The Thermodynamic and pH Metric Binding Studies of Cu+2 Ions with Egg Protein by Spectrometric and Diffusion Current Techniques

2020 ◽  
Vol 234 (3) ◽  
pp. 441-460 ◽  
Author(s):  
Shveta Acharya ◽  
Arun Kumar Sharma
Keyword(s):  
Metal Ion ◽  
Copper Ions ◽  
Protein Molecule ◽  
Living System ◽  
Diffusion Current ◽  
Binding Studies ◽  
Spectrophotometric Methods ◽  
Egg Protein ◽  
Physico Chemical ◽  
Lower Temperature

AbstractTransition metals have unique efficacy in catalyzing various industrial reactions and also in living system, the redox reaction and redox changes in the metal ions catalyzed valence changes in the substrate molecule. The survey of the existing literature revealed that the binding of Molybdenum, Vanadium, Zinc, Cadmium, Copper, Nickel and Cobalt with the protein is well known but no binding studies of copper metal with egg protein are reported. With a view to extend the existing knowledge of ecological nature of metal-protein system, it was thought of interest to investigate the properties of metal-protein mixture. Investigations on the aspects of these binding problems were planned and their bindings constants have been determined using suitable physico-chemical methods. The pH metric, diffusion current measurements, spectrophotometric methods have been used on the binding of copper ions with albumin. The effect of physico-chemical factors on interaction between divalent metal ion i.e. copper with albumin has been discussed. On the basis of observed results, it is found that the binding data were dependent on pH and temperature. From scatchard plots, the intrinsic association constants (k) and the number of binding sites (n) were calculated and found high at lower pH and temperatures. Therefore, a lower temperature and lower pH offered more sites in the protein molecule for interaction with copper (II) ions. The enthalpy (ΔH), entropy (ΔS) changes, free energy change (ΔG°) have been calculated.

The Thermodynamic and Binding Studies of Hg+2 Ions with Egg Protein by Polarographic and pH Metric Techniques

2019 ◽  
Vol 233 (8) ◽  
pp. 1073-1090 ◽  
Author(s):  
Shveta Acharya ◽  
Arun Kumar Sharma
Keyword(s):  
Protein Molecule ◽  
Binding Studies ◽  
Temperature Dependent ◽  
Ph Values ◽  
Egg Protein ◽  
Binding Data ◽  
Number Of Binding Sites ◽  
Lower Temperature ◽  
Scatchard Plots ◽  
Statistical Effects

AbstractThe binding of mercury (II) ion has been studied with egg protein at different pH values and temperatures by the polarographic technique. The binding data were found to be pH and temperature dependent. The intrinsic association constants (k) and the number of binding sites (n) were calculated from Scatchard plots and found tobe at the maximum at lower pH and at lower temperatures. The free energy change (ΔG°) of the combining sites were least at the higher pH and highest at the low pH; therefore, a lower temperature and lower pH offered more sites in the protein molecule for interaction with mercury (II) ions. Statistical effects seem to be more significant at lower mercury (II) ion concentrations, while at higher concentrations electrostatic effects and heterogeneity of sites are more significant.

The Binding and Viscometric Studies of Ni+2, Co+2 and Mn+2 Ions with Protein by Spectrometric and pH Metric Techniques

2019 ◽  
Vol 9 (2) ◽  
pp. 151-162
Author(s):  
Shveta Acharya ◽  
Arun Kumar Sharma
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Protein Molecule ◽  
Vital Role ◽  
Sufficient Evidence ◽  
Structural Requirement ◽  
Nickel Ions ◽  
Cobalt Ions ◽  
Lower Temperature ◽  
Specific Oxidation

