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

Contact Details ORCID

Publications (14)
Projects (0)

Showing 14 publications

2020

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

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2020

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

2020

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

2020

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

2020

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

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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

Amyloid Fibril Formation - Dye Detection and Effects of Lipids

David Lindberg

Doctoral thesis

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

Development of the Amyloid Fibril Characterisation Toolbox - New use for old dyes

David Lindberg

Licentiate thesis

2015

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

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

2005

Vortex matter in Bi2Sr2CaCu2O8+x with controlled interlayer coupling

David Lindberg

Licentiate thesis

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