Complexes of doubly chelating ligands. Part III. Proton and copper(II) complexes of 3,4-dihydroxyphenylglycine (DOPG)

Gorton, J. E.; Jameson, R. F.

doi:10.1039/dt9720000307

Cited by 9 publications

(3 citation statements)

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“…Since the intensity of the interactions between the carboxylate groups of the amino acids (Figure S10, Supporting Information) is decreased in the presence of MgCl 2 , our results do not support the presence of complexes of the type proposed by Tian et al Though a clear description of the structure of amino acid–magnesium complexes cannot be found in literature and the data obtained in this work does not either allow to properly infer the molecular nature of those species, further support for the existence of such complexes can be provided by several studies. In fact, chelation of magnesium ions by carboxylic acids and amino acids in aqueous solutions has been considered before and the stability constants for such systems have been reported. − Moreover, the participation of the carboxyl group in the chelating reaction has been confirmed by spectroscopic methods . Other pharmaceutical and medical reports describe as well the use of preparations of magnesium–amino acid chelates as commercial products to treat human magnesium deficiency related diseases. , Those chelate forms are very soluble and are known to be one of the most bioavailable forms of magnesium…”

Section: Results and Discussionmentioning

confidence: 99%

Salting-in with a Salting-out Agent: Explaining the Cation Specific Effects on the Aqueous Solubility of Amino Acids

et al. 2013

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Although the understanding of ion specific effects on the aqueous solubilities of biomolecules is crucial for the development of many areas of biochemistry and life sciences, a consensual and well-supported molecular picture of the phenomena has not yet been established. Mostly, the influence of cations and the nature of the molecular interactions responsible for the reversal of the Hofmeister trend in aqueous solutions of amino acids and proteins are still defectively understood. Aiming at contributing to the understanding of the molecular-level mechanisms governing the cation specific effects on the aqueous solubilities of biocompounds, experimental solubility measurements and classical molecular dynamics simulations were performed for aqueous solutions of three amino acids (alanine, valine, and isoleucine), in the presence of a series of inorganic salts. The evidence gathered suggests that the mechanism by which salting-in inducing cations operate in aqueous solutions of amino acids is different from that of anions, and allows for a novel and consistent molecular description of the effect of the cation on the solubility based on specific interactions of the cations with the negatively charged moieties of the biomolecules.

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Section: Results and Discussionmentioning

confidence: 99%

Salting-in with a Salting-out Agent: Explaining the Cation Specific Effects on the Aqueous Solubility of Amino Acids

et al. 2013

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“…At BGE of pH 6.5 and voltage of −20 kV, the surface of the capillary inner wall was negatively charged so that the EOF migrated from the anodic end (injection) to cathodic end (detection). Apparent dissociation constant values of l ‐DOPA were 2.30, 8.11, 9.92, and 13.40, respectively , which the pKa of carboxyl was 2.30 and the pKa of protonated amino was 8.11. Because the pH 6.5 was <8.11, the main dissociation group of l ‐DOPA was carboxyl.…”

Section: Resultsmentioning

confidence: 99%

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Cheng

Chen

2016

Electrophoresis

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A new method for screening tyrosinase inhibitors from traditional Chinese medicines (TCMs) was successfully developed by capillary electrophoresis with reliable online immobilized enzyme microreactor (IMER). In addition, molecular docking study has been used for supporting inhibition interaction between enzyme and inhibitors. The IMER of tyrosinase was constructed at the outlet of the capillary by using glutaraldehyde as cross-linker. The parameters including enzyme reaction, separation of the substrate and product, and the performance of immobilized tyrosinase were investigated systematically. Because of using short-end injection procedure, the product and substrate were effectively separated within 2 min. The immobilized tyrosinase could remain 80% active for 30 days at 4°C. The Michaelis-Menten constant of tyrosinase was determined as 1.78 mM. Kojic acid, a known tyrosinase inhibitor, was used as a model compound for the validation of the inhibitors screening method. The half-maximal inhibitory concentration of kojic acid was 5.55 μM. The method was successfully applied for screening tyrosinase inhibitors from 15 compounds of TCM. Four compounds including quercetin, kaempferol, bavachinin, and bakuchiol were found having inhibitory potentials. The results obtained in this work were supported by molecular docking study.

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“…For example, the operations of neurotransmitters are distorted if they react with heavy metals such as Pb, Hg, or lanthanides that frequently act as hard acids. The coordination chemistry of these compounds is complicated by their ability to act as ambidentate or bridging ligands. , …”

Section: Introductionmentioning

confidence: 99%

Thermodynamic Complexation of Dopamine with Molybdenum(VI) in Media with Different Dielectric Constants

Bagheri

2009

J. Chem. Eng. Data

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The complexation of Mo(VI) with dopamine has been investigated by spectrophotometric measurements in a mixed solvent system at an ionic strength of 0.2 mol • dm -3 sodium chloride, employed [(15, 25, or 35 ( 0.1) °C] at pH ranges of ∼4 to ∼7 with a high ratio of ligand to metal. The effect of solvent systems on protonation and complexation are discussed. Linear relationships are observed by plotting log K versus 1/D, where K and D are the stability and dielectric constants, respectively.

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Complexes of doubly chelating ligands. Part III. Proton and copper(II) complexes of 3,4-dihydroxyphenylglycine (DOPG)

Cited by 9 publications

References 0 publications

Salting-in with a Salting-out Agent: Explaining the Cation Specific Effects on the Aqueous Solubility of Amino Acids

Salting-in with a Salting-out Agent: Explaining the Cation Specific Effects on the Aqueous Solubility of Amino Acids

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Thermodynamic Complexation of Dopamine with Molybdenum(VI) in Media with Different Dielectric Constants

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