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The de novo design of α-helical peptides for supramolecular self-assembly

Research output: Contribution to journalReview article

Original languageEnglish
Pages (from-to)175-182
Number of pages8
JournalCurrent Opinions in Biotechnology
Volume58
Early online date28 Apr 2019
DOIs
DateAccepted/In press - 25 Mar 2019
DateE-pub ahead of print - 28 Apr 2019
DatePublished (current) - 1 Aug 2019

Abstract

One approach to designing de novo proteinaceous assemblies and materials is to develop simple, standardised building blocks and then to combine these symmetrically to construct more-complex higher-order structures. This has been done extensively using β-structured peptides to produce peptide fibres and hydrogels. Here, we focus on building with de novo α-helical peptides. Because of their self-contained, well-defined structures and clear sequence-to-structure relationships, α helices are highly programmable making them robust building blocks for biomolecular construction. The progress made with this approach over the past two decades is astonishing and has led to a variety of de novo assemblies, including discrete nanoscale objects, and fibrous, nanotube, sheet and colloidal materials. This body of work provides an exceptionally strong foundation for advancing the field beyond in vitro design and into in vivo applications including what we call protein design in cells.

    Structured keywords

  • Bristol BioDesign Institute
  • BrisSynBio

    Research areas

  • synthetic biology

Documents

Documents

  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Elsevier at https://www.sciencedirect.com/science/article/pii/S0958166919300199?via%3Dihub. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 583 KB, PDF document

    Embargo ends: 28/04/20

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    Licence: CC BY-NC-ND

DOI

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