Twisted intramolecular charge transfer (TICT) and twists beyond TICT: from mechanisms to rational designs of bright and sensitive fluorophores

C Wang, W Chi, Q Qiao, D Tan, Z Xu… - Chemical Society Reviews, 2021 - pubs.rsc.org
The twisted intramolecular charge transfer (TICT) mechanism has guided the development
of numerous bright and sensitive fluorophores. This review briefly overviews the history of …

ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

K Gade Malmos, LM Blancas-Mejia, B Weber… - Amyloid, 2017 - Taylor & Francis
Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While
concerns have recently been raised about its use as a probe specific for amyloid, ThT still …

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 …

From macroscopic measurements to microscopic mechanisms of protein aggregation

SIA Cohen, M Vendruscolo, CM Dobson… - Journal of molecular …, 2012 - Elsevier
The ability to relate bulk experimental measurements of amyloid formation to the
microscopic assembly processes that underlie protein aggregation is critical in order to …

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 …

Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis

L Radamaker, J Baur, S Huhn, C Haupt… - Nature …, 2021 - nature.com
Systemic AL amyloidosis is a debilitating and potentially fatal disease that arises from the
misfolding and fibrillation of immunoglobulin light chains (LCs). The disease is patient …

[HTML][HTML] Formation and characterization of plant-based amyloid fibrils from hemp seed protein

I Kutzli, J Zhou, T Li, SK Baier, R Mezzenga - Food Hydrocolloids, 2023 - Elsevier
Amyloid fibrils from plant-based food protein sources bear a large unexploited potential for
applications in food and other biomaterials due to their techno-functional features. However …

Nanoparticles in relation to peptide and protein aggregation

M Zaman, E Ahmad, A Qadeer, G Rabbani… - International journal of …, 2014 - Taylor & Francis
Over the past two decades, there has been considerable research interest in the use of
nanoparticles in the study of protein and peptide aggregation, and of amyloid-related …

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 …

Formation, structure and functional characteristics of amyloid fibrils formed based on soy protein isolates

Z Yu, N Li, Y Liu, B Zhang, M Zhang, X Wang… - International Journal of …, 2024 - Elsevier
Food protein-derived amyloid fibrils possess great untapped potential applications in food
and other biomaterials. The objective of this report was to investigate the formation …