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Issue 28, 2017
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Halogenation dictates the architecture of amyloid peptide nanostructures

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Abstract

Amyloid peptides yield a plethora of interesting nanostructures though difficult to control. Here we report that depending on the number, position, and nature of the halogen atoms introduced into either one or both phenylalanine benzene rings of the amyloid β peptide-derived core-sequence KLVFF, four different architectures were obtained in a controlled manner. Our findings demonstrate that halogenation may develop as a general strategy to engineer amyloidal peptide self-assembly and obtain new amyloidal nanostructures.

Graphical abstract: Halogenation dictates the architecture of amyloid peptide nanostructures

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Publication details

The article was received on 08 May 2017, accepted on 20 Jun 2017 and first published on 22 Jun 2017


Article type: Communication
DOI: 10.1039/C7NR03263C
Citation: Nanoscale, 2017,9, 9805-9810
  • Open access: Creative Commons BY license
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    Halogenation dictates the architecture of amyloid peptide nanostructures

    A. Pizzi, C. Pigliacelli, A. Gori, Nonappa, O. Ikkala, N. Demitri, G. Terraneo, V. Castelletto, I. W. Hamley, F. Baldelli Bombelli and P. Metrangolo, Nanoscale, 2017, 9, 9805
    DOI: 10.1039/C7NR03263C

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