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. ORCID: https://orcid.org/0000-0002-4549-0926, Baldelli Bombelli, F. and Metrangolo, P. (2017) Halogenation dictates the architecture of amyloid peptide nanostructures. Nanoscale, 9 (28). pp. 9805-9810. ISSN 2040-3364 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
URI	https://reading-clone.eprints-hosting.org/id/eprint/72035
Identification Number/DOI	10.1039/C7NR03263C
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	The Royal Society of Chemistry
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