On the Role of Chirality in Guiding the Self-Assembly of Peptides Academic Article uri icon

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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.

authors

  • Basak, Shibaji
  • Singh, Ishwar
  • Ferranco, Annaleizle
  • Syed, Jebreil
  • Kraatz, Heinz-Bernhard

publication date

  • October 16, 2017