“Bio-inorganic chemistry: From mimicking metalloenzymes to Cu chelation therapy.”
Dr Charlène Esmieu
LCC, équipe F
Email: charlene.esmieu(at)lcc-toulouse.fr
The presentation will be centered on bio-inorganic chemistry focusing on iron and copper ions found either in metalloenzyme or bound to amyloidogenic peptides in the human brain.
In a first part, results from my PhD thesis and postdoc on bio-inspired approach to molecular catalyst design will be presented. Metalloenzymes are catalyst that perform specific functions with high selectivity and efficiency containing actives sites with intricate structures.
The complexity of these macromolecules complicates the study of their function and the understanding of the properties that give rise to their amazing reactivity. One approach elaborated to understand, and ultimately reproduce the activity of these metalloproteins, is the study of synthetic models reproducing one or more aspects of the native metalloproteins. I will present bio-inspired routes that we followed to mimic the active site of two different enzymes, the nitrous oxide reductase and the [FeFe] hydrogenase.
The second part of my presentation will be dedicated to the chelation therapy in the context of Alzheimer disease (AD). Significant results obtained within the ALAMBIC team will be presented with a focus on the Cu(I) coordination. In the Alzheimer’s brain deposits of amyloid-beta (Aβ) peptides rich in transition metal ions are found and called senile plaques.
Redox active metal ions such as copper are able to catalyze the production of reactive oxygen species (ROS) when bound to Aβ. Removing these harmful copper ions from Aβ to exogeneous ligands would hamper the ROS production and be extremely beneficial for the AD brains.
