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Issue 12, 2014
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Comparison of three competing dynamic force spectroscopy models to study binding forces of amyloid-β (1–42)

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Abstract

We performed single molecule dynamic force spectroscopy experiments to study the dimerization of two amyloid-β (1–42) peptides and compared three different theoretical models used to fit experimental data: Bell–Evans, Dudko–Hummer–Szabo, and Friddle–De Yoreo. Using these models we extracted values of the dissociation rate at zero force, k0, and height and the width of the energy barrier, ΔG and xβ. We show the importance of including the effect of the linker molecule. All three models corrected for the linker effect give comparable results for xβ and show more discrepancy for k0 and ΔG values, ΔG parameter correlates well between Dudko–Hummer–Szabo and Friddle–De Yoreo models but differs for the Bell–Evans model.

Graphical abstract: Comparison of three competing dynamic force spectroscopy models to study binding forces of amyloid-β (1–42)

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Publication details

The article was received on 23 Aug 2013, accepted on 08 Jan 2014 and first published on 09 Jan 2014


Article type: Paper
DOI: 10.1039/C3SM52257A
Soft Matter, 2014,10, 1924-1930

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    Comparison of three competing dynamic force spectroscopy models to study binding forces of amyloid-β (1–42)

    F. T. Hane, S. J. Attwood and Z. Leonenko, Soft Matter, 2014, 10, 1924
    DOI: 10.1039/C3SM52257A

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