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PubMed2004

A high-resolution titrator: a new approach to studying binding sites of microbial biosorbents.

The high-resolution potentiometric titration was used as a physico-chemical method to study the acid properties of selected biosorbent materials in order to quantify the functional acidic groups for sorption and to determine their affinities by considering their partial or total ionization equilibrium reactions. The Gran's method and the Henderson-Hasselbach's equation were employed in establishing the partition of the total acidity as associated with strong, weak and very weak acidic chemical active groups. The differences in the total organic acidity (A(TO)) for the two selected types of bacteria and two mycelia revealed by this method were explained by the chemical composition of their cell walls. The total organic acidities obtained were 3.87 me g(-1) for Thiobacillus ferrooxidans, 1.31 me g(-1) for Corynebacterium glutamicum, 0.81 me g(-1) for Aspergillus niger and 2.54 me g(-1) for Rhizopus arrhizus. The links between the activity of protons and the sorption capacities of the selected bioorganic matters were established. Sorption of lead by C. glutamicum and R. arrhizus biomass indicated an optimum pH of 6. It appeared that 64% (Pb(uptake)=0.48 me g(-1)) and 38% (Pb(uptake)=0.28 me g(-1)) of A(TO) were involved during lead sorption onto R. arrhizus and C. glutamicum, respectively. The applications of titration techniques become a powerful tool for the characterization of heterogeneous materials involved in biosorption and bioremediation processes.

Aspergillus niger↗
PubMed1999

A randomized, multicenter trial of weight-adjusted intravenous heparin dose titration and point-of-care coagulation monitoring in hospitalized patients with active thromboembolic disease. Antithrombotic Therapy Consortium Investigators.

BACKGROUND: Therapy with intravenous unfractionated heparin improves clinical outcome in patients with active thromboembolic disease, but achieving and maintaining a therapeutic level of anticoagulation remains a major challenge for clinicians. METHODS: A total of 113 patients requiring heparin for at least 48 hours were randomly assigned at 7 medical centers to either weight-adjusted or non-weight-adjusted dose titration. They were separately assigned to either laboratory-based or point-of-care (bedside) coagulation monitoring. RESULTS: Weight-adjusted heparin dosing yielded a higher mean activated partial thromboplastin time (aPTT) value 6 hours after treatment initiation than non-weight-adjusted dosing (99.9 vs 78.8 seconds; P =.002) and reduced the time required to exceed a minimum threshold (aPTT >45 seconds) of anticoagulation (10.5 vs 8.6 hours; P =.002). Point-of-care coagulation monitoring significantly reduced the time from blood sample acquisition to a heparin infusion adjustment (0.4 vs 1.6 hours; P <.0001) and to reach the therapeutic aPTT range (51 to 80 seconds) (16.1 vs 19.4 hours; P =.24) compared with laboratory monitoring. Although a majority of patients participating in the study surpassed the minimum threshold of anticoagulation within the first 12 hours and reached the target aPTT within 24 hours, maintaining the aPTT within the therapeutic range was relatively uncommon (on average 30% of the overall study period) and did not differ between treatment or monitoring strategies. CONCLUSIONS: Weight-adjusted heparin dosing according to a standardized titration nomogram combined with point-of-care coagulation monitoring using the BMC Coaguchek Plus System represents an effective and widely generalizable strategy for managing patients with thromboembolic disease that fosters the rapid achievement of a desired range of anticoagulation. Additional work is needed, however, to improve on existing patient-specific strategies that can more effectively sustain a therapeutic state of anticoagulation.

Adult↗
PubMed1999

Efficacy and tolerability of tasosartan, a novel angiotensin II receptor blocker: results from a 10-week, double-blind, placebo-controlled, dose-titration study. Tasosartan Investigators Group.

