Research output: Contribution to journal › Review article
Original language | English |
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Pages (from-to) | 175-182 |
Number of pages | 8 |
Journal | Current Opinions in Biotechnology |
Volume | 58 |
Early online date | 28 Apr 2019 |
DOIs | |
Date | Accepted/In press - 25 Mar 2019 |
Date | E-pub ahead of print - 28 Apr 2019 |
Date | Published (current) - 1 Aug 2019 |
Additional links |
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.