This title appears in the Scientific Report :
2020
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 of Thioflavin T and Congo Red to the Fibril Structure of Amyloid-β(1–42)
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...
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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://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. |