BACKGROUND: Angiotensin II receptor antagonists are selective blockers of the renin-angiotensin system and represent an alternative to angiotensin-converting enzyme inhibitors in the treatment of hypertension. Tasosartan is a newly developed nonpeptide AT1 receptor blocker. METHODS AND RESULTS: In this double-blind, randomized, dose-titration, multicenter trial, tasosartan and placebo were compared in patients with stage I and stage II hypertension. A prequalification washout period (antihypertensive medications withdrawn) and a 2-week qualification period (patients received single-blind placebo) preceded a 10-week, double-blind treatment period. The patients received either 50 mg tasosartan (n = 132) or placebo (n = 130) once per day and were evaluated once per week. The dose of tasosartan was increased at 3-week intervals to 100 mg and then to 200 mg if the mean sitting diastolic blood pressure (SiDBP) exceeded 90 mm Hg. Compared with placebo, tasosartan produced significantly (P <.05) greater reductions in both SiDBP (-9.4 +/- 0.7 vs -2.0 +/- 0.7 mm Hg) and sitting systolic blood pressure (SBP) (-12.2 +/- 1.2 vs +0.4 +/- 1.2 mm Hg). The rate of response (SiDBP </=90 mm Hg or a decrease from baseline of >/=10 mm Hg) was significantly (P <.05) greater in the tasosartan group than in the placebo group (55% vs 19%). The mean 24-hour blood pressure reduction with tasosartan was -12.6 +/- 0. 9/-8.1 +/- 0.6, significantly greater (P <.05) than the reduction with placebo (+0.6 +/- 0.9/+0.5 +/- 0.6 mm Hg). The trough-to-peak ratio (determined from the ambulatory data) was 0.66 for DBP and 0. 72 for SBP for the tasosartan treatment group, demonstrating 24-hour efficacy with once-a-day administration. The safety profile of tasosartan was similar to placebo. CONCLUSIONS: These results demonstrate that tasosartan at 50 to 200 mg given once a day over a titration period of 10 weeks was effective and safe in the treatment of essential hypertension.

Adult↗
PubMed2003

Equilibrium titration of protein-ligand binding affinity in the presence of volatile reagents--a semiautomated approach.

An existing method of equilibrium titration was significantly improved for investigating the effects of volatile anesthetics on Ca(2+) binding characteristics of human recombinant cardiac troponin C in in vitro conditions. The modified method increases stability of volatile compound concentrations in solution and allows for faster and more accurate data acquisition. The time to complete a titration series could be reduced from 28.3 +/- 6.2 min to 9.3 +/- 2.1 min, whereas the dispersion for pK(d) was decreased from 2.16 +/- 0.27 to 0.63 +/- 0.27. The method utilizes a semiautomatic approach to continuously monitor stability of fluorescence signals in a sealed chamber with greatly reduced air space.

Halothane↗
PubMed2003

Estimation of parvalbumin Ca(2+)- and Mg(2+)-binding constants by global least-squares analysis of isothermal titration calorimetry data.

The use of competitive isothermal titration calorimetry (ITC) to measure high-affinity binding constants has been largely restricted to systems with a single binding site or multiple identical sites. This study demonstrates the extension of this approach to proteins with two nonequivalent EF-hand Ca(2+)-binding sites--rat beta parvalbumin and the S55D/E59D variant of rat alpha parvalbumin. The method involves simultaneous (global) least-squares analysis of titrations with Ca(2+), with Mg(2+), with Ca(2+) in the presence of Mg(2+), and with Ca(2+) or Mg(2+) in the presence of a competitive chelator (EDTA or EGTA). The Ca(2+) and Mg(2+) binding constants obtained for rat beta agree well with estimates obtained by flow dialysis. Although the Ca(2+) affinity of alpha S55D/E59D is too high to measure by flow dialysis, it was amenable to analysis using the ITC-based approach. The combined S55D and E59D mutations increase the Ca(2+) and Mg(2+) affinities of the mutated binding site by factors of 14 and 26, respectively. This behavior is consistent with that seen previously for the rat beta S55D variant.

