Holding a Master's degree in Structural Biology and Genomics from Aix-Marseille University and boasting expertise in structural biochemistry, I am proficient in protein molecular modeling, docking, and protein interaction analysis techniques. These skills allow me to study in depth the molecular mechanisms involved in neurodegenerative diseases and to contribute to the design of new therapeutic strategies.
I am currently a doctoral candidate in Structural Biochemistry, and my thesis topic is: Role of Tau phosphorylations in its binding to microtubules and tubulin.
My research focuses on the role of Tau protein phosphorylations in its binding to microtubules, a crucial aspect in understanding and treating Alzheimer's disease. Alzheimer's disease is characterized by the accumulation of hyperphosphorylated Tau protein deposits, leading to neuronal death. I am particularly interested in the AT8 epitope of Tau, whose phosphorylation is correlated with the stages of the disease. My work aims to determine how phosphorylations, especially that of Serine 208, affect the interaction of Tau with microtubules and its ability to stabilize them. The objective is to propose new therapeutic strategies targeting these phosphorylations.
My research approach combines structural biochemistry techniques with advanced biophysical methods such as dynamic light scattering (DLS), analytical ultracentrifugation (AUC), and electron microscopy. This combination allows me to analyze not only the structure of proteins but also their dynamics and interactions in a broader context.