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Issue 32, 2015
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Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid

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Abstract

We identify distinct site-specific dynamics over the time course of Aβ1–23 amyloid formation by using an unnatural amino acid, p-cyanophenylalanine, as a sensitive fluorescent and Raman probe. Our results also suggest the key role of an edge-to-face aromatic interaction in the conformational conversion to form and stabilize β-sheet structure.

Graphical abstract: Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid

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Publication details

The article was received on 07 Jan 2015, accepted on 18 Mar 2015 and first published on 18 Mar 2015


Article type: Communication
DOI: 10.1039/C5CC00149H
Author version available: Download Author version (PDF)
Citation: Chem. Commun., 2015,51, 7000-7003
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    Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid

    H. Liu, R. Lantz, P. Cosme, N. Rivera, C. Andino, W. G. Gonzalez, A. C. Terentis, E. P. Wojcikiewicz, R. Oyola, J. Miksovska and D. Du, Chem. Commun., 2015, 51, 7000
    DOI: 10.1039/C5CC00149H

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