Amino Acid Substitution↗
PubMed2003

A study of statistical error in isothermal titration calorimetry.

In isothermal titration calorimetry (ITC), the two main sources of random (statistical) error are associated with the extraction of the heat q from the measured temperature changes and with the delivery of metered volumes of titrant. The former leads to uncertainty that is approximately constant and the latter to uncertainty that is proportional to q. The role of these errors in the analysis of ITC data by nonlinear least squares is examined for the case of 1:1 binding, M+X right arrow over left arrow MX. The standard errors in the key parameters-the equilibrium constant Ko and the enthalpy DeltaHo-are assessed from the variance-covariance matrix computed for exactly fitting data. Monte Carlo calculations confirm that these "exact" estimates will normally suffice and show further that neglect of weights in the nonlinear fitting can result in significant loss of efficiency. The effects of the titrant volume error are strongly dependent on assumptions about the nature of this error: If it is random in the integral volume instead of the differential volume, correlated least-squares is required for proper analysis, and the parameter standard errors decrease with increasing number of titration steps rather than increase.

Calorimetry↗
PubMed1997

Thermodynamics of interaction of octyl glucoside with phosphatidylcholine vesicles: partitioning and solubilization as studied by high sensitivity titration calorimetry.

The interaction of the surfactant octyl glucoside (OG) with dimyristoylphosphatidylcholine (DMPC), dipalmitoylphosphatidylcholine (DPPC), distearoylphosphatidylcholine (DSPC), and soy bean phosphatidylcholine (soy bean PC) was studied using high-sensitivity titration calorimetry. We determined the partition coefficient of OG between water and lipid bilayers and the transfer enthalpy of the surfactant by addition of lipid vesicles to OG monomers or vice versa. Comparison with the micellization enthalpy of the surfactant gives information on differences in the hydrophobic environment of OG in a liquid-crystalline bilayer or a micelle. The average partition coefficient P in mole fraction units for x(e) approximately 0.12-0.2 decreases slightly from 4152 at 27 degrees C to 3479 at 70 degrees C for DMPC and from 4260 to 3879 for soy bean PC, respectively. The transfer enthalpy deltaH(T) of OG into lipid vesicles is positive at 27 degrees C and negative at 70 degrees C. Its temperature dependence is larger for the incorporation of OG into DMPC than into soy bean PC vesicles. It is concluded that OG in DMPC vesicles is better shielded from water than in soy bean PC vesicles or in micelles. Titration calorimetry was also used to determine the phase boundaries of the coexistence region of mixed vesicles and mixed micelles in the systems OG/DMPC, OG/DPPC, OG/DSPC, and OG/soy bean PC vesicles at 70 degrees C in the liquid-crystalline phase. DMPC and soy bean PC solubilization was also studied at 27 degrees C to investigate the effect of temperature. The effective surfactant to lipid ratios at saturation, R(e)(sat), for all PCs studied are in the range between 1.33-1.72 and the ratios at complete solubilization, R(e)(sol), are between 1.79-3.06. At 70 degrees C, the R(e)(sat) values decrease with increasing chain length of the saturated PC. The ratios depend also slightly on temperature and the degree of unsaturation of the fatty acyl chains. For the OG/soy bean PC system, the coexistence range for mixed vesicles and mixed micelles is larger than for the corresponding PCs with saturated chains.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1998

Proton induced vesicle fusion and the isothermal lalpha-->HII phase transition of lipid bilayers: a 31P-NMR and titration calorimetry study.

