Formation of α-Helical Nanoï¬bers by Mixing β-Structured and α-Helical Coiled Coil Peptides
E. Brandenburg , H. von Berlepsch , J. Leiterer , F. Emmerling , B. Koksch
Biomacromolecules, Just Accepted Manuscript
DOI: 10.1021/bm300882d
The helical coiled coil is a well-studied folding motif that can be used for the design of nanometer-sized bio-inspired 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 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.
Keyword: Peptide Modification Services