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Reversible, Short α-Peptide Assembly for Controlled Capture and Selective Release of Enantiomers
- Chen, Xi, He, Ying, Kim, Yongju, Lee, Myongsoo
- Journal of the American Chemical Society 2016 v.138 no.18 pp. 5773-5776
- containers, enantiomers, nanomaterials, peptides
- 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.