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Issue 24, 2018
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Binding sites for luminescent amyloid biomarkers from non-biased molecular dynamics simulations

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Abstract

A very stable binding site for the interaction between a pentameric oligothiophene and an amyloid-β(1–42) fibril has been identified by means of non-biased molecular dynamics simulations. In this site, the probe is locked in an all-trans conformation with a Coulombic binding energy of 1200 kJ mol−1 due to the interactions between the anionic carboxyl groups of the probe and the cationic ε-amino groups in the lysine side chain. Upon binding, the conformationally restricted probes show a pronounced increase in molecular planarity. This is in line with the observed changes in luminescence properties that serve as the foundation for their use as biomarkers.

Graphical abstract: Binding sites for luminescent amyloid biomarkers from non-biased molecular dynamics simulations

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Publication details

The article was received on 09 Jan 2018, accepted on 28 Feb 2018 and first published on 01 Mar 2018


Article type: Communication
DOI: 10.1039/C8CC00105G
Citation: Chem. Commun., 2018,54, 3030-3033
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    Binding sites for luminescent amyloid biomarkers from non-biased molecular dynamics simulations

    C. König, R. Skånberg, I. Hotz, A. Ynnerman, P. Norman and M. Linares, Chem. Commun., 2018, 54, 3030
    DOI: 10.1039/C8CC00105G

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