title: Self-assembled peptide architecture with a tooth shape: folding into shape.
abstract: Molecular self-assembly is the spontaneous association of molecules into structured aggregates by which nature builds complex functional systems. While numerous examples have focused on 2D self-assembly to understand the underlying mechanism and mimic this process to create artificial nano- and microstructures, limited progress has been made toward 3D self-assembly on the molecular level. Here we show that a helical β-peptide foldamer, an artificial protein fragment, with well-defined secondary structure self-assembles to form an unprecedented 3D molecular architecture with a molar tooth shape in a controlled manner in aqueous solution. Powder X-ray diffraction analysis, combined with global optimization and Rietveld refinement, allowed us to propose its molecular arrangement. We found that four individual left-handed helical monomers constitute a right-handed superhelix in a unit cell of the assembly, similar to that found in the supercoiled structure of collagen.
authors: Molecular-Level Interface Research Center, Department of Chemistry, KAIST, Daejeon 305-701, Korea.
authors: Sunbum
authors: S
authors: Kwon
authors: Hye Sun
authors: HS
authors: Shin
authors: Jintaek
authors: J
authors: Gong
authors: Jae-Hoon
authors: JH
authors: Eom
authors: Aram
authors: A
authors: Jeon
authors: Sung Hyun
authors: SH
authors: Yoo
authors: Im Sik
authors: IS
authors: Chung
authors: Sung June
authors: SJ
authors: Cho
authors: Hee-Seung
authors: HS
authors: Lee
mesh_terms: D008958:Models, Molecular; D010316:Particle Size; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D017510:Protein Folding
chemical_list: D010455:Peptides