Thermodynamic interactions of the alkaline earth metal ions with citric acid

Wyrzykowski, Dariusz; Czupryniak, Justyna; Ossowski, Tadeusz; Chmurzyński, Lech

doi:10.1007/s10973-010-0970-y

Cited by 36 publications

(27 citation statements)

References 29 publications

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“…It is connected with the transfer of the proton from the ligand to the buffer. Carrying out the ITC measurements in buffer solutions of equal pH but different enthalpies of proton association of its components (Mes, Caco, Pipes), DH BH , made it possible to determine the enthalpy of complex formation, independent of the nature of the buffer used [16][17][18]. Moreover, when the enthalpy of the metal-ligand (strong ligand) reaction is known, DH MNTA o , the metalbuffer (weak ligand) enthalpy can be calculated, DH MB o .…”

Section: Resultsmentioning

confidence: 99%

Investigation of metal–buffer interactions using isothermal titration calorimetry

Wyrzykowski

Pilarski²,

Jacewicz

et al. 2012

J Therm Anal Calorim

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Isothermal titration calorimetry (ITC) and potentiometric titration (PT) methods were used to study the interactions of cobalt(II) and nickel(II) ions with buffer substances 2-(N-morpholino)ethanesulfonic acid (Mes), dimethylarsenic acid (Caco), and piperazine-N,N 0 -bis (2-ethanesulfonic acid) (Pipes). Based on the results of PT data, the stability constants were calculated for the metal-buffer complexes (T = 298.15 K, ionic strength I = 100 mM NaClO 4 ). Furthermore, calorimetric measurements (ITC) were run in 100 mM Mes, Caco, and Pipes solutions with pH 6, at 298.15 K. The enthalpies (DH) of the metalbuffer complexation reactions were calculated indirectly by displacement titration using nitrilotriacetic acid (H 3 NTA) as a strong-binding, competitive ligand. Finally, to verify obtained results, the number of protons released by H 3 NTA due to complexation of the cobalt(II) and nickel(II) ions was determined from calorimetric data and compared with results of calculations.

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Section: Resultsmentioning

confidence: 99%

Investigation of metal–buffer interactions using isothermal titration calorimetry

Wyrzykowski

Pilarski²,

Jacewicz

et al. 2012

J Therm Anal Calorim

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“…7 The choice of buffer also inuenced the determination of the thermodynamic parameters associated with the interaction of alkaline metal ions with citric acid. 117 On the other hand, AMPSO and TAPSO have been described to inhibit the activity of catalysts in chemical reaction due to their capacity to bind with Cu(II), which was not a problem when HEPES was used as a buffer. 14 Nakano et al, while examining MOPSO, ACES, BES, MOPS, TES, HEPES and 3,3-dimethylglutaric acid (DGA) in an attempt to nd the optimal conditions for the determination of Mn(II) by ow-injection photometry, ultimately selected DGA, as it was the only one to present no effects on the peaks obtained up to a concentration of 1 Â 10 À2 M. 118 BTP is recognized as a strong coordinating buffer to Cu(II) 46 and should be avoided in the use of an assay for proteases, which uses a water soluble uorescein-based ligand-Cu based method.…”

Section: Hepesmentioning

confidence: 99%

(Un)suitability of the use of pH buffers in biological, biochemical and environmental studies and their interaction with metal ions – a review

et al. 2015

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The use of buffers to maintain the pH within a desired range is a very common practice in chemical, biochemical and biological studies.Among them, zwitterionic N-substituted aminosulfonic acids, usually known as Good'sbuffers, although widely used, can complex metals and interact with biological systems. The present work reviews, discusses and updates the metal complexation characteristics of thirty one commercially available buffers. In addition, their impact on biological systems is also presented. The influences of these buffers on the results obtained in biological, biochemical and environmental studies, with special focus on their interaction with metal ions, are highlighted and critically reviewed. Using chemical speciation simulations, based on the current knowledge of the metal-buffer stability constants, a proposal of the most adequate buffer to employ for a given metal ion is presented.

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“…The reference cell contained the distilled water. All details of the measuring devices and the experimental set-up were described previously [17][18][19]. All reagents were dissolved directly into 50 mM buffer solution of HEPES or Tricine of pH 8.0, containing 20 mM CaCl 2 .…”

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

Interactions between trypsin and its peptidic inhibitors studied by isothermal titration calorimetry (ITC)

Dębowski

Wyrzykowski

Lubos

et al. 2015

J Therm Anal Calorim

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Isothermal titration calorimetry (ITC) technique was used to study the interactions of trypsin with bicyclic sunflower-derived trypsin inhibitor (SFTI-1) as well as with its new monocyclic (with disulphide bridge only) analogues (C 3 H 5 O)-SFTI-1 and (C 8 H 15 O)-SFTI-1. ITC measurements were run in 50 mM buffer solution of HEPES or Tricine of pH 8, containing 20 mM CaCl 2 at 298.15 K. Based on calorimetric data, the equilibrium constants for the inhibitor-enzyme-binding processes, K, the binding stoichiometry, N (inhibitor-to-enzyme molar ratio), as well as thermodynamic parameters (DG, DH, DS) for the reactions were determined. The study revealed that the stoichiometry of the resulting complexes equals 1:1. The negative binding enthalpy (D ITC H) and favourable entropy factor (TD ITC S) suggest an important contribution of hydrogen bonding as well as hydrophobic interactions to the inhibitor-enzyme affinity. Furthermore, the relationship between the modification of the peptide structure, the experimental conditions and the thermodynamic parameters has been discussed.

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Thermodynamic interactions of the alkaline earth metal ions with citric acid

Cited by 36 publications

References 29 publications

Investigation of metal–buffer interactions using isothermal titration calorimetry

Investigation of metal–buffer interactions using isothermal titration calorimetry

(Un)suitability of the use of pH buffers in biological, biochemical and environmental studies and their interaction with metal ions – a review

Interactions between trypsin and its peptidic inhibitors studied by isothermal titration calorimetry (ITC)

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