[Expired] Strasbourg. PhD Thesis in Bio-(inorganic) Chemistry on: Self-Assembly and Metal-binding of the Amyloid-beta Peptide
Biometals and Biological Chemistry Group
Institut de Chimie (UMR 7177) Strasbourg (France)
dead-line: May 20th
There is a large body of evidence from In vivo, in cellulo and in vitro experiments that metal ions (mostly Cu, Zn and Fe) play an important role in the development of Alzheimer’s disease (AD). Cu and Zn ions are found in high concentration in the amyloid plaques, a hallmark of AD. These metal ions are bound to the peptide called amyloid-beta (Aβ), which is the major component of these plaques and are present in an aggregated form. Metal ions were reported to intervene in two key processes of Alzheimer’s disease: the aggregation of the peptide amyloid-β (Aβ) (mainly Cu and Zn) and the production of reactive oxygen species (ROS) (for Cu and Fe). Compounds that counteract the metal imbalance were reported to be a promising therapeutical approach. The objective of the project is to elucidate the role of metal ions in the aggregation of Aβ. We plan to generate Aβ peptides labeled by different fluorophores in order to probe metal-binding, aggregation and interaction with different metalloproteins in the full-length Aβ under biologically relevant conditions.
Chemical and biochemical methods; spectroscopy (NMR, fluorescence, FTIR, etc), microscopy (AFM, TEM), chromatography; electrophoreses; cell culture and fluorescence microscopy
biometals; bioinorganic chemistry; copper, zinc; reactive oxygen species, self-assembly; amyloids; metal trafficking; fluorophores; spectroscopies.
Recent reviews of the group:
- Nasica-Labouze J, et al. Chem Rev. 2015, 115, 3518-63.
- Faller P, et al. Acc Chem Res. 2014, 47,2252-9.
Expires on Monday May 30th, 2016