title: Microtubes with rectangular cross-section by self-assembly of a short β-peptide foldamer.
abstract: In nature, complex and well-defined structures are constructed by the self-assembly of biomolecules. It has been shown that β-peptide foldamers can mimic natural peptides and self-assemble into three-dimensional molecular architectures thanks to their rigid and predictable helical conformation in solution. Using shorter foldamers, which can be prepared more easily than longer ones, to form such architectures is highly desirable, but shorter foldamers have been overlooked due to the seemingly inferior number of intramolecular hydrogen bonds to stabilize a folded state in solution. Here we report that a β-peptide tetramer, although it lacks full helical propensity in solution, does self-assemble to form well-defined microtubes with rectangular cross-section by evaporation-induced self-assembly.
authors.affiliation: Institute for Basic Science, Department of Chemistry, KAIST, Daejeon 305-701, Korea.
authors.forename: Jangbae
authors.initials: J
authors.lastname: Kim
authors.forename: Sunbum
authors.initials: S
authors.lastname: Kwon
authors.forename: Su Hyun
authors.initials: SH
authors.lastname: Kim
authors.forename: Chung-Kyung
authors.initials: CK
authors.lastname: Lee
authors.forename: Joon-Hwa
authors.initials: JH
authors.lastname: Lee
authors.forename: Sung June
authors.initials: SJ
authors.lastname: Cho
authors.forename: Hee-Seung
authors.initials: HS
authors.lastname: Lee
authors.forename: Hyotcherl
authors.initials: H
authors.lastname: Ihee
mesh_terms: D018360:Crystallography, X-Ray; D003515:Cycloleucine / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D009842:Oligopeptides; D003515:Cycloleucine