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.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Brandenburg E,Berlepsch HV,Leiterer J,Emmerling F,Koksch Bdoi
10.1021/bm300882dsubject
Has Abstractpub_date
2012-11-12 00:00:00pages
3542-51issue
11eissn
1525-7797issn
1526-4602journal_volume
13pub_type
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