amyloid peptides and lipoprotein structure

Lipid – protein modeling in apoliporotein

Human apolipoprotein E (apoE) stabilizes lipoprotein particles and plays an important role in regulating cholesterol homeostasis. A lipid-binding induced conformational change in the N-terminal domain is essential for apoE to serve as a ligand for the low-density lipoprotein receptor (LDLR). We performed and analyzed Molecular dynamics (MD) simulations starting from mass spectrometry cross-linking experiments to explore the conformational transitions of apoE.



Amyloid β  interaction with the lipid bilayer

The amyloid β peptide responsible for Alzheimer disease is an amphipathic peptide which interacts with the lipid membrane. This interaction contributes to the peptide high toxicity. So far little is known on this interaction. We characterized this interaction with our dedicated techniques (western blot, fluorescence, FTIR et AFM) as a function of lipid composition and oligomeric state. We now validated a unique marker of the oligomeric structure which is believed to be the most toxic one, not present in the fibrils.