TY - JOUR A1 - Brandenburg, E. A1 - von Berlepsch, H. A1 - Leiterer, Jork A1 - Emmerling, Franziska A1 - Koksch, B. T1 - Formation of alpha-helical nanofibers by mixing beta-structured and alpha-helical coiled coil peptides JF - Biomacromolecules N2 - 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. PY - 2012 DO - https://doi.org/10.1021/bm300882d SN - 1525-7797 VL - 13 IS - 11 SP - 3542 EP - 3551 PB - ACS Publ. CY - Washington, DC, USA AN - OPUS4-27126 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER -