%0 Conference Paper
%A Frieg, Benedikt
%A Gohlke, Holger
%T Simulating Thioflavin T and Congo Red Binding to the Fibril Structure of Amyloid-$ß$(1-42)
%V 50
%C Jülich
%I Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag
%M FZJ-2020-01378
%@ 978-3-95806-443-0
%B Publication Series of the John von Neumann Institute for Computing (NIC) NIC Series
%P 53 - 61
%D 2020
%< NIC Symposium 2020
%X Binding modes for two amyloid-β(1-42) fibril tracers,  namely Thioflavin T and Congo red, were  identified  using  unbiased  all-atom  molecular  dynamics  simulations  and  binding  free-energy computations.  Both dyes bind to primarily hydrophobic grooves on the amyloid fibril  surface,  perpendicular  to  itsβ-strands.   Binding  affinities  computed  by  the  MM-GBSA method are in excellent agreement with experimental values and corroborate the proposed binding modes.  The binding modes can guide the rational design of novel biomarkers for amyloid fibrils.
%B NIC Symposium 2020
%C 27 Feb 2020 - 28 Feb 2020, Jülich (Germany)
Y2 27 Feb 2020 - 28 Feb 2020
M2 Jülich, Germany
%F PUB:(DE-HGF)8 ; PUB:(DE-HGF)7
%9 Contribution to a conference proceedingsContribution to a book
%U https://juser.fz-juelich.de/record/874345