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.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Brandenburg E,Berlepsch HV,Leiterer J,Emmerling F,Koksch B

doi

10.1021/bm300882d

subject

Has Abstract

pub_date

2012-11-12 00:00:00

pages

3542-51

issue

11

eissn

1525-7797

issn

1526-4602

journal_volume

13

pub_type

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