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• W2076189730 startingPage "9117" @default.
• W2076189730 abstract "We provide direct evidence that all three histidine residues in amyloid-beta 1-16 (Abeta 1-16) coordinate to Cu(II). In our approach, we generate Abeta 1-16 analogues, in each of which a selected histidine residue is isotopically enriched with (15)N. Pulsed electron spin resonance (ESR) experiments such as electron spin echo envelope modulation (ESEEM) and hyperfine sublevel correlation (HYSCORE) spectroscopy clearly show that all three histidine imidazole rings at positions 6, 13 and 14 in Abeta 1-16 bind to Cu(II). The method employed here does not require either chemical side chain modification or amino acid residue replacement, each of which is traditionally used to determine whether an amino acid residue in a protein binds to a metal ion. We find that the histidine coordination in the Abeta 1-16 peptide is independent of the Cu(II)-to-peptide ratio, which is in contrast to the Abeta 1-40 peptide. The ESR results also suggest tight binding between the histidine residues and the Cu(II) ion, which is likely the reason for the high binding affinity of the Abeta peptide for Cu(II)." @default.
• W2076189730 created "2016-06-24" @default.
• W2076189730 creator A5051559805 @default.
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• W2076189730 date "2008-08-09" @default.
• W2076189730 modified "2023-10-05" @default.
• W2076189730 title "Direct Evidence That All Three Histidine Residues Coordinate to Cu(II) in Amyloid-β₁₋₁₆" @default.
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• W2076189730 doi "https://doi.org/10.1021/bi801014x" @default.
• W2076189730 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18690709" @default.
• W2076189730 hasPublicationYear "2008" @default.
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