EPR Methods Applied on Food Analysis

An overview of the different methodologies developed so far for the investigation of paramagnetic species in foods is presented. Electron paramagnetic resonance spectroscopy (EPR), also known as electron spin resonance spectroscopy (ESR), is the primary technique toward the development of methods for the exploration of EPR-sensitive species, such as free radicals, reactive oxygen species (ROS), nitrogen reactive species (NRS), and C-centered radicals and metal ions. These methods aim for: (a) quantification of radical species, (b) exploration of redox chemical reaction mechanisms in foods, (c) assessment of the antioxidant capacity of food, and (d) food quality, stability, and food shelf life. For these purposes, different radical initiations and detections have been used in foods depending on both the chemistry of the target system and the kind of information required, listed in: the induction of radicals by (a) microwave, UV, or γ-radiation; (b) heating; (c) addition of metals; and (d) use of oxidants

pH-Potentiometric Investigation towards Chelating Tendencies of p-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes

Copper ions in the active sites of several proteins/enzymes interact with phenols and quinones, and this interaction is associated to the reactivity of the enzymes. In this study the speciation of the Cu2+ with iminodiacetic phenolate/hydroquinonate ligands has been examined by pH-potentiometry. The results reveal that the iminodiacetic phenol ligand forms mononuclear complexes with Cu2+ at acidic and alkaline pHs, and a binuclear Ophenolate-bridged complex at pH range from 7 to 8.5. The binucleating hydroquinone ligand forms only 2 : 1 metal to ligand complexes in solution. The pK values of the protonation of the phenolate oxygen of the two ligands are reduced about 2 units after complexation with the metal ion and are close to the pK values for the copper-interacting tyrosine phenol oxygen in copper enzymes

Insulin-mimetic action of vanadium compounds on osteoblast-like cells in culture

Vanadium compounds mimic insulin actions in different cell types. The present study concerns the insulin-like effects of three vanadium(V) derivatives and one vanadium(IV) complex on osteoblast-like (UMR106 and MC3T3E1) cells in culture. The vanadium oxalate and vanadium citrate complexes hydrolyzed completely under the culture conditions, whereas more than 40% of the vanadium tartrate and nitrilotriacetate complexes remained. Vanadate, as well as vanadium oxalate, citrate, and tartrate complexes enhanced cell proliferation (as measured by the crystal violet assay), glucose consumption, and protein content in UMR106 and MC3T3E1 osteoblast-like cells. The vanadium nitrilotriacetate complex (the only peroxo complex tested) stimulated cell proliferation in UMR106 but not in MC3T3E1 cells. This derivative strongly transformed the morphology of the MC3T3E1 cells. All vanadium(V) compounds inhibited cell differentiation (alkaline phosphatase activity) in UMR106 cells. Our data are consistent with the interpretation that vanadium oxalate and citrate complexes hydrolyze to vanadate. Vanadium nitrilotriacetate would appear to be toxic for normal MC3T3E1 osteoblasts. In contrast, the vanadium tartrate complex induced a proliferative effect; however, it did not alter cell differentiation

Insulin-mimetic action of vanadium compounds on osteoblast-like cells in culture

Vanadium compounds mimic insulin actions in different cell types. The present study concerns the insulin-like effects of three vanadium(V) derivatives and one vanadium(IV) complex on osteoblast-like (UMR106 and MC3T3E1) cells in culture. The vanadium oxalate and vanadium citrate complexes hydrolyzed completely under the culture conditions, whereas more than 40% of the vanadium tartrate and nitrilotriacetate complexes remained. Vanadate, as well as vanadium oxalate, citrate, and tartrate complexes enhanced cell proliferation (as measured by the crystal violet assay), glucose consumption, and protein content in UMR106 and MC3T3E1 osteoblast-like cells. The vanadium nitrilotriacetate complex (the only peroxo complex tested) stimulated cell proliferation in UMR106 but not in MC3T3E1 cells. This derivative strongly transformed the morphology of the MC3T3E1 cells. All vanadium(V) compounds inhibited cell differentiation (alkaline phosphatase activity) in UMR106 cells. Our data are consistent with the interpretation that vanadium oxalate and citrate complexes hydrolyze to vanadate. Vanadium nitrilotriacetate would appear to be toxic for normal MC3T3E1 osteoblasts. In contrast, the vanadium tartrate complex induced a proliferative effect; however, it did not alter cell differentiation.Facultad de Ciencias Exacta

Insulin-mimetic action of vanadium compounds on osteoblast-like cells in culture

Vanadium compounds mimic insulin actions in different cell types. The present study concerns the insulin-like effects of three vanadium(V) derivatives and one vanadium(IV) complex on osteoblast-like (UMR106 and MC3T3E1) cells in culture. The vanadium oxalate and vanadium citrate complexes hydrolyzed completely under the culture conditions, whereas more than 40% of the vanadium tartrate and nitrilotriacetate complexes remained. Vanadate, as well as vanadium oxalate, citrate, and tartrate complexes enhanced cell proliferation (as measured by the crystal violet assay), glucose consumption, and protein content in UMR106 and MC3T3E1 osteoblast-like cells. The vanadium nitrilotriacetate complex (the only peroxo complex tested) stimulated cell proliferation in UMR106 but not in MC3T3E1 cells. This derivative strongly transformed the morphology of the MC3T3E1 cells. All vanadium(V) compounds inhibited cell differentiation (alkaline phosphatase activity) in UMR106 cells. Our data are consistent with the interpretation that vanadium oxalate and citrate complexes hydrolyze to vanadate. Vanadium nitrilotriacetate would appear to be toxic for normal MC3T3E1 osteoblasts. In contrast, the vanadium tartrate complex induced a proliferative effect; however, it did not alter cell differentiation.Facultad de Ciencias Exacta

