Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Residue-Specific Binding Mechanisms of Thioflavin T to a Surface of Flat β-Sheets within a Peptide Self-Assembly Mimic.

Biochemistry - 4 Aug 2020

Namioka Sae, Yoshida Norio, Konno Hiroyuki, Makabe Koki

Abstract excerpt

Thioflavin T (ThT) is a popular fluorescent dye for detecting amyloid, a protein aggregate with a β-sheet-rich structure that causes many neurodegenerative diseases. Despite the dye's popularity, a detailed understanding of its molecular binding mechanism remains elusive. We previously reported a protein model that can bind ThT on a single-layer β-sheet and revealed that a channel formed by aromatic rings with a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Benzothiazoles
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence

Share to Models, Molecular

Share to Mutation

Share to Peptides

Share to Protein Conformation, beta-Strand

Source

Identifiers

PMID: 32496046
DOI: 10.1021/acs.biochem.0c00280

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Residue-Specific Binding Mechanisms of Thioflavin T to a Surface of Flat β-Sheets within a Peptide Self-Assembly Mimic.PMID 32496046Read ↗

Redesign of a thioflavin-T-binding protein with a flat β-sheet to evaluate a thioflavin-T-derived photocatalyst with enhanced affinity.Semantic proximity Read ↗

ThX – A next-generation probe for the early detection of amyloid aggregatesSemantic proximity Read ↗

Rational design of amyloid beta peptide-binding proteins: pseudo-Abeta beta-sheet surface presented in green fluorescent protein binds tightly and preferentially to structured Abeta.Semantic proximity Read ↗

Conformational dynamics of Tau in the cell quantified by an intramolecular FRET biosensor in physiological and pathological contextSemantic proximity Read ↗

Loop Site Mutation-Enhanced Sensing Performance of G-Triplex Probe: Preliminary Exploration on Its Stability and "Structure-Efficiency" Relationship.Semantic proximity Read ↗

Peptide Self-Assembly and Its Modulation: Imaging on the Nanoscale.Semantic proximity Read ↗

Aggregation gatekeeper and controlled assembly of Trpzip β-hairpins.Semantic proximity Read ↗

A KLVFFAE-Derived Peptide Probe for Detection of Alpha-Synuclein Fibrils.Semantic proximity Read ↗

Growth, Polymorphism, and Spatially Controlled Surface Immobilization of Biotinylated Variants of IAPP21-27 Fibrils.Semantic proximity Read ↗

Highly Potent Peptide Therapeutics To Prevent Protein Aggregation In Huntington’s DiseaseSemantic proximity Read ↗

Computational Modeling of Functionalized Graphene Quantum Dots Binding to Tau Fibrils in Alzheimer’s DiseaseSemantic proximity Read ↗

Design of amyloidogenic peptide trapsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.