Thioflavin Derivatives as Markers for Amyloid‐β Fibrils: Insights into Structural Features Important for High‐Affinity Binding
Abstract
How do we go together? Structural variations have been used to obtain information regarding the interaction of thioflavin-derived markers and amyloid-β fibril targets. Affinity variations of up to three orders of magnitude were observed, revealing some structural requirements for these markers at the molecular level.
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Titrations with various amounts of compounds reveal competitive binding curves that yield Ki values 180±25 nM and 36±6 nM for L1 and L2, respectively.
“Titrations with various amounts of compounds reveal competitive binding curves that yield Ki values 180±25 nM and 36±6 nM for L1 and L2, respectively (Figure 6b).84,85”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [85]
Performing the same titration of Aβ fibrils with ThT yields a Kd of 1.17±0.14 μM, a value similar to those reported previously.
“By comparison, performing the same titration of Aβ fibrils with ThT yields a Kd of 1.17±0.14 μM (Figure S21b), a value similar to those reported previously.83,85”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [85]
L1 exhibits a high affinity for Aβ fibrils comparable to other neutral ThT derivatives, suggesting that appending a metal-binding group to the 2-phenylbenzothiazole fragment does not limit its amyloid binding affinity.
“This value suggests that L1 exhibits a high affinity for the Aβ fibrils comparable to other neutral ThT derivatives,83,85 suggesting that appending a metal-binding group to the 2-phenylbenzothiazole fragment does not limit its amyloid binding affinity.”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [85]
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References 30 · Cited by 72
- Authors
- Leuma Yona, R., Mazères, S., Faller, P., & Gras, E.
- Affiliations
- Institut de Pharmacologie et de Biologie Structurale (FR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Gras, Emmanuel
- Venue
- ChemMedChem
- Publisher
- Wiley
- Published
- 2008-01-03
- Volume
- 3
- Issue
- 1
- Pages
- 63-66
- ISSN
- 1860-7179 (ISSN-L)
- 1860-7187
- OpenAlex
- W2087303538
- Cited by
- 72
- References
- 30
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 1 · 2023: 4 · 2022: 1 · 2021: 1 · 2020: 5 · 2018: 3 · 2017: 4 · 2016: 6 · 2015: 1 · 2014: 10 · 2013: 7 · 2012: 7
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- ChemMedChem (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Association France Alzheimer
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Spectroscopy › Molecular Sensors and Ion Detection
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta fibrils, amyloid-beta detection, binding affinity, structural requirements
- MeSH terms
- Alzheimer Disease, Binding Sites, Heterocyclic Compounds, Peptides, Structure-Activity Relationship, Thiazoles, Biomarkers, Amyloid beta-Peptides, Protein Structure, Tertiary, Benzothiazoles
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