title: Directional assembly of α-helical peptides induced by cyclization.
abstract: Effective stabilization of short peptide chains into a helical structure has been a challenge in the fields of chemistry and biology. Here we report a novel method for α-helix stabilization of short peptides through their confinement in a cyclic architecture. We synthesized block peptides based on a short peptide and a flexible linker as linear precursors. Subsequent cyclization of the peptide precursors resulted in a conformational change of the peptide unit from a random coil to an α-helix. The incorporation of hydrophobic residues into the peptide unit led to a facially amphiphilic conformation of the molecular cycle. The resulting amphiphilic peptide self-assembled into undulated nanofibers through the directional assembly of small oblate micelles.
authors.affiliation: Center for Bio-Responsive Assembly and Department of Chemistry, Seoul National University, Seoul 151-747, Korea.
authors.forename: Seunghyun
authors.initials: S
authors.lastname: Sim
authors.forename: Yongju
authors.initials: Y
authors.lastname: Kim
authors.forename: Taehoon
authors.initials: T
authors.lastname: Kim
authors.forename: Sunhee
authors.initials: S
authors.lastname: Lim
authors.forename: Myongsoo
authors.initials: M
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003500:Cyclization; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010455:Peptides