The proton-induced isothermal fusion of unilamellar lipid vesicles (Duzgunes et al., Biochemistry 24 (1985) 3091-3098) is compared with the lamellar (Lalpha)-->hexagonal (HII) phase transition of multilamellar lipid dispersions. Both lipid systems are composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) and oleic acid (OA) at a 7:3 molar ratio. Using solid-state phosphorus-31 nuclear magnetic resonance (31P-NMR) it is demonstrated that the multilamellar lipid dispersions are in the bilayer state at physiological pH and undergo a Lalpha-->HII phase transition between pH 6.3 and 5.7. This phase transition can also be induced at constant pH by increasing the temperature. The midpoint of the temperature-induced Lalpha-->HII transition is Th=56 degrees C (at pH 7.4) and the corresponding transition enthalpy is DeltaH=0. 7+/-0.1 kcal/mol as determined with differential scanning calorimetry. Both the proton-induced and the temperature-induced phase transition can be completely inhibited by addition of 30 mol% of 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine (LPC). In a second set of experiments unilamellar vesicles are prepared either by sonication or by extrusion through polycarbonate filters at pH 7. 4 and are titrated into buffer at pH 5.7. The proton-induced fusion of the lipid vesicles is monitored with isothermal titration calorimetry, light scattering and fluorescence spectroscopy. The fusion reaction is characterized by an endothermic enthalpy of DeltaH=0.5+/-0.2 kcal/mol (at 28 degrees C). The fusion enthalpy is independent of the vesicle diameter and is only slightly reduced by an increase in temperature to 50 degrees C. Vesicle fusion is accompanied by an increase in light scattering, indicating the formation of larger lipid structures. The transition from unilamellar vesicles to fused lipid structures occurs in the same narrow pH range of 6.3-5.7 as observed for the Lalpha-->HII transition of multilamellar dispersions. Vesicle fusion can be inhibited with 30% LPC. The virtually identical set of parameters found for the Lalpha-->HII phase transition and the vesicle fusion reaction suggests that vesicle fusion also entails a Lalpha-->HII phase transition.

Calorimetry↗
PubMed1995

Modified spectrophotometer for multi-dimensional circular dichroism/fluorescence data acquisition in titration experiments: application to the pH and guanidine-HCI induced unfolding of apomyoglobin.

In a previous paper (Ramsay and Eftink, Biophys. J. 66:516-523) we reported the development of a modified spectrophotometer that can make nearly simultaneous circular dichroism (CD) and fluorescence measurements. This arrangement allows multiple data sets to be collected during a single experiment, resulting in a saving of time and material, and improved correlation between the different types of measurements. The usefulness of the instrument was shown by thermal melting experiments on several different protein systems. This CD/fluorometer spectrophotometer has been further modified by interfacing with a syringe pump and a pH meter. This arrangement allows ligand, pH, and chemical denaturation titration experiments to be performed while monitoring changes in the sample's CD, absorbance, fluorescence, and light scattering properties. Our data acquisition program also has an ability to check whether the signals have approached equilibrium before the data is recorded. For performing pH titrations we have developed a procedure which uses the signal from a pH meter in a feedback circuit in order to collect data at evenly spaced pH intervals. We demonstrate the use of this instrument with studies of the unfolding of sperm whale apomyoglobin, as induced by acid pH and by the addition of guanidine-HCI.

Animals↗
PubMed1998

Membrane surface-charge titration probed by gramicidin A channel conductance.

We manipulate lipid bilayer surface charge and gauge its influence on gramicidin A channel conductance by two strategies: titration of the lipid charge through bulk solution pH and dilution of a charged lipid by neutral. Using diphytanoyl phosphatidylserine (PS) bilayers with CsCl aqueous solutions, we show that the effects of lipid charge titration on channel conductance are masked 1) by conductance saturation with Cs+ ions in the neutral pH range and 2) by increased proton concentration when the bathing solution pH is less than 3. A smeared charge model permits us to separate different contributions to the channel conductance and to introduce a new method for "bilayer pKa" determination. We use the Gouy-Chapman expression for the charged surface potential to obtain equilibria of protons and cations with lipid charges. To calculate cation concentration at the channel mouth, we compare different models for the ion distribution, exact and linearized forms of the planar Poisson-Boltzmann equation, as well as the construction of a "Gibbs dividing surface" between salt bath and charged membrane. All approximations yield the intrinsic pKain of PS lipid in 0.1 M CsCl to be in the range 2.5-3.0. By diluting PS surface charge at a fixed pH with admixed neutral diphytanoyl phosphatidylcholine (PC), we obtain a conductance decrease in magnitude greater than expected from the electrostatic model. This observation is in accord with the different conductance saturation values for PS and PC lipids reported earlier (, Biochim. Biophys. Acta. 552:369-378) and verified in the present work for solvent-free membranes. In addition to electrostatic effects of surface charge, gramicidin A channel conductance is also influenced by lipid-dependent structural factors.

