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Self‐assembled chiral nanostructures of amphiphilic peptide: from single molecule to aggregate
Author(s) -
Zhou Ting,
Zhang Zhiqing,
Zhang Xuemei,
Wang Chen,
Xu Guiying,
Yang Yanlian
Publication year - 2017
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3032
Subject(s) - circular dichroism , self assembly , chirality (physics) , chemistry , peptide , amphiphile , intermolecular force , molecule , fibril , crystallography , beta sheet , nanotechnology , stereochemistry , biophysics , materials science , organic chemistry , polymer , biochemistry , copolymer , chiral symmetry breaking , physics , quantum mechanics , nambu–jona lasinio model , quark , biology
We report interesting hierarchical self‐assembled architectures from a designed amphiphilic peptide. The bisignate cotton effects in circular dichroism spectra show typical peptide aggregation‐induced. The observation of peptide assembly structures from initial particles and fibrils to ribbon structures is supported by microscopy (atomic force microscopy and transmission electron microscopy). The visualization of individual peptide at the single molecular level offered insights of the intermolecular interactions responsible for the formation of aggregates, which is investigated by scanning tunneling microscopy. The orientation of intermolecular bonds between carboxylic and amine group and the hydrophobic interactions between alanine residues could be the dominant driving force for the assembly chirality at near‐neutral pH. The single molecular and aggregate level evidence in this manuscript will shed light on the understanding of hierarchical chiral self‐assembly pathway and the underlying mechanism. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.