Protein Aggregation

Early aggregation of Amyloid-β (1-42) studied by Fluorescence Correlation Spectroscopy.- Preparation and investigation of crucial oligomers in the early stages of Aβ40 and Aβ42 aggregation.- Preparation and fractionation of heterogeneous Aβ42 oligomers with different aggregation properties.- An efficient method of expression and purification of amyloid beta (Aβ1-42) peptide from E.coli.- Solid-state NMR structure of amyloid-β fibrils.- Time-resolved in situ AFM measurement of growth rates of Aβ40 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 α-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 α-synuclein amyloid fibrils.- Preparation of α-synuclein fibril, ribbon and fibril-91 amyloid polymorphs for structural studies.- Propagation of distinct alpha-synuclein strains within human reconstructed neuronal network and associated neuronal dysfunctions.- Single-particle analysis of the interaction between molecules and protein aggregated species by Dual-Color Time-Resolved Fluorescence Spectroscopy.- FRAP & FRET investigation of α-synuclein fibrillization via liquid-liquid phase separation in vitro and in HeLa cells.- Spectrally-resolved FRET microscopy of -synuclein phase-separated liquid droplets.- Combined H-N cross polarization and carbonyl detection NMR spectroscopy allows to record high-resolution, high-sensitivity spectra of alpha-synuclein in bacterial cells.- Identification of distinct soluble states during fibril formation using multilinear analysis of NMR diffusiondata.- Structural analysis of SOD1 fibrils with mass spectrometry, limited proteolysis and atomic force microscopy (AFM).- Biophysical studies of LLPS and aggregation of TDP-43 LCD.- A spectrophotometric turbidity assay to study Liquid-Liquid Phase Separation of UBQLN2 in vitro.- An optimized SG detection method: Investigation of UBQLN2 effect on RNA-FUS interaction and SG formation.- Neuronal puncta/aggregate formation by wild-type and mutant UBQLN2.- In vivo analysis of a biomolecular condensate in the nervous system of C. elegans.- FLIM-FRET investigation of heterogeneous huntingtin aggregation in HeLa cells.- In vitro characterization of protein:nucleic acid liquid-liquid phase separation by microscopy methods and nanoparticle tracking analysis.- Cross-seeding assay in the investigation of the amyloid core of prion fibrils.- Mapping the domain structure and aggregation propensity of proteins using a Gateway plasmid vector system.