Gramicidin↗
PubMed1999

A "release" protocol for isothermal titration calorimetry.

Isothermal titration calorimetry (ITC) has become a standard method for investigating the binding of ligands to receptor molecules or the partitioning of solutes between water and lipid vesicles. Accordingly, solutes are mixed with membranes (or ligands with receptors), and the subsequent heats of incorporation (or binding) are measured. In this paper we derive a general formula for modeling ITC titration heats in both binding and partitioning systems that allows for the modeling of the classic incorporation or binding protocols, as well as of new protocols assessing the release of solute from previously solute-loaded vesicles (or the dissociation of ligand/receptor complexes) upon dilution. One major advantage of a simultaneous application of the incorporation/binding and release protocols is that it allows for the determination of whether a ligand is able to access the vesicle interior within the time scale of the ITC experiment. This information cannot be obtained from a classical partitioning experiment, but it must be known to determine the partition coefficient (or binding constant and stochiometry) and the transfer enthalpy. The approach is presented using the partitioning of the nonionic detergent C12EO7 to palmitoyloleoylphosphatidylcholine vesicles. The release protocol could also be advantageous in the case of receptors that are more stable in the ligand-saturated rather than the ligand-depleted state.

Biophysical Phenomena↗
PubMed1998

CD-monitored redox titration of the Rieske Fe-S protein of Rhodobacter sphaeroides: pH dependence of the midpoint potential in isolated bc1 complex and in membranes.

The redox potential of the Rieske Fe-S protein has been investigated using circular dichroism (CD)-spectroscopy. The CD features characteristic of the purified bc1 complex and membranes of Rhodobacter sphaeroides were found in the region between 450 and 550 nm. The difference between reduced and oxidized CD-spectra shows a negative band at about 500 nm with a half of width 30 nm that corresponds to the specific dichroic absorption of the reduced Rieske protein (Fee, J.A. et al. (1984) J. Biol. Chem. 259, 124-133; Degli Esposti, M. et al. (1987) Biochem. J. 241, 285-290; Rich, P.R. and Wiggins, T.E. (1992) Biochem. Soc. Trans. 20, 241S). It was found that the redox potential at pH 7.0 for the Rieske center in the isolated bc1 complex and in chromatophore membranes from the R-26 strain of Rh. sphaeroides is 300 +/- 5 mV. In chromatophores from the BC17C strain of Rh. sphaeroides, the Em value measured for the Rieske iron-sulfur protein (ISP) was higher (315 +/- 5 mV), but the presence of carotenoids made measurement less accurate. The Em varied with pH in the range above pH 7, and the pH dependence was well fit either by one pK at approximately 7.5 in the range of titration, or by two pK values, pK1 = 7.6 and pK2 = 9.8. Similar titrations and pK values were found for the Rieske Fe-S protein in the isolated bc1 complex and membranes from the R-26 strain of Rb. sphaeroides. The results are discussed in the context of the mechanism of quinol oxidation by the bc1 complex, and the role of the iron sulfur protein in formation of a reaction complex at the Qo-site.

Cell Membrane↗
PubMed2001

Isothermal titration calorimetry in drug discovery.

