Halogenation Dictates Architecture of Amyloid Peptide Nanostructures

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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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Date
2017
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Language
en
Pages
6
9805–9810
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Nanoscale, Volume 9, issue 28
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 at either one or both phenylalanine benzene rings of the amyloid [small beta] peptide-derived core-sequence KLVFF, four different architectures were obtained in a controlled manner. Our findings demonstrate halogenation may develop as a general strategy to engineer amyloidal peptide self-assembly and obtain new amyloidal nanostructures.
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Pizzi , A , Pigliacelli , C , Gori , A , Nonappa , N , Ikkala , O , Demitri , N , Terraneo , G , Castelletto , V , Hamley , I W , Bombelli , F B & Metrangolo , P 2017 , ' Halogenation Dictates Architecture of Amyloid Peptide Nanostructures ' , Nanoscale , vol. 9 , no. 28 , pp. 9805–9810 . https://doi.org/10.1039/C7NR03263C