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NMR studies of the Zn2+ interactions with rat and human β-amyloid (1-28) peptides in water-micelle environment.
Autorzy
Rok wydania
2008
Czasopismo
Journal of Physical Chemistry B
Numer woluminu
112
Strony
100-109
DOI
10.1021/jp075168m
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
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.
Adres publiczny
https://doi.org/10.1021/jp075168m
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