Synthesis, Solution, and Structural Characterization of Tetrahydrofuranyl-2,2-Bisphosphonic Acid Disodium Salt

Bisphosphonates are biologically relevant therapeutics for bone disorders and cancer. Reaction of γ-chlorobutyric acid, phosphorus acid, and phosphorus trichloride without the use of solvent gave the tetrahydrofuranyl-2,2-bisphosphonate sodium salt (Na2H2L). The Na2H2L was isolated, characterized in solution by 1H, 13C, and 31P NMR spectroscopy and in solid state by single X-Ray crystallography. The crystal structure showed that the Na2H2L forms in the crystal infinite two-dimensional sheets stacked one parallel to the other. A comparison of the chelating properties of H2L2− with similar hydroxyl bisphosphonate ligands shows that the strength of the Na–O(furanyl/hydroxyl) bond is directly related to the total charge of the ligand anion

Cation-selective Mutations in the M2 Domain of the Inhibitory Glycine Receptor Channel Reveal Determinants of Ion-Charge Selectivity

Ligand-gated ion channel receptors mediate neuronal inhibition or excitation depending on their ion charge selectivity. An investigation into the determinants of ion charge selectivity of the anion-selective α1 homomeric glycine receptor (α1 glycine receptor [GlyR]) was undertaken using point mutations to residues lining the extra- and intracellular ends of the ion channel. Five mutant GlyRs were studied. A single substitution at the intracellular mouth of the channel (A-1′E GlyR) was sufficient to convert the channels to select cations over anions with PCl/PNa = 0.34. This result delimits the selectivity filter and provides evidence that electrostatic interactions between permeating ions and pore residues are a critical factor in ion charge selectivity. The P-2′Δ mutant GlyR retained its anion selectivity (PCl/PNa = 3.81), but it was much reduced compared with the wild-type (WT) GlyR (PCl/PNa = 27.9). When the A-1′E and the P-2′Δ mutations were combined (selectivity double mutant [SDM] GlyR), the relative cation permeability was enhanced (PCl/PNa = 0.13). The SDM GlyR was also Ca2+ permeable (PCa/PNa = 0.29). Neutralizing the extracellular mouth of the SDM GlyR ion channel (SDM+R19′A GlyR) produced a more Ca2+-permeable channel (PCa/PNa = 0.73), without drastically altering monovalent charge selectivity (PCl/PNa = 0.23). The SDM+R19′E GlyR, which introduces a negatively charged ring at the extracellular mouth of the channel, further enhanced Ca2+ permeability (PCa/PNa = 0.92), with little effect on monovalent selectivity (PCl/PNa = 0.19). Estimates of the minimum pore diameter of the A-1′E, SDM, SDM+R19′A, and SDM+R19′E GlyRs revealed that these pores are larger than the α1 GlyR, with the SDM-based GlyRs being comparable in diameter to the cation-selective nicotinic acetylcholine receptors. This result provides evidence that the diameter of the ion channel is also an important factor in ion charge selectivity

Cobalt(II), nickel(II) and zinc(II) coordination chemistry of the N , N ′-disubstituted hydroxylamine-(diamido) ligand, 3,3′-(hydroxyazanediyl)dipropanamide

Although directly relevant to metal mediated biological nitrification and the coordination chemistry of peroxide, the transition metal complexes of hydroxylamines and their functionalized variants remain mainly unexplored except vanadium(V) and molybdenum(VI). Reaction of the chelating hydroxylamine ligand 3,3′-(hydroxyazanediyl)dipropanamide (Hhydia) with [MII(CH3COO)2]·xH2O (M = CoII, ZnII) in methyl alcohol solution yields the complexes [CoII(η1:η1-CH3COO)(η1-CH3COO)(Hhydia)], (1) and [ZnII(η1-CH3COO)2(Hhydia)], (4), while reaction of Hhydia with trans-[NiIICl2(H2O)4]·2H2O yields [NiII(Hhydia)2]Cl2 (3). The X-ray structure analysis of 1 and 4 revealed that the CoII and ZnII atoms are bonded to a neutral tridentate O,N,O-Hhydia ligand and a chelate and a monodentate acetate groups in a severely distorted octahedral geometry for 1 and two monodentate acetate groups for 4 in a highly distorted trigonal bipyramidal geometry (τ = 0.63). The X-ray structure analysis of 3 revealed that the nickel atom in [NiII(Hhydia)2]2+ is bonded to two neutral tridentate O,N,O-Hhydia ligands. The twist angle, θ, in [NiII(Hhydia)2]2+ is 55.1(2)°, that is, very close to an ideal octahedron. The metal/Hhydia complexes were studied by UV–Vis (cobalt and nickel compounds), NMR (zinc compounds), HR-MS spectroscopy. The 1H and 13C NMR spectra of the methyl alcohol or acetonitrile solutions of ZnII-Hhydia complexes show the existence of both the 1:1 and 1:2 metal:ligand species being in dynamic equilibrium. The exchange processes between the ZnII-Hhydia is through complete dissociation-association of the ligand from the complexes as it is evident from the 2D {1H} EXSY NMR spectroscopy. UV–Vis spectroscopy of the CoII-Hhydia in methyl alcohol also shows the existence of both the 1:1 and 1:2 metal:ligand species in contrast to 1:2 complex [NiII(Hhydia)2]2+ which is the only species found in solution. The NMR and UV–Vis observations are additionally supported by the HR-MS studies