David Bernson

Researcher at Chalmers, Biology and Biological Engineering, Chemical Biology

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.

Source: chalmers.se

Showing 9 publications

2018

Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42)

Emelie Vilhelmsson Wesén, Audrey Gallud, Alexandra Paul et al
Biochimica et Biophysica Acta - Biomembranes. Vol. 1860 (11), p. 2204-2214
Journal article
2017

Lipid membranes catalyse the fibril formation of the amyloid-? (1–42) peptide through lipid-fibril interactions that reinforce secondary pathways

David Lindberg, Emelie Vilhelmsson Wesén, Johan Björkeroth et al
Biochimica et Biophysica Acta - Biomembranes. Vol. 1859 (10), p. 1921-1929
Journal article
2017

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

David Lindberg, Anna Wenger, Elin Sundin et al
Biochemistry. Vol. 56 (16), p. 2170-2174
Journal article
2016

Detection of amyloid-beta fibrils using the DNA-intercalating dye YOYO-1: Binding mode and fibril formation kinetics

David Lindberg, Elin Esbjörner Winters
Biochemical and Biophysical Research Communications. Vol. 469 (2), p. 313-318
Journal article
2015

Time-resolved thioflavin-T fluorescence-expanding the amyloid characterisation toolbox

David Lindberg, Elin Esbjörner Winters
FEBS Journal. Vol. 282, p. 178-179
Conference contribution
2015

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)

David Lindberg, Moa Sandberg Wranne, Melina Gilbert Gatty et al
Biochemical and Biophysical Research Communications. Vol. 458 (2), p. 418-423
Journal article

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