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 …

Recent advancements of nanomedicine in neurodegenerative disorders theranostics

S Mukherjee, VS Madamsetty… - Advanced Functional …, 2020 - Wiley Online Library
Recent times have witnessed an upsurge in the incidence of neurodegenerative disorders
such as Alzheimer's disease, Parkinson's disease, Huntington's disease, Prion disease, and …

BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra

A Micsonai, F Wien, É Bulyáki, J Kun… - Nucleic acids …, 2018 - academic.oup.com
Circular dichroism (CD) spectroscopy is a widely used method to study the protein
secondary structure. However, for decades, the general opinion was that the correct …

Self-Assembly of Amyloid-Beta (Aβ) Peptides from Solution to Near In Vivo Conditions

PH Nguyen, F Sterpone… - The Journal of Physical …, 2022 - ACS Publications
Understanding the atomistic resolution changes during the self-assembly of amyloid
peptides or proteins is important to develop compounds or conditions to alter the …

Tryptophan self-assembly yields cytotoxic nanofibers containing amyloid-mimicking and cross-seeding competent conformers

KP Prajapati, BG Anand, M Ansari, AB Tiku, K Kar - Nanoscale, 2022 - pubs.rsc.org
Dietary consumption of Trp via protein-based foods is essential for the maintenance of
crucial metabolic processes including the synthesis of proteins and several vital metabolites …

Conformation dependence of diphenylalanine self-assembly structures and dynamics: Insights from hybrid-resolution simulations

Q Xiong, Y Jiang, X Cai, F Yang, Z Li, W Han - ACS nano, 2019 - ACS Publications
The molecular design of peptide-assembled nanostructures relies on extensive knowledge
pertaining to the relationship between conformational features of peptide constituents and …

Exploding the repeat length paradigm while exploring amyloid toxicity in Huntington's disease

R Wetzel - Accounts of Chemical Research, 2020 - ACS Publications
Conspectus Huntington's disease (HD) is a progressive, familial neurodegenerative disease
triggered by the expansion of a polyglutamine (polyQ) track in the protein huntingtin (htt) …

Fluorescence chemicals to detect insoluble and soluble amyloid-β aggregates

D Lee, SM Kim, HY Kim, YS Kim - ACS Chemical Neuroscience, 2019 - ACS Publications
Misfolded amyloid-β (Aβ) is the key biomarker of Alzheimer's disease (AD), and discoveries
of fluorescence chemicals visualizing such Aβ aggregates in the brain have made major …

Small oligomers of Aβ42 protein in the bulk solution with AlphaFold2

H Santuz, PH Nguyen, F Sterpone… - ACS Chemical …, 2022 - ACS Publications
Aggregation of amyloid-β (Aβ42) protein is one hallmark of Alzheimer's disease, and the
conformations of the smallest Aβ42 oligomers are largely unknown. Here, we explore the …

Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease

KW Drombosky, S Rode, R Kodali, TC Jacob… - Neurobiology of …, 2018 - Elsevier
In Huntington disease (HD), an expanded polyglutamine (polyQ> 37) sequence within
huntingtin (htt) exon1 leads to enhanced disease risk. It has proved difficult, however, to …