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J Am Chem Soc. 2006 Mar 22;128(11):3540-2.

Modulating amyloid self-assembly and fibril morphology with Zn(II).

Author information

1
Center for the Analysis of SupraMolecular Self-assemblies, Department of Chemistry, Emory University, 1521 Dickey Drive, Atlanta, Georgia 30322, USA.

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.

PMID:
16536526
PMCID:
PMC3555692
DOI:
10.1021/ja055973j
[Indexed for MEDLINE]
Free PMC Article

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