Contribution to a conference proceedings/Contribution to a book

FZJ-2020-01378

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Simulating Thioflavin T and Congo Red Binding to the Fibril Structure of Amyloid-$ß$(1-42)

Frieg, B.FZJ* ; Gohlke, H. (Corresponding author)FZJ*

2020
Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag Jülich
ISBN: 978-3-95806-443-0

This record in other databases:

Please use a persistent id in citations: http://hdl.handle.net/2128/24449

Abstract: 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.

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Contributing Institute(s):

1. John von Neumann - Institut für Computing (NIC)
2. Jülich Supercomputing Center (JSC)
3. Strukturbiochemie (ICS-6)

Research Program(s):

1. 511 - Computational Science and Mathematical Methods (POF3-511) (POF3-511)

Appears in the scientific report 2020

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Linked articles:

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Book/Proceedings Müller, M. (Editor)Extern* ; Binder, K. (Editor) ; Trautmann, A. (Editor)FZJ*
NIC Symposium 2020: proceedings
2020NIC Symposium, JülichJülich, Germany, 27 Feb 2020 - 28 Feb 20202020-02-272020-02-28 Jülich : Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag, NIC Series 50, v, 424 S. (2020)2020   Files  Fulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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