The Strong Influence of Structure Polymorphism on the Conductivity of Peptide Fibrils

Denis Ivnitski, Moran Amit, Ohad Silberbush, Yoav Atsmon-Raz, Jayanta Nanda, Rivka Cohen-Luria, Yifat Miller, Gonen Ashkenasy, Nurit Ashkenasy

Research output: Contribution to journalArticlepeer-review


Peptide fibril nanostructures have been advocated as components of future biotechnology and nanotechnology devices. However, the ability to exploit the fibril functionality for applications, such as catalysis or electron transfer, depends on the formation of well-defined architectures. Fibrils made of peptides substituted with aromatic groups are described presenting efficient electron delocalization. Peptide self-assembly under various conditions produced polymorphic fibril products presenting distinctly different conductivities. This process is driven by a collective set of hydrogen bonding, electrostatic, and π-stacking interactions, and as a result it can be directed towards formation of a distinct polymorph by using the medium to enhance specific interactions rather than the others. This method facilitates the detailed characterization of different polymorphs, and allows specific conditions to be established that lead to the polymorph with the highest conductivity.

Original languageAmerican English
Pages (from-to)9988-9992
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number34
StatePublished - 16 Aug 2016


  • bio-electronics
  • chemical evolution
  • peptide fibrils
  • polymorphism

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Catalysis


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