSTANTS, GA(III), HUMAN-SERUM TRANSFERRIN, IN(III), IN-VIVO, METAL-IONS, SCHIFF-BASE LIGANDS, STABILITIES},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1997WC88700021},
	author = {Caravan, P. and Orvig, Chris}
}
@article {3692,
	title = {Speciation of aluminum in biological systems},
	journal = {Journal of Toxicology and Environmental Health},
	volume = {48},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: VE144Times Cited: 99Cited Reference Count: 131Research Issues in Aluminum Toxicity WorkshopJUL, 1995VANCOUVER, CANADA},
	month = {Aug},
	pages = {543-568},
	type = {Proceedings Paper},
	abstract = {As a {\textquoteright}{\textquoteright}hard{\textquoteright}{\textquoteright} trivalent metal ion, Al3+ binds strongly to oxygen-donor ligands such as citrate and phosphate. The aqueous coordination chemistry of Al is complicated by the tendency of many Al complexes to hydrolyze and form polynuclear species, many of which are sparingly soluble. Thus there is considerable variation among the Al stability constants reported for several important ligands. The complexity in the aqueous chemistry of Al has also affected Al toxicity studies, which have often utilized poorly characterized Al stock solutions. Serum fractionation studies show that most Al is protein bound, primarily to the serum iron transport protein transferrin. Albumin appears to play little, if any, role in serum transport. There is little agreement as to the speciation of the remaining low-molecular-mass fraction of serum Al. The lability of the Al3+ ion precludes the simple separation and identification of individual Al complexes. Computational methods are available for detailed computer calculations of the Al speciation in serum, but efforts in this area have been severely hampered by the uncertainties regarding the stability constants of the low molecular mass Al complexes with Citrate, phosphate, and hydroxide. Specific recommendations for further research on Al speciation include: (1) Determine more accurate Al stability constants with critical low molecular mass ligands such as citrate and phosphate; (2) supplement traditional potentiometric studies on Al complexes with data from other techniques such as Al-27-NMR and accelerator mass spectrometry with Al-26; (3) develop new methods for generating reliable linear free energy relationships for Al complexation; (4) determine equilibrium and rate constants for Al binding to transferrin al 37 degrees C; (5) confirm the possible formation of low-molecular-mass Al-protein complexes following desferrioxamine therapy; (6) continue research efforts to incorporate kinetic considerations into the present equilibrium speciation calculations; (7) improve methods for preparing chemically well-defined stock solutions for toxicological studies; (8) incorporate more detailed speciation data into studies on Al toxicity and pharmacokinetics; and (9) incorporate more detailed speciation data into future epidemiological studies on the relationship between Al toxicity and various water quality parameters.},
	keywords = {ALZHEIMERS-DISEASE, DIETARY CONSTITUENTS, DRINKING-WATER, GASTROINTESTINAL ABSORPTION, HUMAN-SERUM TRANSFERRIN, MURINE, NEUROBLASTOMA-CELLS, POTENTIAL, PROTEIN-BINDING, SIGNIFICANCE INVIVO, SIZE-EXCLUSION CHROMATOGRAPHY, THERAPEUTIC CHELATING-AGENTS},
	isbn = {0098-4108},
	url = {<Go to ISI>://A1996VE14400005},
	author = {Harris, W. R. and Berthon, G. and Day, J. P. and Exley, C. and Flaten, T. P. and Forbes, W. F. and Kiss, T. and Orvig, Chris and Zatta, P. F.}
}
