title: Formation of α-helical nanofibers by mixing β-structured and α-helical coiled coil peptides.
abstract: The helical coiled coil is a well-studied folding motif that can be used for the design of nanometer-sized bioinspired fibrous structures with potential applications as functional materials. A two-component system of coiled coil based model peptides is investigated, which forms, under acidic conditions, uniform, hundreds of nanometers long, and ~2.6 nm thick trimeric α-helical fibers. In the absence of the other component and under the same solvent conditions, one model peptide forms β-sheet-rich amyloid fibrils and the other forms stable trimeric α-helical coiled coils, respectively. These observations reveal that the complementary interactions driving helical folding are much stronger here than those promoting the intermolecular β-sheet formation. The results of this study are important in the context of amyloid inhibition but also open up new avenues for the design of novel fibrous peptidic materials.
authors.affiliation: Department of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.
authors.forename: Enrico
authors.initials: E
authors.lastname: Brandenburg
authors.forename: Hans V
authors.initials: HV
authors.lastname: Berlepsch
authors.forename: Jork
authors.initials: J
authors.lastname: Leiterer
authors.forename: Franziska
authors.initials: F
authors.lastname: Emmerling
authors.forename: Beate
authors.initials: B
authors.lastname: Koksch
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D057139:Nanofibers / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D010455:Peptides