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Formation of alpha-helical nanofibers by mixing beta-structured and alpha-helical coiled coil peptides.

E. Brandenburg, H. v. Berlepsch, J.Leiterer, F. Emmerling, and B. Koksch – 2012

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 alpha-helical fibers. In the absence of the other component and under the same solvent conditions, one model peptide forms beta-sheet-rich amyloid fibrils and the other forms stable trimeric alpha-helical coiled coils, respectively. These observations reveal that the complementary interactions driving helical folding are much stronger here than those promoting the intermolecular beta-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.

Titel
Formation of alpha-helical nanofibers by mixing beta-structured and alpha-helical coiled coil peptides.
Verfasser
E. Brandenburg, H. v. Berlepsch, J.Leiterer, F. Emmerling, and B. Koksch
Datum
2012
Kennung
DOI: 10.1021/bm300882d
Zitierweise
Biomacromolecules, 13, (11), 3542 - 3551.
Sprache
eng
Art
Text