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

Copper ligation to soluble oligomers of the English mutant of the amyloid-β peptide yields a linear Cu(I) site that is resistant to O2 oxidation.

Chemical communications (Cambridge, England) - 25 May 2013

Peck Kristy L, Clewett Heather S, Schmitt Jennifer C, Shearer Jason

Abstract excerpt

Copper coordination to soluble oligomers of the English (AβH(6)R) mutant of the amyloid-β peptide is probed. Cu(II) coordination yields a square planar (N/O)4 coordination environment, while reduction yields an O2 inert linear bis-His Cu(I) centre.

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Peptides
Share to Copper
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Oxidation-Reduction

Share to Oxygen

Share to Peptide Fragments

Source

Open in PubMed Open full text

Identifiers

PMID: 23608950
DOI: 10.1039/c3cc40326b
PMCID: PMC3697824

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Copper ligation to soluble oligomers of the English mutant of the amyloid-β peptide yields a linear Cu(I) site that is resistant to O2 oxidation.PMID 23608950Read ↗

Alzheimer's Aβ peptides with disease-associated N-terminal modifications: influence of isomerisation, truncation and mutation on Cu2+ coordination.Semantic proximity Read ↗

Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.Semantic proximity Read ↗

Dual-action peptide shuttles rescue Cu-amyloid-β-induced neurotoxicity and relocate Cu intracellularlySemantic proximity Read ↗

The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain.Semantic proximity Read ↗

Quantification of the binding properties of Cu2+ to the amyloid beta peptide: coordination spheres for human and rat peptides and implication on Cu2+-induced aggregation.Semantic proximity Read ↗

Dissecting the copper bioinorganic chemistry of the functional and pathological roles of the prion protein: Relevance in Alzheimer's disease and cancerSemantic proximity Read ↗

The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion.Semantic proximity Read ↗

Self-assembled monolayers of Aβ peptides on Au electrodes: an artificial platform for probing the reactivity of redox active metals and cofactors relevant to Alzheimer's disease.Semantic proximity Read ↗

Kinetics of the Interactions between Copper and Amyloid-β with FAD Mutations and Phosphorylation at the N terminus.Semantic proximity Read ↗

Dityrosine cross-link trapping of amyloid-β intermediates reveals that self-assembly is required for Aβ-induced cytotoxicitySemantic proximity Read ↗

The Co(II) ion binds to the N-terminal region of amyloid-beta (Aβ) peptides and modulates Aβ aggregationSemantic proximity Read ↗

Mutation of the Phe20 residue in Alzheimer's amyloid beta-peptide might decrease its toxicity due to disruption of the Met35-cupric site electron transfer pathway.Semantic proximity Read ↗

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