David Bernson
David Bernson is a Post-doc at the division of Chemical Biology. His primary research focus is on the misfolding and aggregation of proteins into amyloid fibrils, and their involvement in neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease. Biophysical techniques such as fluorescence, polarization spectroscopy and confocal microscopy are combined with live cell studies to investigate toxic properties of amyloid aggregates, as well as how this is influenced by presence of other molecules. David is also teaching basic chemistry at bachelor’s level.
Showing 12 publications
Amyloid formation of bovine insulin is retarded in moderately acidic pH and by addition of short-chain alcohols
Correlation between Cellular Uptake and Cytotoxicity of Fragmented α-Synuclein Amyloid Fibrils Suggests Intracellular Basis for Toxicity
Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro
Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42)
Lipid membranes catalyse the fibril formation of the amyloid-? (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways
Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction
Detection of amyloid-beta fibrils using the DNA-intercalating dye YOYO-1: Binding mode and fibril formation kinetics
Development of the Amyloid Fibril Characterisation Toolbox - New use for old dyes
Time-resolved thioflavin-T fluorescence-expanding the amyloid characterisation toolbox
Steady-state and time-resolved Thioflavin-T fluorescence can report on morphological differences in amyloid fibrils formed by A beta(1-40) and A beta(1-42)
Vortex matter in Bi2Sr2CaCu2O8+x with controlled interlayer coupling
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