Copper(II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: Stoichiometry and coordination geometry are independent of Aβ oligomeric form

Biochemistry

Volumn 48, Issue 20, 2009, Pages 4388-4402

  Sarell, Claire J ^a   Syme, Christopher D ^a   Rigby, Stephen E J ^a   Viles, John H ^a  

^a QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; BINDING CURVES; CIRCULAR DICHROISM; COORDINATION GEOMETRY; DISSOCIATION CONSTANT; ELECTRON PARAMAGNETIC RESONANCE; FLUORESCENCE QUENCHING; HYDROPHOBIC INTERACTIONS; L-HISTIDINE; MONOMERIC FORMS; N-TERMINAL; NEUROTOXICITY; NITRILOTRIACETIC ACID; ORDERS OF MAGNITUDE; SECONDARY STRUCTURES; SELF-ASSOCIATION; SENILE PLAQUES;

AMINES; ASSOCIATION REACTIONS; BINDING ENERGY; BINDING SITES; CARBOXYLATION; DICHROISM; DISSOCIATION; ELECTRON RESONANCE; GLYCOPROTEINS; HYDROPHOBICITY; IONS; METHANOL; PARAMAGNETIC RESONANCE; PARAMAGNETISM; QUENCHING; STOICHIOMETRY;

COORDINATION REACTIONS;

AMYLOID BETA PROTEIN[1-42]; CUPRIC ION; GLYCINE; HISTIDINE; NITRILOTRIACETIC ACID;

ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; COMPLEX FORMATION; ELECTRON SPIN RESONANCE; METAL BINDING; NEUROTOXICITY; PH; PRIORITY JOURNAL; PROTEIN BINDING;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; BINDING, COMPETITIVE; CIRCULAR DICHROISM; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; HYDROGEN-ION CONCENTRATION; IONS; METHANOL; MODELS, CHEMICAL; MOLECULAR CONFORMATION; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 66149161888     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900254n     Document Type: Article

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