| Titre : |
Towards new bioinorganic hybrid catalysts based on amyloid fibres |
| Type de document : |
texte imprimé |
| Auteurs : |
Marie Hoarau, Auteur ; Gras, Emmanuel, Directeur de thèse ; Magali Remaud-Siméon, Directeur de thèse |
| Langues : |
Anglais (eng) |
| Tags : |
FIBRES AMYLOIDES COMPLEXES DE COORDINATION CATALYSEURS HYBRIDES CHIMIE BIO-INORGANIQUE |
| Résumé : |
"Developing sustainable alternatives to catalytic systems developed to date is a key point of the
Green Chemistry Principles. Among the different existing approaches, the artificial metalloenzyme
strategy aims at combining the efficiency of enzymes with the versatility of chemical catalysts. In this
context, we turned our interest in developing a new type of bioinorganic hybrid catalysts through
incorporation of coordination complexes in amyloid fibres. These protein aggregates display
unique mechanical properties that make them good candidates for applications in catalysis.
In a first part, our work consisted in overexpressing amyloid-? peptides in Escherichia coli.
A new purification procedure was set up that allowed to obtain peptides in a few steps. A series of
organic ligands was synthesized, as well as the corresponding Cu(II), Fe(II) and Ru(II) complexes.
The interaction between amyloid fibres and metal complexes was assessed, using a set of
techniques (UV-Visible, Fluorescence, NMR…). Docking studies were also conducted by molecular
modelling to acquire further insights in the interaction.
Finally, catalytic experiments were performed with Fe(II) complexes, showing high
conversion rates for styrene oxidation reaction. Preliminary results on the final hybrid systems show
that the catalytic activity of metal complexes is maintained upon incorporation within fibres. This
constitutes a proof of concept for the elaboration of hybrid catalysts based on amyloid fibres." |
| Document : |
Thèse de Doctorat |
| Etablissement_delivrance : |
Université Toulouse 3 |
| Date_soutenance : |
03/11/2016 |
| Ecole_doctorale : |
Sciences de la matière (SdM) |
| Domaine : |
Chimie Biologie Santé |
| En ligne : |
http://thesesups.ups-tlse.fr/3579/ |
Towards new bioinorganic hybrid catalysts based on amyloid fibres [texte imprimé] / Marie Hoarau, Auteur ; Gras, Emmanuel, Directeur de thèse ; Magali Remaud-Siméon, Directeur de thèse . - [s.d.]. Langues : Anglais ( eng)
| Tags : |
FIBRES AMYLOIDES COMPLEXES DE COORDINATION CATALYSEURS HYBRIDES CHIMIE BIO-INORGANIQUE |
| Résumé : |
"Developing sustainable alternatives to catalytic systems developed to date is a key point of the
Green Chemistry Principles. Among the different existing approaches, the artificial metalloenzyme
strategy aims at combining the efficiency of enzymes with the versatility of chemical catalysts. In this
context, we turned our interest in developing a new type of bioinorganic hybrid catalysts through
incorporation of coordination complexes in amyloid fibres. These protein aggregates display
unique mechanical properties that make them good candidates for applications in catalysis.
In a first part, our work consisted in overexpressing amyloid-? peptides in Escherichia coli.
A new purification procedure was set up that allowed to obtain peptides in a few steps. A series of
organic ligands was synthesized, as well as the corresponding Cu(II), Fe(II) and Ru(II) complexes.
The interaction between amyloid fibres and metal complexes was assessed, using a set of
techniques (UV-Visible, Fluorescence, NMR…). Docking studies were also conducted by molecular
modelling to acquire further insights in the interaction.
Finally, catalytic experiments were performed with Fe(II) complexes, showing high
conversion rates for styrene oxidation reaction. Preliminary results on the final hybrid systems show
that the catalytic activity of metal complexes is maintained upon incorporation within fibres. This
constitutes a proof of concept for the elaboration of hybrid catalysts based on amyloid fibres." |
| Document : |
Thèse de Doctorat |
| Etablissement_delivrance : |
Université Toulouse 3 |
| Date_soutenance : |
03/11/2016 |
| Ecole_doctorale : |
Sciences de la matière (SdM) |
| Domaine : |
Chimie Biologie Santé |
| En ligne : |
http://thesesups.ups-tlse.fr/3579/ |
|  |
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