| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Christine, Mousty
in Cooperation with on an Cooperation-Score of 37%
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thesis
Contribution of iron clays in the preparation of amperometric biosensors : Study of the interaction of hemoglobin with Clays and Layered Doubles Hydroxides.
Abstract
In this thesis work, we were interested in the development of electrochemical biosensors by using iron rich clays and Layered Doubles Hydroxides (LDH), as matrices for immobilizing hemoglobin (Hb). The aim of this work was to study the contribution of iron structural materials in improving the performance of biosensors by a phenomenon of redox catalysis. Hemoglobin is a metalloprotein containing iron porphyrin (heme) as prosthetic group. A preferred orientation of the biomolecule on an electrode surface may improve the direct electron transfer between the active site of the protein and the electrode. The electro-catalytic properties of immobilized Hb were studied for the reduction of hydrogen peroxide (H2O2) and, allowed the development of different amperometric biosensors. We have immobilized Hb in iron rich cationic clays (nontronite from Garfield, montmorillonites) and in a montmorillonite containing non iron as a reference. The electrochemical properties of these clays were studied by cyclic voltammetry and impedancemetry. The adsorption isotherms of Hb on these clays showed a strong affinity of Hb for nontronite. We have also shown that octahedral structural iron clays, especially nontronite, improve the direct electron transfer between Hb and electrode. Immobilization of Hb in LDH of different compositions (MgAl and ZnAl) was performed by adsorption and coprecipitation methods. We noted that iron situated in octahedral site in LDH (MgFe) is not electroactive and therefore can not improve the electro-enzymatic process. The chemical and morphological characterizations of the Hb-LDH biohybrids were carried out by several techniques, such as XRD, IR, UV, SEM and TEM. We noted a partial denaturation of the tertiary structure of the protein, due to the formation hydrogen bonds between the biomolecule and hydroxyl layers of LDH, which limits the accessibility of heme to direct electronic transfer. Besides the interactions of Hb with LDH, we was also interested in the immobilization of a negatively charged metalloporphyrin, (FeTSPP) in three different LDH: Zn2Al Mg2Al and Zn2Cr and we have starting the first electrochemical study of these materials.