Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction-Reference-Cited by-同舟云学术

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Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

Published:2017-04-17 Issue:16 Volume:56 Page:2170-2174
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lindberg David J.¹^ORCID,Wenger Anna¹,Sundin Elin²,Wesén Emelie¹,Westerlund Fredrik¹^ORCID,Esbjörner Elin K.¹^ORCID

Affiliation:

1. Division of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Kemivägen 10, 412 96 Gothenburg, Sweden

2. Division of Chemistry and Biochemistry, Department of Chemistry and Chemical Engineering, Chalmers University of Technology, Kemivägen 10, 412 96 Gothenburg, Sweden

Funder

Vetenskapsr?det

VINNOVA

Wenner-Gren Foundation

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00035

Reference22 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

3. Thioflavin T as a Molecular Rotor: Fluorescent Properties of Thioflavin T in Solvents with Different Viscosity

4. Molecular mechanism of Thioflavin-T binding to amyloid fibrils

5. Steady-state and time-resolved Thioflavin-T fluorescence can report on morphological differences in amyloid fibrils formed by Aβ(1-40) and Aβ(1-42)

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