The chelation targeting metal–Aβ40 aggregates may lead to formation of Aβ40 oligomers
Abstract
The fluorescent chelator (FC-1) was designed by combining a metal-chelating unit and a ThT-based Aβ aggregate-binding fluorescent unit. FC-1 is a cell membrane-penetrable chelator with a moderate chelation ability to Cu(2+) and Zn(2+) and can target metal-Aβ40 aggregates. Treatment with FC-1 led to enhanced cytotoxicity of the aggregates, because the aggregates were converted into a pool of oligomers.
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Two approaches have been pursued in BFC design: direct incorporation of metal-binding atom donors into the structural framework of an Aβ-interacting compound, and linking the metal-chelating and Aβ-binding molecular fragments.
“In this context, two approaches have been pursued in BFC design. 31,49–58 One strategy is based on the direct incorporation of metal-binding atom donors into the structural framework of an Aβ-interacting compoud (Scheme 1, approach A), and the other involves linking the metal-chelating and Aβ-binding molecular fragments (Scheme 1, approach B).”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [53]
Other reported BFCs have employed benzothiazole fragments as amyloid-binding motifs, but no binding affinities for the Aβ species have been measured for those systems.
“While other reported BFCs have employed benzothiazole fragments as amyloid-binding motifs, no binding affinities for the Aβ species have been measured for those systems.49,53,54”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [53]
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Self-citation
- Authors
- Zhang, Y., Chen, L.-Y., Yin, W.-X., Yin, J., Zhang, S.-B., & Liu, C.-L.
- Affiliations
- Central China Normal University (CN)
- Venue
- Dalton Transactions
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2011
- Volume
- 40
- Issue
- 18
- Pages
- 4830
- ISSN
- 1477-9226 (ISSN-L)
- 1477-9234
- OpenAlex
- W2144307327
- Semantic Scholar
- b8b6c48abe4d3e12937b904e9fee4fe1b75462f4
- Cited by
- 26
- References
- 25
- Citations by year
- 2024: 3 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 2 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 5
- FWCI
- 1.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Dalton Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Spectroscopy › Molecular Sensors and Ion Detection
- Physical Sciences › Materials Science › Materials Chemistry › Luminescence and Fluorescent Materials
- Keywords
- Aβ40, copper(II) chelation, amyloid aggregates, oligomerization, cytotoxicity, Alzheimer's disease
- MeSH terms
- Chelating Agents, Copper, HeLa Cells, Humans, Hydrogen-Ion Concentration, Metals, Molecular Conformation, Peptide Fragments, Zinc, Amyloid beta-Peptides, Coordination Complexes
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