More than 20 human diseases, including Alzheimer's disease, Type II diabetes, prion diseases, and dialysis-related amyloidosis, are associated with the pathological self-assembly of soluble proteins into cytotoxic oligomers and amyloid fibrils. Although the proteins share very little sequence identity and structure similarity in solution, x-ray diffraction data show that all fibrils contain a common cross beta-sheet structure with beta-strands perpendicular to the fibril axis，suggesting a common aggregation mechanism for all amyloidogenic proteins. The study of peptide aggregation in solution and on surface (i.e. membrane and nanoparticles) is important for understanding the molecular mechanism of protein aggregation. This will also be helpful for rational design of improved therapeutics preventing neurodegenerative diseases.

In our research, by using coarse-grained and all-atom molecular dynamics simulations, in combination with experiments, we investigate:
  1. Protein/peptide folding and aggregation
  2. Peptide self-assembly and co-assembly
  3. Conformational ensembles of intrinsically disordered proteins (IDPs)
  4. Protein-nanoparticle interactions
  5. Inhibitory mechanism of small molecules against protein aggregation