Abstract
A generic model is presented for the self-assembly of chiral units into intrinsically twisted tapes, ribbons, fibrils and fibres. Rationally designed self-assembling β-strand-forming peptides are shown to behave as chiral rod-like objects, exhibiting the entire hierarchy of these structures, which can form nematic fluids or gels. These observations provide new insight into the generic self-assembling properties of ?-sheets, and the factors governing the structures and extraordinary stability of pathological amyloid fibrils in vivo. More generally, they provide a prescription of routes to novel tape and fibril-like macromolecules based on a wide variety of self-assembling chiral units.
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Aggeli, A. et al. (2002). Exploiting Peptide Self-assembly to Engineer Novel Biopolymers: Tapes, Ribbons, Fibrils and Fibres. In: Self-Assembling Peptide Systems in Biology, Medicine and Engineering. Springer, Dordrecht. https://doi.org/10.1007/0-306-46890-5_1
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DOI: https://doi.org/10.1007/0-306-46890-5_1
Publisher Name: Springer, Dordrecht
Print ISBN: 978-0-7923-7090-1
Online ISBN: 978-0-306-46890-2
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