Description: Binding Modes of Thioflavin T and Congo Red to the Fibril Structure of Amyloid-β(1

This title appears in the Scientific Report : 2020

Binding Modes of Thioflavin T and Congo Red to the Fibril Structure of Amyloid-β(1–42)

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 th...

Personal Name(s):	Frieg, Benedikt
	Gremer, Lothar / Heise, Henrike / Willbold, Dieter / Gohlke, Holger (Corresponding author)
Contributing Institute:	Strukturbiochemie; IBI-7 Jülich Supercomputing Center; JSC John von Neumann - Institut für Computing; NIC
Published in:	Chemical communications, 56 (2020) S. 7589-7592
Imprint:	Cambridge Soc. 2020
PubMed ID:	32510059
DOI:	10.1039/D0CC01161D
Document Type:	Journal Article
Research Program:	Forschergruppe Gohlke Physical Basis of Diseases Computational Science and Mathematical Methods
Link:	Get full text Published on 2020-06-01. Available in OpenAccess from 2021-06-01. Published on 2020-06-01. Available in OpenAccess from 2021-06-01. Get full text
	Publikationsportal JuSER

Please use the identifier: http://hdl.handle.net/2128/25277 in citations.
Please use the identifier: http://dx.doi.org/10.1039/D0CC01161D in citations.

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.