TY - JOUR
T1 - Mechanism of Side Chain-Controlled Proton Conductivity in Bioinspired Peptidic Nanostructures
AU - Roy, Subhasish
AU - Zheng, Lianjun
AU - Silberbush, Ohad
AU - Engel, Maor
AU - Atsmon-Raz, Yoav
AU - Miller, Yifat
AU - Migliore, Agostino
AU - Beratan, David N.
AU - Ashkenasy, Nurit
N1 - Publisher Copyright:
© 2021 American Chemical Society.
PY - 2021/11/25
Y1 - 2021/11/25
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85119913114&partnerID=8YFLogxK
U2 - 10.1021/acs.jpcb.1c08857
DO - 10.1021/acs.jpcb.1c08857
M3 - Article
C2 - 34780197
AN - SCOPUS:85119913114
SN - 1520-6106
VL - 125
SP - 12741
EP - 12752
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 46
ER -