Halogenation Dictates Architecture of Amyloid Peptide Nanostructures
Loading...
Access rights
openAccess
publishedVersion
URL
Journal Title
Journal ISSN
Volume Title
A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
This publication is imported from Aalto University research portal.
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
Date
Major/Subject
Mcode
Degree programme
Language
en
Pages
6
Series
Nanoscale, Volume 9, issue 28, pp. 9805–9810
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.Description
Keywords
Other note
Citation
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