On the Role of Chirality in Guiding the Self‐Assembly of Peptides. (22nd September 2017)

• Record Type: Journal Article
• Authors: Basak, Shibaji; Singh, Ishwar; Ferranco, Annaleizle; Syed, Jebreil; Kraatz, Heinz‐Bernhard
• Is Part Of: Angewandte Chemie. Volume 129:Number 43(2017)
• Page Start: 13473
• Page End: 13477
• Publication Date: 2017-09-22
• Subjects: Gele -- Molekulare Erkennung -- Peptide -- Selbstorganisation -- Selbstsortierung; Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201706162
• Languages: English
• ISSNs: 0044-8249

Abstract

Abstract: 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.