Background: The metal ions play a vital role in a large number of widely differing biological processes. Some of these processes are quite specific in their metal ion requirements. In that only certain metal ions, in specific oxidation states, can full fill the necessary catalytic or structural requirement, while other processes are much less specific. Objective: In this paper we report the binding of Mn (II), Ni (II) and Co (II) with albumin are reported employing spectrophotometric and pH metric method. In order to distinguish between ionic and colloidal linking, the binding of metal by using pH metric and viscometric methods and the result are discussed in terms of electrovalent and coordinate bonding. Methods: The binding of Ni+2, Co+2 and Mn+2 ions have been studied with egg protein at different pH values and temperatures by the spectrometric technique. Results: The binding data were found to be pH and temperature dependent. The intrinsic association constants (k) and the number of binding sites (n) were calculated from Scatchard plots and found to be at the maximum at lower pH and at lower temperatures. Therefore, a lower temperature and lower pH offered more sites in the protein molecule for interaction with these metal ions. Statistical effects seem to be more significant at lower Ni+2, Co+2 and Mn+2 ions concentrations, while at higher concentrations electrostatic effects and heterogeneity of sites are more significant. Conclusion: The pH metric as well as viscometric data provided sufficient evidence about the linking of cobalt, nickel and manganese ions with the nitrogen groups of albumin. From the nature and height of curves in the three cases it may be concluded that nickel ions bound strongly while the cobalt ions bound weakly.

scholarly journals MITIGATION OF METAL ION POLLUTION FROM INDUSTRIAL WASTE WATER USING WASTE WOOL

2013 ◽  
Vol 22 ◽  
pp. 619-625 ◽  
Author(s):  
GARIMA PRAJAPAT ◽  
PRAVEEN PUROHIT
Keyword(s):  
Waste Water ◽  
Industrial Waste ◽  
Metal Ion ◽  
Copper Ions ◽  
Industrial Effluents ◽  
Composite Ceramic ◽  
Industrial Waste Water ◽  
Spectrophotometric Methods ◽  
Fixed Weight ◽  
Removal Of Metal Ions

A study on the adsorption of copper (II) ions from the aqueous solution on waste wool had been carried out to analyze the adsorption capacity of waste wool, thereby aiming towards mitigation of metal ion pollution in industrial waste water. The effect of varying concentration of copper ions and varying time period, was studied on fixed weight of waste wool. The initial and final concentration of copper ions was measured by conductometric and spectrophotometric methods. Adsorption data were modeled with the langmuir and freundlich adsorption isotherms. The isotherm and first order equation were found to be applicable. Removal of metal ions using industrial waste wool is found to be favourable. Thus the work can be extended to study various physico-chemical parameters for removal of copper (II) ions from industrial effluents using waste wool. A later work can be involved where the waste wool adsorption parameter can be further utilized for composite ceramic products.

Spectrometric, Thermodynamic, pH Metric and Viscometric Studies on the Binding of TEALS as Surfactant with Albumin as Biopolymer

2020 ◽  
Vol 10 (1) ◽  
pp. 47-64
Author(s):  
Shveta Acharya ◽  
Arun Kumar Sharma
Keyword(s):  
Binding Sites ◽  
Equilibrium Dialysis ◽  
Protein Molecule ◽  
Structure Characterization ◽  
Binding Interaction ◽  
Practical Applications ◽  
Egg Protein ◽  
Binding Data ◽  
Number Of Binding Sites ◽  
Lower Temperature

Background:: Since the interactions of small anions with protein are very important in their transportation and distribution processes in biological systems, it is helpful to study these interactions to understand the nature of the transportation and distribution processes. Therefore, it is aimed to study the interaction of albumin with surfactant molecule by different physical methods. Objective:: Present work attempts to work on assessing the structure, characterization of the surfactants as TEALS (tri-ethanalamine lauryl sulphate) binding sites, with albumin involved in various process of living being are discussed. Method:: The binding of surfactant TEALS to egg protein has been studied at different pH values and temperatures by spectrophotometric and equilibrium dialysis methods. The binding data were found to be pH and temperature dependent. The binding data studied by the absorbance method, were found approximately identical with those obtained from the equilibrium dialysis method. Results:: The association constants and the number of binding sites were calculated from Scatchard plots and found to be at maximum at lower pH and at lower temperature. The free energy of the combining sites was lowest at higher pH and highest at low pH. Therefore, a lower temperature and a lower pH offered more sites in the protein molecule for interaction with surfactant. The ΔG (free energies of aggregation) associated with the binding interaction of the surfactants and protein were calculated. The negative values of the ΔG confirm the feasibility of interaction between the surfactant and protein. All the observations recorded in this paper indicate that the TEALS has a good affinity of binding with egg protein and the number of binding sites is dependent on various physical and chemical factors. Conclusion:: On the basis of the results of the experiments which were conducted to examine the interaction between anionic surfactant and protein by measuring the various parameters of the solutions, it is concluded that the interaction of surfactant and protein gives an idea of fundamental understanding of the structure of surfactant-protein complex and their practical applications in every field.

scholarly journals Solvent-Induced Hysteresis Loop in Anionic Spin Crossover (SCO) Isomorph Complexes

2021 ◽  
Vol 7 (6) ◽  
pp. 75
Author(s):  
Emmelyne Cuza ◽  
Samia Benmansour ◽  
Nathalie Cosquer ◽  
Françoise Conan ◽  
Carlos J. Gómez-García ◽  
...  
Keyword(s):  
Metal Ion ◽  
Spin Crossover ◽  
Magnetic Behaviour ◽  
Magnetic Studies ◽  
Tridentate Ligands ◽  
Tripodal Ligand ◽  
Single Crystal Structures ◽  
One Step ◽  
Lower Temperature ◽  
Step Transition

Reaction of Fe(II) with the tris-(pyridin-2-yl)ethoxymethane (py3C-OEt) tripodal ligand in the presence of the pseudohalide ancillary NCSe- (E = S, Se, BH3) ligand leads to the mononuclear complex [Fe(py3C-OEt)2][Fe(py3C-OEt)(NCSe)3]2·2CH3CN (3), which has been characterised as an isomorph of the two previously reported complexes, Fe(py3C-OEt)2][Fe(py3C-OEt)(NCE)3]2·2CH3CN, with E = S (1), BH3 (2). X-ray powder diffraction of the three complexes (1–3), associated with the previously reported single crystal structures of 1–2, revealed a monomeric isomorph structure for 3, formed by the spin crossover (SCO) anionic [Fe(py3C-OEt)(NCSe)3]− complex, associated with the low spin (LS) [Fe(py3C-OEt)2]2+ cationic complex and two solvent acetonitrile molecules. In the [Fe(py3C-OEt)2]2+ complex, the metal ion environment involves two py3C-OEt tridentate ligands, while the [Fe(py3C-OEt)(NCSe)3]− anion displays a hexacoordinated environment involving three N-donor atoms of one py3C-OEt ligand and three nitrogen atoms arising from the three (NCSe)− coligands. The magnetic studies for 3 performed in the temperature range 300-5-400 K, indicated the presence of a two-step SCO transition centred around 170 and 298 K, while when the sample was heated at 400 K until its complete desolvation, the magnetic behaviour of the high temperature transition (T1/2 = 298 K) shifted to a lower temperature until the two-step behaviour merged with a gradual one-step transition at ca. 216 K.

Bromine substituted aminonaphthoquinones: synthesis, characterization, DFT and metal ion binding studies

RSC Advances ◽  
2016 ◽  
Vol 6 (91) ◽  
pp. 88010-88029 ◽  
Author(s):  
Gunjan Agarwal ◽  
Dipali N. Lande ◽  
Debamitra Chakrovarty ◽  
Shridhar P. Gejji ◽  
Prajakta Gosavi-Mirkute ◽  
...  
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Bromine substituted aminonaphthoquinones – chemosensors for metal ions.

Electrochemical characterization of Cu(II) complexes of brain-related tau peptides

2021 ◽  
Vol 99 (7) ◽  
pp. 628-636
Author(s):  
Camilla Golec ◽  
Jose O. Esteves-Villanueva ◽  
Sanela Martic
Keyword(s):  
Metal Ions ◽  
Tau Protein ◽  
Metal Ion ◽  
Differential Pulse ◽  
Redox Couple ◽  
Peptide Sequence ◽  
Binding Studies ◽  
Biologically Relevant ◽  
Redox Active ◽  
Competition Binding

