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Halogenation dictates the architecture of amyloid peptide nanostructures

Pizzi, A., Pigliacelli, C., Gori, A., Nonappa, --, Ikkala, O., Demitri, N., Terraneo, G., Castelletto, V., Hamley, I. W., Baldelli Bombelli, F. and Metrangolo, P. (2017) Halogenation dictates the architecture of amyloid peptide nanostructures. Nanoscale, 9 (28). pp. 9805-9810. ISSN 2040-3364

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To link to this item DOI: 10.1039/C7NR03263C

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:72035
Publisher:The Royal Society of Chemistry

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