ArticleThe Journal of biological chemistry2015
Truncated Amyloid-β(11-40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Cell-specific copper dyshomeostasis mechanism in Alzheimer's disease.Translational neurodegeneration · 2025Review
- Impact of aging on copper isotopic composition in the murine brain.Metallomics : integrated biometal science · 2024Article
- Review
- Direct Competition of ATCUN Peptides with Human Serum Albumin for Copper(II) Ions Determined by LC-ICP MS.ACS omega · 2023Article
- Revisiting the Role of Vitamins and Minerals in Alzheimer's Disease.Antioxidants (Basel, Switzerland) · 2023Review
- Review
- Microglia and Astrocytes in Alzheimer's Disease in the Context of the Aberrant Copper Homeostasis Hypothesis.Biomolecules · 2021Review
- N-Terminally Truncated and Pyroglutamate-Modified Aβ Forms Are Measurable in Human Cerebrospinal Fluid and Are Potential Markers of Disease Progression in Alzheimer's Disease.Frontiers in neuroscience · 2021Article
- Polyphenols as Potential Metal Chelation Compounds Against Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2021Review
- Article
- Copper stabilizes antiparallel β-sheet fibrils of the amyloid β40 (Aβ40)-Iowa variant.The Journal of biological chemistry · 2020Article
- Vascular Dysfunction in Alzheimer's Disease: A Prelude to the Pathological Process or a Consequence of It?Journal of clinical medicine · 2019Review
- Recent Expansions on Cellular Models to Uncover the Scientific Barriers Towards Drug Development for Alzheimer's Disease.Cellular and molecular neurobiology · 2019Review
- Copper Redox Cycling Inhibits Aβ Fibre Formation and Promotes Fibre Fragmentation, while Generating a Dityrosine Aβ Dimer.Scientific reports · 2018Article
- Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in aThe Journal of biological chemistry · 2018Article
- Neurotoxicity Linked to Dysfunctional Metal Ion Homeostasis and Xenobiotic Metal Exposure: Redox Signaling and Oxidative Stress.Antioxidants & redox signaling · 2018Review
- Cu(II) binding to various forms of amyloid-β peptides. Are they friends or foes?European journal of inorganic chemistry · 2018Article
- BACE1 Cleavage Site Selection Critical for Amyloidogenesis and Alzheimer's Pathogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Mammalian Metallothionein-3: New Functional and Structural Insights.International journal of molecular sciences · 2017Review
- Role of Copper in the Onset of Alzheimer's Disease Compared to Other Metals.Frontiers in aging neuroscience · 2017Review
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alzheimer disease coincides with the formation of extracellular amyloid plaques composed of the amyloid-β (Aβ) peptide. Aβ is typically 40 residues long (Aβ(1-40)) but can have variable C and N termini. Naturally occurring N-terminally truncated Aβ(11-40/42) is found in the cerebrospinal fluid and has a similar abundance to Aβ(1-42), constituting one-fifth of the plaque load. Based on its specific N-terminal sequence we hypothesized that truncated Aβ(11-40/42) would have an elevated affinity for Cu(2+). Various spectroscopic techniques, complemented with transmission electron microscopy, were used to determine the properties of the Cu(2+)-Aβ(11-40/42) interaction and how Cu(2+) influences amyloid fiber formation. We show that Cu(2+)-Aβ(11-40) forms a tetragonal complex with a 34 ± 5 fm dissociation constant at pH 7.4. This affinity is 3 orders of magnitude tighter than Cu(2+) binding to Aβ(1-40/42) and more than an order of magnitude tighter than that of serum albumin, the extracellular Cu(2+) transport protein. Furthermore, Aβ(11-40/42) forms fibers twice as fast as Aβ(1-40) with a very different morphology, forming bundles of very short amyloid rods. Substoichiometric Cu(2+) drastically perturbs Aβ(11-40/42) assembly, stabilizing much longer fibers. The very tight fm affinity of Cu(2+) for Aβ(11-40/42) explains the high levels of Cu(2+) observed in Alzheimer disease plaques.
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