Formation of 伪-Helical Nanofibers by Mixing 尾-Structured and 伪-Helical Coiled Coil Peptides

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• 作者：Enrico Brandenburg ; Hans v. Berlepsch ; Jork Leiterer ; Franziska Emmerling ; Beate Koksch
• 刊名：Biomacromolecules
• 出版年：2012
• 出版时间：November 12, 2012
• 年：2012
• 卷：13
• 期：11
• 页码：3542-3551
• 全文大小：635K
• 年卷期：v.13,no.11(November 12, 2012)
• ISSN：1526-4602

文摘

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