Reversible, short α-peptide assembly for controlled capture and selective release of enantiomers

Xi Chen, Ying He, Yongju Kim, Myongsoo Lee

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)


Although significant progress has been achieved with short peptide nanostructures, the construction of switchable membrane assemblies remains a great challenge. Here we report short α-peptide assemblies that undergo thermo-reversible switching between assembly and disassembly states, triggered by the conformational change of laterally grafted short peptides from a folded α-helix to a random coil conformation. The α-helical peptide based on two oligoether dendron side groups forms flat disks, while the peptide helix based on three dendron side groups forms hollow vesicles. The vesicular membrane can spontaneously capture a racemic mixture through the self-formation of vesicular containers upon heating and enantioselectively release the chiral guest molecule through preferential diffusion across the vesicular walls.

Original languageEnglish
Pages (from-to)5773-5776
Number of pages4
JournalJournal of the American Chemical Society
Issue number18
Publication statusPublished - 2016 May 11
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Reversible, short α-peptide assembly for controlled capture and selective release of enantiomers'. Together they form a unique fingerprint.

Cite this