Metal ion dyshomeostasis plays an important role in diseases, including neurodegeneration. Tau protein is a known neurodegeneration biomarker, but its interactions with biologically relevant metal ions, such as Cu(II), are not fully understood. Herein, the Cu(II) complexes of four tau R peptides, based on the tau repeat domains, R1, R2, R3, and R4, were characterized by electrochemical methods, including cyclic voltammetry, square-wave voltammetry, and differential pulse voltammetry in solution under aerobic conditions. The current and potential associated with Cu(II)/(I) redox couple was modulated as a function of R peptide sequence and concentration. All R peptides coordinated Cu(II) resulting in a dramatic decrease in the current associated with free Cu(II), and the appearance of a new redox couple due to metallo–peptide complex. The metallo–peptide complexes were characterized by the irreversible redox couple at more positive potentials and slower electron-transfer rates compared with the free Cu(II). The competition binding studies between R peptides with Cu(II) indicated that the strongest binding affinity was observed for the R3 peptide, which contained 2 His and 1 Cys residues. The formation of complexes was also evaluated as a function of peptide concentration and in the presence of competing Zn(II) ions. Data indicate that all metallo–peptides remain redox active pointing to the potential importance of the interactions between tau protein with metal ions in a biological setting.

Cytotoxicity and Antibacterial Studies of Newly Synthesized Novel Heterocylcic Pyridine Derivative and its Metal Complexes

2021 ◽  
Vol 6 (4) ◽  
pp. 243-249
Author(s):  
B.R. Chaitanya Kumar ◽  
K. Sudhakar Babu ◽  
J. Latha
Keyword(s):  
Metal Complexes ◽  
Cell Lines ◽  
Cancer Cell ◽  
Metal Ion ◽  
Analytical Data ◽  
Cancer Cell Lines ◽  
Diffusion Method ◽  
Pyridine Derivative ◽  
Bacterial Strains ◽  
Physico Chemical

A pyridine derivative 2-((E)-1-(2-hydrazinyl-4-methyl-6-phenyl-pyridine-3-carboyl)ethyl)pyridine-4- carbonitrile (CPHPC) ligand and its 3d-metal(II) complexes has been synthesized (where [M = Co(II), Ni(II) and Cu(II)]. The physico-chemical, analytical data, UV-Vis, FT-IR, 1H NMR and ESR spectrum methods were used to characterize all of the synthesized complexes. Spectral investigations of metal(II) complexes revealed that the metal ion is surrounded by an octahedral geometry. Low conductance values indicated that the metal(II) complexes behave as non-electrolyte. The cytotoxic activity on lung cancer cell lines and hepatic cancer cell lines A549 and HepG2, respectively, with the ligand and their metal complexes were tested with MTT assay. The ligand and its metal complexes were tested for diverse harmful bacterial strains using the agar well diffusion method on Gram-negative bacteria such as Pseudomonas desmolyticum, Escherichia coli and Klebsiella aerogenes, as well as Gram-positive bacteria Staphylococcus aureus.

New Fluorescence PET Systems Based on N2S2Pyridine-Anthracene-Containing Macrocyclic Ligands. Spectrophotometric, Spectrofluorimetric, and Metal Ion Binding Studies

2005 ◽  
Vol 44 (22) ◽  
pp. 8105-8115 ◽  
Author(s):  
Abel Tamayo ◽  
Carlos Lodeiro ◽  
Lluis Escriche ◽  
Jaume Casabó ◽  
Berta Covelo ◽  
...  
Keyword(s):  
Metal Ion ◽  
Macrocyclic Ligands ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Physico-chemical characterization of Cu2+-exchanged sepiolite

Clay Minerals ◽  
1985 ◽  
Vol 20 (4) ◽  
pp. 467-475 ◽  
Author(s):  
A. Corma ◽  
J. Pérez-Pariente ◽  
J. Soria
Keyword(s):  
Chemical Characterization ◽  
Tetrahedral Symmetry ◽  
Pyramidal Geometry ◽  
Physico Chemical ◽  
One Step ◽  
Lower Temperature ◽  
Coordinated Water ◽  
Square Pyramidal Geometry ◽  
Different Levels

AbstractCopper-sepiolites exchanged at different levels have been studied by ESR, IR, and TG. The results indicate that in the unheated samples the Cu2+ ions are located in octahedral edge positions. After dehydration, the Cu2+ ions occur in two positions with different environments. Some of the Cu2+ ions lose the two molecules of coordinated water in one step, at low dehydration temperatures, and adopt a square pyramidal geometry. Other Cu2+ ions lose the coordination water in two steps, at lower temperature than the natural sepiolite, and adopt a tetrahedral symmetry.

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