David Bernson

Researcher at 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
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Showing 14 publications


Graphene oxide sheets and quantum dots inhibit alpha-synuclein amyloid formation by different mechanisms

Marziyeh Ghaeidamini, David Bernson, Nima Sasanian et al
Nanoscale. Vol. 12 (37), p. 19450-19460
Journal article

Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers

Tony Werner, David Bernson, Elin Esbjörner Winters et al
Proceedings of the National Academy of Sciences of the United States of America. Vol. 117 (45), p. 27997-28004
Journal article

Amyloid formation of bovine insulin is retarded in moderately acidic pH and by addition of short-chain alcohols

David Bernson, Almedina Basic, MD Tuhin Abed et al
European Biophysics Journal. Vol. 49 (2), p. 145-153
Journal article

Correlation between Cellular Uptake and Cytotoxicity of Fragmented α-Synuclein Amyloid Fibrils Suggests Intracellular Basis for Toxicity

Xiaolu Zhang, Emelie Vilhelmsson Wesén, Ranjeet Kumar et al
ACS Chemical Neuroscience. Vol. 11 (3), p. 233-241
Journal article

Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro

Nima Sasanian, David Bernson, Istvan Horvath et al
Biomolecules. Vol. 10 (6), p. 1-19
Journal article

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

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

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

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

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

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

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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