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• W2070377130 endingPage "109" @default.
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• W2070377130 abstract "Alzheimer's disease is a fatal neurodegenerative disorder involving the abnormal accumulation and deposition of peptides (amyloid-β, Aβ) derived from the amyloid precursor protein. Here, we present the structure and the Zn2+ binding sites of human and rat Aβ(1−28) fragments in water/sodium dodecyl sulfate (SDS) micelles by using 1H NMR spectroscopy. The chemical shift variations measured after Zn2+ addition at T > 310 K allowed us to assign the binding donor atoms in both rat and human zinc complexes. The Asp-1 amine, His-6 Nδ, Glu-11 COO-, and His-13 Nε of rat Aβ28 all enter the metal coordination sphere, while His-6 Nδ, His-13, His-14 Nε, Asp-1 amine, and/or Glu-11 COO- are all bound to Zn2+ in the case of human Aβ28. Finally, a comparison between the rat and human binding abilities was discussed." @default.
• W2070377130 created "2016-06-24" @default.
• W2070377130 creator A5001116577 @default.
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• W2070377130 date "2007-12-12" @default.
• W2070377130 modified "2023-09-25" @default.
• W2070377130 title "NMR Studies of the Zn²⁺Interactions with Rat and Human β-Amyloid (1−28) Peptides in Water-Micelle Environment" @default.
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• W2070377130 doi "https://doi.org/10.1021/jp075168m" @default.
• W2070377130 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18072760" @default.
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