Premium
The Strong Influence of Structure Polymorphism on the Conductivity of Peptide Fibrils
Author(s) -
Ivnitski Denis,
Amit Moran,
Silberbush Ohad,
AtsmonRaz Yoav,
Nanda Jayanta,
CohenLuria Rivka,
Miller Yifat,
Ashkenasy Gonen,
Ashkenasy Nurit
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201604833
Subject(s) - fibril , stacking , peptide , delocalized electron , polymorphism (computer science) , hydrogen bond , chemistry , materials science , conductivity , crystallography , nanotechnology , chemical physics , molecule , organic chemistry , biochemistry , genotype , gene
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.