NMR studies of the Zn2+ interactions with rat and human beta-amyloid (1-28) peptides in water-micelle environment |
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Authors: | Gaggelli Elena Janicka-Klos Anna Jankowska Elzbieta Kozlowski Henryk Migliorini Caterina Molteni Elena Valensin Daniela Valensin Gianni Wieczerzak Ewa |
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Institution: | Department of Chemistry, University of Siena, via Aldo Moro, 53-100 Siena, Italy. |
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Abstract: | Alzheimer's disease is a fatal neurodegenerative disorder involving the abnormal accumulation and deposition of peptides (amyloid-beta, Abeta) derived from the amyloid precursor protein. Here, we present the structure and the Zn2+ binding sites of human and rat Abeta(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 Ndelta, Glu-11 COO-, and His-13 Nepsilon of rat Abeta28 all enter the metal coordination sphere, while His-6 Ndelta, His-13, His-14 Nepsilon, Asp-1 amine, and/or Glu-11 COO- are all bound to Zn2+ in the case of human Abeta28. Finally, a comparison between the rat and human binding abilities was discussed. |
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