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Communication

Modulating Amyloid Self-Assembly and Fibril Morphology with Zn(II)

Supporting Info

Jijun Dong,^§ Jacob E. Shokes,^† Robert A. Scott,^† and David G. Lynn*^§

Center for the Analysis of SupraMolecular Self-assemblies, Departments of Chemistry and Biology, Emory University, 1521 Dickey Drive, Atlanta, Georgia 30322, and Center for Metalloenzyme Studies and Department of Chemistry, University of Georgia, Athens, Georgia 30602-2556

J. Am. Chem. Soc., 2006, 128 (11), pp 3540–3542

DOI: 10.1021/ja055973j

Publication Date (Web): March 1, 2006

Emory University.

†

University of Georgia.

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

, dlynn2@emory.edu

Abstract

Metal ions (Zn(II)) are demonstrated as probes of amyloid structure in simple segments of the Aβ peptide, Aβ(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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