Isothermal titration calorimetry (ITC) follows the heat change when a test compound binds to a target protein. It allows precise measurement of affinity. The method is direct, making interpretation facile, because there is no requirement for competing molecules. Titration in the presence of other ligands rapidly provides information on the mechanism of action of the test compound, identifying the intermolecular complexes that are relevant for structure-based design. Calorimetry allows measurement of stoichiometry and so evaluation of the proportion of the sample that is functional. ITC can characterize protein fragments and catalytically inactive mutant enzymes. It is the only technique which directly measures the enthalpy of binding (delta H degree). Interpretation of delta H degree and its temperature dependence (delta Cp) is usually qualitative, not quantitative. This is because of complicated contributions from linked equilibria and a single change in structure giving modification of several physicochemical properties. Measured delta H degree values allow characterization of proton movement linked to the association of protein and ligand, giving information on the ionization of groups involved in binding. Biochemical systems characteristically exhibit enthalpy-entropy compensation where increased bonding is offset by an entropic penalty, reducing the magnitude of change in affinity. This also causes a lack of correlation between the free energy of binding (delta G degree) and delta H degree. When characterizing structure-activity relationships (SAR), most groups involved in binding can be detected as contributing to delta H degree, but not to affinity. Large enthalpy changes may reflect a modified binding mode, or protein conformation changes. Thus, delta H degree values may highlight a potential discontinuity in SAR, so that experimental structural data are likely to be particularly valuable in molecular design.

Animals↗
PubMed1983

[Comparison of 4 technics for serologic titration of antibodies against rabies virus in dogs].

Four different serological techniques were used for the determination of antibody levels against rabies virus in 55 vaccinated street dogs: mouse neutralization test (reference), rapid fluorescent focus inhibition test, plaque reduction test and immunoenzymatic test (protein A). The results obtained with each of the last three methods were compared with those obtained with the reference test: correlation coefficients were, respectively, 0.810, 0.812 and 0.682, each being significantly correlated with the others. Therefore the three techniques may each be recommended as an alternative to the mouse neutralization test for routine titrations; the immunoenzymatic method, which titrates not only neutralizing antibodies being, nevertheless, better used as a screening test.

Animals↗
PubMed1984

The titration of tetanus antitoxin II. A comparative evaluation of the indirect haemagglutination and toxin neutralization tests.

Serum samples from 77 guinea pigs immunized against tetanus have been titrated for tetanus antitoxin by a standardized indirect haemagglutination (IHA) test and the conventional toxin neutralization (TN) test. These sera were titrated before and after treatment of the sera with 2-mercaptoethanol (2-ME) by the IHA test using unfixed sheep erythrocytes and erythrocytes fixed with glutaraldehyde, formaldehyde and pyruvic aldehyde. The titres of these sera obtained by IHA using unfixed and glutaraldehyde-fixed sheep erythrocytes before treatment of the sera with 2-ME were two to six times higher than the TN titres, whereas the IHA-titres using formaldehyde- and pyruvic aldehyde-fixed sheep erythrocytes were 10 times higher than the TN titres in some of the sera. There was no statistically significant difference between TN and IHA titres using unfixed and glutaraldehyde-fixed sheep erythrocytes after the treatment of the sera with 2-ME.

Animals↗
PubMed1997

Titration calorimetry study of an anti-idiotypic antibody cascade in a human melanoma-associated antigen system.

