Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
Matthew Biancalana,Shohei Koide +1 more
TLDR
Recent progress in the understanding of ThT-fibril interactions at an atomic resolution is reviewed to offer guidance for designing the next generation of amyloid assembly diagnostics, inhibitors, and therapeutics.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2010-07-01 and is currently open access. It has received 1580 citations till now. The article focuses on the topics: Amyloid.read more
Citations
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Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Gang Wei,Zhiqiang Su,Nicholas P. Reynolds,Paolo Arosio,Ian W. Hamley,Ehud Gazit,Raffaele Mezzenga +6 more
TL;DR: This review will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality.
Journal ArticleDOI
On the lag phase in amyloid fibril formation
TL;DR: Rates of microscopic processes taking place during the lag phase of amyloid fibril formation for a reaction starting from an initially monomeric 4 μm solution of Aβ42.
Journal ArticleDOI
Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation.
TL;DR: It is shown that ThT fluorescence correlates linearly with amyloid concentration over ThT concentrations ranging from 0.2 to 500 µM, which could affect the shape of the aggregation curves, but this effect is protein-dependent and not universal.
Journal ArticleDOI
Molecular rotors: what lies behind the high sensitivity of the thioflavin-T fluorescent marker.
TL;DR: The advantages and disadvantages of the various nonradiative models while focusing on the model that was initially proposed by Glasbeek and co-workers for auramine-O to be the best suited for ThT are discussed.
Journal ArticleDOI
Protein-induced photophysical changes to the amyloid indicator dye thioflavin T
Leslie S. Wolfe,Matthew F. Calabrese,Abhinav Nath,Dorottya Blaho,Andrew D. Miranker,Yong Xiong +5 more
TL;DR: These efforts fundamentally extend existing understanding about the origins of amyloid-induced photophysical changes by preventing the fluorophore from adopting its preferred excited state configuration, nonradiative relaxation pathways are minimized and quantum yield is increased.
References
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Protein folding and misfolding
TL;DR: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound-B.
William E. Klunk,Henry Engler,Agneta Nordberg,Yanming Wang,G. Blomqvist,Daniel P. Holt,Mats Bergström,Irina Savitcheva,Guo Feng Huang,Sergio Estrada,Birgitta Ausén,Manik L. Debnath,Julien Barletta,Julie C. Price,Johan Sandell,Brian J. Lopresti,Anders Wall,Pernilla Koivisto,Gunnar Antoni,Chester A. Mathis,Bengt Långström +20 more
TL;DR: The results suggest that PET imaging with the novel tracer, PIB, can provide quantitative information on amyloid deposits in living subjects.
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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.
TL;DR: Thioflavine T associates rapidly with aggregated fibrils of the synthetic β/A4‐derived peptides β( 1–28) and β(1–40), giving rise to a new excitation maximum at 450 nm and enhanced emission at 482 nm, as opposed to the 385 nm and 445 nm of the free dye.
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Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Michael R. Sawaya,S. Sambashivan,Rebecca Nelson,Magdalena I. Ivanova,Stuart A. Sievers,Marcin I. Apostol,Michael J. Thompson,Melinda Balbirnie,Jed J.W. Wiltzius,Heather T. McFarlane,Anders Ø. Madsen,Anders Ø. Madsen,Christian Riekel,David Eisenberg +13 more
TL;DR: Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.
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Structure of the cross-beta spine of amyloid-like fibrils.
Rebecca Nelson,Michael R. Sawaya,Melinda Balbirnie,Anders Ø. Madsen,Anders Ø. Madsen,Christian Riekel,Robert Grothe,David Eisenberg +7 more
TL;DR: The atomic structure of the cross-β spine illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.