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Author Notes:

dlynn2@emory.edu

The XAS data were collected at the Stanford Synchrotron Radiation Laboratory, a national user facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences.

Subject:

Research Funding:

The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, and Biomedical Technology Program.

We thank DOE ER15377 (D.G.L.) and NIH GM42025 (R.A.S.) for support, NSF (CHE-0131013) for CD instrumentation, Emory microscopy core laboratory for TEM, and C.L. Emerson for AFM instrumentation.

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

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Journal Title:

Journal of the American Chemical Society

Volume:

Volume 128, Number 11

Publisher:

, Pages 3540-3542

Type of Work:

Article | Post-print: After Peer Review

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.

Copyright information:

© 2006 American Chemical Society

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