The thermodynamic parameters of interactions between six variants of the anti-idiotypic monoclonal antibody (mAb) CGP 60686 produced by the hybridoma MK2-23 with an idiotypic mAb and five different anti-anti-idiotypic mAb were studied with high sensitivity titration calorimetry. CGP 60686 recognizes an epitope in the antigen-combining region of the human high-molecular-weight-melanoma-associated antigen (HMW-MAA)-specific mouse mAb CGP 76873 produced by the hybridoma 763.74. The five HMW-MAA-specific anti-anti-idiotypic mAbs GH 464, GH 518, GH 149, GH 386 and GH 586 were generated from mice immunization with mAb CGP 60686. All interactions between the anti-idiotypic mAb and the idiotypic mAb or the anti-anti-idiotypic mAb showed large exothermic binding enthalpies between -15 and -23 kcal/mol and binding affinities larger than 6 x 10(9) M-1. Four of the five anti-anti-idiotypic mAbs tested exhibited significantly higher binding enthalpies for the interaction with the anti-idiotypic than the idiotypic mAbs. Replacement of either the heavy or the light chain variable region of the anti-idiotypic mAbs with an unrelated variable region abolished the idiotype to anti-idiotype interaction. Thus, both the heavy and the light chain variable region of the anti-idiotypic mAbs are required for binding to the idiotype. The values of the binding enthalpy showed only small variations when binding of the idiotypic mAb CGP 76873 to four variants of the anti-idiotypic mAb CGP 60686 with different immunoglobulin constant regions, but identical variable regions were compared. Furthermore, Fab fragments of the idiotypic mAbs showed almost the same binding enthalpy per binding site as the whole IgG molecules. Immunoglobulin constant regions thus had little influence on the idiotype to anti-idiotype interactions. Taken together, the observed thermodynamic parameters suggest that the idiotype to anti-idiotype interactions studied here are enthalpy-driven processes with only minor entropic contributions. High sensitivity titration calorimetry was used to monitor protein-protein interactions within an anti-idiotypic antibody cascade. It was found that the direct measurement of the interaction enthalpy allowed a quantitative characterization of the binding processes studied.

Animals↗
PubMed2002

Aqueous and solid complexes of iron(III) with hyaluronic acid. Potentiometric titrations and infrared spectroscopy studies.

The coordination of iron(III) ion to hyaluronic acid (Hyal) in aqueous solutions and solid state was accomplished by potentiometric titrations and infrared spectroscopy. The potentiometric titration studies provided the binding constants for the complexes found in the systems and the speciation of these species according to the variation of pH values. The complexes found presented a complexing ability through both the chelating moieties of Hyal (via the N-glucosamine and D-glucoronic acid), showing no special preference for either one while in solid state, but when in aqueous solution the complexation via the N-glucosamine moiety was the preferred, forming two complexed species, ML and ML(2) (log K(ML)=8.2 and log K(ML2)=7.9). The presence of a mu-oxo complex via the D-glucoronic acid was also detected in both aqueous (log K=6.7) and solid states via the N-glucosamine and D-glucoronic acid simultaneously linked to two Hyal chains. A structure for this latter complex was suggested. The results indicated that these complexes could be used in eliminating the excess iron(III) in living organisms.

Carbohydrate Conformation↗
PubMed1999

Synthesis, potentiometric titration, electrochemical investigation and biological properties of trans-[RuCl2(dinic)4] (dinic = 3,5-pyridinecarboxylic acid).

This work discusses both the synthesis of trans-[RuCl2(dinic)4], dinic = 3,5-pyridinecarboxylic acid, and its main characteristics including potentiometric titration, spectroscopic and electrochemical properties, and some biological properties. The complex was synthesized using ruthenium blue solution as the precursor in a synthetic route. The complex was characterized using electronic spectroscopy, vibrational FT-IR spectroscopy, and Raman spectroscopy, as well as 1H and 13C NMR. The results indicated that the complex exhibits a trans-geometry. Cyclic voltammetry carried out in water:acetone 1:1 solution revealed a quasi-reversible process centered on the Ru(II) atom, as well as a dependence of the redox potential, E1/2, on pH. An analysis of the electronic spectra revealed that the MLCT (metal ligand charge transfer) band underwent a hypsochromic shift as the pH increased. Spectroelectrochemical analysis indicated that the visible region band progressively faded out upon oxidation. The equilibrium constants for the eight protons of the complex were determined by potentiometric titration. The complex neither inhibits the activity of nitrogen monoxide synthase nor acts as a scavenger for nitrogen monoxide. Nevertheless, the complex shows antinociceptive properties and acts as a scavenger for hydroxyl radicals.

Analgesics↗