title: Reversible, Short α-Peptide Assembly for Controlled Capture and Selective Release of Enantiomers.
abstract: 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.
authors.affiliation: State Key Lab of Supramolecular Structure and Materials, College of Chemistry, Jilin University , Changchun 130012, China.
authors.forename: Xi
authors.initials: X
authors.lastname: Chen
authors.affiliation: State Key Lab of Supramolecular Structure and Materials, College of Chemistry, Jilin University , Changchun 130012, China.
authors.forename: Ying
authors.initials: Y
authors.lastname: He
authors.affiliation: State Key Lab of Supramolecular Structure and Materials, College of Chemistry, Jilin University , Changchun 130012, China.
authors.forename: Yongju
authors.initials: Y
authors.lastname: Kim
authors.affiliation: State Key Lab of Supramolecular Structure and Materials, College of Chemistry, Jilin University , Changchun 130012, China.
authors.forename: Myongsoo
authors.initials: M
authors.lastname: Lee
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D050091:Dendrimers; D004058:Diffusion; D009682:Magnetic Resonance Spectroscopy; D008567:Membranes, Artificial; D008968:Molecular Conformation; D049329:Nanostructures; D010455:Peptides / Q000737:chemistry*; D000072756:Protein Conformation, alpha-Helical; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
chemical_list: D050091:Dendrimers; D008567:Membranes, Artificial; D010455:Peptides