Journal Article

FZJ-2020-02199

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

Frieg, B.FZJ* ; Gremer, L.FZJ* ; Heise, H.FZJ* ; Willbold, D.FZJ* ; Gohlke, H. (Corresponding author)FZJ*

2020
Soc. Cambridge

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Please use a persistent id in citations: http://hdl.handle.net/2128/25277  doi:10.1039/D0CC01161D

Abstract: Binding modes for the amyloid-β(1–42) fibril fluorescent dyes thioflavin T and Congo red were predicted by molecular dynamics simulations and binding free energy calculations. Both probes bind on the fibril surface to primarily hydrophobic grooves, with their long axis oriented almost parallel to the fibril axis. The computed binding affinities are in agreement with experimental values. The binding modes also explain observables from previous structural studies and, thus, provide a starting point for the systematic search and design of novel molecules, which may improve in vitro diagnostics for Alzheimer's disease.

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Contributing Institute(s):

1. John von Neumann - Institut für Computing (NIC)
2. Jülich Supercomputing Center (JSC)
3. Strukturbiochemie (IBI-7)

Research Program(s):

1. 511 - Computational Science and Mathematical Methods (POF3-511) (POF3-511)
2. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)
3. Forschergruppe Gohlke (hkf7_20170501) (hkf7_20170501)

Appears in the scientific report 2020

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Database coverage:
; ; Allianz-Lizenz / DFG ; Chemical Reactions ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 5 ; Index Chemicus ; JCR ; NCBI Molecular Biology Database ; National-Konsortium ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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