Mechanism of Side Chain-Controlled Proton Conductivity in Bioinspired Peptidic Nanostructures

Subhasish Roy, Lianjun Zheng, Ohad Silberbush, Maor Engel, Yoav Atsmon-Raz, Yifat Miller, Agostino Migliore, David N. Beratan, Nurit Ashkenasy

Research output: Contribution to journalArticlepeer-review


Bioinspired peptide assemblies are promising candidates for use as proton-conducting materials in electrochemical devices and other advanced technologies. Progress toward applications requires establishing foundational structure-function relationships for transport in these materials. This experimental-theoretical study sheds light on how the molecular structure and proton conduction are linked in three synthetic cyclic peptide nanotube assemblies that comprise the three canonical basic amino acids (lysine, arginine, and histidine). Experiments find an order of magnitude higher proton conductivity for lysine-containing peptide assemblies compared to histidine and arginine containing assemblies. The simulations indicate that, upon peptide assembly, the basic amino acid side chains are close enough to enable direct proton transfer. The proton transfer kinetics is determined in the simulations to be governed by the structure and flexibility of the side chains. Together, experiments and theory indicate that the proton mobility is the main determinant of proton conductivity, critical for the performance of peptide-based devices.

Original languageAmerican English
Pages (from-to)12741-12752
Number of pages12
JournalJournal of Physical Chemistry B
Issue number46
StatePublished - 25 Nov 2021

All Science Journal Classification (ASJC) codes

  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Physical and Theoretical Chemistry


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