title: Toroidal nanostructures from self-assembly of block copolypeptides based on poly(L-arginine) and β-sheet peptide.
abstract: We demonstrate here that rationally designed block copolypeptides based on poly(L-arginine) and β-sheet peptides can form toroidal nanostructures. In aqueous solution, we found that 1D nanoribbons roll up and connect in an end-to-end fashion under charge-balanced conditions, resulting in the formation of barrel-like toroidal nanostructures. Toroidal diameter was highly uniform (10 nm), indicating that there is a preferred geometrical packing requirement for toroid formation. Our results demonstrate that, when suitably designed, β-sheet nanostructures can be manipulated to form more complex 2D nanostructures. This finding offers new opportunities not only for the fabrication of more sophisticated peptide-based nanobiomaterials, but also for understanding and inhibiting protein misfolding diseases.
authors: Translational Research Center for Protein Function Control, Department of Materials Science and Engineering, Yonsei University, Seoul 120-749, Korea.
authors: Yong-beom
authors: YB
authors: Lim
authors: Eunji
authors: E
authors: Lee
authors: Myongsoo
authors: M
authors: Lee
mesh_terms: D003208:Concanavalin A / Q000737:chemistry*; D007700:Kinetics; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D010455:Peptides; D003208:Concanavalin A; C015462:polyarginine