Halogenation Dictates Architecture of Amyloid Peptide Nanostructures

Research output: Contribution to journalArticleScientificpeer-review

Researchers

Research units

  • Polytechnic University of Milan
  • Istituto di Chimica del Riconoscimento Molecolare
  • Elettra Sincrotrone Trieste
  • University of Reading

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.

Details

Original languageEnglish
Pages (from-to)9805–9810
Number of pages6
JournalNanoscale
Volume9
Issue number28
Publication statusPublished - 2017
MoE publication typeA1 Journal article-refereed

ID: 13869917