Interrogating amyloid aggregates using fluorescent probes

A Aliyan, NP Cook, AA Martí - Chemical reviews, 2019 - ACS Publications
Amyloids are a broad class of proteins and peptides that can misfold and assemble into long
unbranched fibrils with a cross-β conformation. These misfolding and aggregation events …

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

M Biancalana, S Koide - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2010 - Elsevier
Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of
amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since …

Detection of amyloid fibrils in Parkinson's disease using plasmonic chirality

J Kumar, H Eraña, E López-Martínez… - Proceedings of the …, 2018 - National Acad Sciences
Amyloid fibrils, which are closely associated with various neurodegenerative diseases, are
the final products in many protein aggregation pathways. The identification of fibrils at low …

Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status

M Groenning - Journal of chemical biology, 2010 - Springer
Because understanding amyloid fibrillation in molecular detail is essential for development
of strategies to control amyloid formation and overcome neurodegenerative disorders …

Protein-induced photophysical changes to the amyloid indicator dye thioflavin T

LS Wolfe, MF Calabrese, A Nath… - Proceedings of the …, 2010 - National Acad Sciences
The small molecule thioflavin T (ThT) is a defining probe for the identification and
mechanistic study of amyloid fiber formation. As such, ThT is fundamental to investigations of …

Direct observation of morphological tranformation from twisted ribbons into helical ribbons

ET Pashuck, SI Stupp - Journal of the American Chemical Society, 2010 - ACS Publications
We report on the direct observation of a nanostructural transformation from a twisted ribbon
to a helical ribbon in supramolecular assemblies of peptide amphiphiles. Using cryogenic …

Biomarker-activated multifunctional lysosome-targeting chimeras mediated selective degradation of extracellular amyloid fibrils

Z Liu, Q Deng, G Qin, J Yang, H Zhang, J Ren, X Qu - Chem, 2023 - cell.com
Selective degradation of extracellular pathogenic proteins by degrader technologies such as
lysosome-targeting chimeras (LYATCs) provides promising therapeutic strategies for" …

General principles underpinning amyloid structure

AIP Taylor, RA Staniforth - Frontiers in Neuroscience, 2022 - frontiersin.org
Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …

A comparison of three fluorophores for the detection of amyloid fibers and prefibrillar oligomeric assemblies. ThT (thioflavin T); ANS (1-anilinonaphthalene-8-sulfonic …

ND Younan, JH Viles - Biochemistry, 2015 - ACS Publications
Amyloid fiber formation is a key event in many misfolding disorders. The ability to monitor the
kinetics of fiber formation and other prefibrillar assemblies is therefore crucial for …

Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease

DJ Hayne, SC Lim, PS Donnelly - Chemical Society Reviews, 2014 - pubs.rsc.org
Alzheimer's disease is the most common form of age-related neurodegenerative dementia.
The disease is characterised by the presence of plaques in the cerebral cortex. The major …