Premium
On the Role of Chirality in Guiding the Self‐Assembly of Peptides
Author(s) -
Basak Shibaji,
Singh Ishwar,
Ferranco Annaleizle,
Syed Jebreil,
Kraatz HeinzBernhard
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201706162
Subject(s) - homochirality , chemistry , self assembly , tripeptide , chirality (physics) , peptide , intermolecular force , stereochemistry , molecule , enantiomer , organic chemistry , chiral symmetry , biochemistry , nambu–jona lasinio model , physics , quantum mechanics , quark
Homochirality in peptides is crucial in sustaining “like–like” intermolecular interactions that allow the formation of assemblies and aggregates and is ultimately responsible for the resulting material properties. With the help of a series of stereoisomers of the tripeptide F–F–L, we demonstrate the critical role that peptide stereochemistry plays in the self‐assembly of peptides, guided by molecular recognition, and for self‐sorting. Homochiral self‐assemblies are thermally and mechanically more robust compared to heterochiral self‐assemblies. Morphological studies of the multicomponent peptide systems showed that aggregates formed from homochiral peptides possessed a uniform nano‐fibrous structure, whereas heterochiral systems resulted in self‐sorted systems with a heterogeneous morphology. In essence, homochiral peptides form the stronger aggregates, which may be one of reasons why homochirality is preferred in living systems.