Modulating amyloid self-assembly and fibril morphology with Zn(II) |
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Authors: | Dong Jijun Shokes Jacob E Scott Robert A Lynn David G |
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Affiliation: | Center for the Analysis of SupraMolecular Self-assemblies, Department of Chemistry, Emory University, 1521 Dickey Drive, Atlanta, Georgia 30322, USA. |
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Abstract: | Metal ions (Zn(II)) are demonstrated as probes of amyloid structure in simple segments of the Abeta peptide, Abeta(13-21). By restricting the possible metal binding sites to His13/His14 dyad, we show that Zn2+ can specifically control the rate of self-assembly and dramatically regulate amyloid morphology via distinct coordination environments as characterized by X-ray absorption spectroscopy. The data establish that the single His13 is sufficient to coordinate Zn2+ productively for typical amyloid fiber formation, while a distinct Zn2+ coordination environment can be accessed in the presence of His13/Hi14 dyad to stabilize sheet/sheet associations and the transition to a ribbon/tube morphology. |
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