Protein Aggregation

Early aggregation of Amyloid-beta (1-42) studied by Fluorescence Correlation Spectroscopy.- Preparation and investigation of crucial oligomers in the early stages of Abeta40 and Abeta42 aggregation.- Preparation and fractionation of heterogeneous Abeta42 oligomers with different aggregation properties.- An efficient method of expression and purification of amyloid beta (Abeta1-42) peptide from E.coli.- Solid-state NMR structure of amyloid-beta fibrils.- Time-resolved in situ AFM measurement of growth rates of Abeta40 fibrils.- Monitoring kinetics of pH-dependent aggregation and disaggregation of the Pmel17 repeat domain.- Analysis of Tau:nucleoporin interactions by Surface Plasmon Resonance Spectroscopy.- Microfluidic chamber technology to study missorting and spreading of Tau protein in Alzheimer disease.- Using FRET-based biosensor cells to study the seeding activity of tau and -synuclein.- Functional applications of stable tau oligomers in cell biology and electrophysiology studies.- An additive-free model for tau self-assembly.- Cross-linking mass spectrometry analysis of metastable compact structures in intrinsically disordered proteins.- A validated method to prepare stable tau oligomers.- Light microscopy and dynamic light scattering to study liquid-liquid phase separation of Tau proteins in vitro.- Study of tau liquid-liquid phase separation in vitro.- Liquid-Liquid Phase Separation to study the association of proteins in solution.- Mapping phase diagram of tau-RNA LLPS under live cell coculturing conditions.- The role of buffers in wild-type HEWL amyloid fibril formation mechanism - a methodological approach.- Reproducible formation of insulin superstructures: amyloid-like fibrils, spherulites and particulates.- CD and solid-state NMR studies of low-order oligomers of transthyretin.- Identifying biological and biophysical features of different maturation states of