A self-assembled protein β-helix as a self-contained biofunctional motif

Camilla Dondi, Javier Garcia-Ruiz, Erol Hasan, Stephanie Rey, James E. Noble, Alex Hoose, Andrea Briones, Ibolya E. Kepiro, Nilofar Faruqui, Purnank Aggarwal, Poonam Ghai, Michael Shaw, Antony T. Fry, Antony Maxwell, Bart W. Hoogenboom, Christian D. Lorenz and Maxim G. Ryadnov ()
Additional contact information
Camilla Dondi: National Physical Laboratory
Javier Garcia-Ruiz: National Physical Laboratory
Erol Hasan: National Physical Laboratory
Stephanie Rey: National Physical Laboratory
James E. Noble: National Physical Laboratory
Alex Hoose: National Physical Laboratory
Andrea Briones: National Physical Laboratory
Ibolya E. Kepiro: National Physical Laboratory
Nilofar Faruqui: National Physical Laboratory
Purnank Aggarwal: National Physical Laboratory
Poonam Ghai: National Physical Laboratory
Michael Shaw: National Physical Laboratory
Antony T. Fry: National Physical Laboratory
Antony Maxwell: National Physical Laboratory
Bart W. Hoogenboom: University College London
Christian D. Lorenz: King’s College London
Maxim G. Ryadnov: National Physical Laboratory

Nature Communications, 2025, vol. 16, issue 1, 1-18

Abstract: Abstract Nature constructs matter by employing protein folding motifs, many of which have been synthetically reconstituted to exploit function. A less understood motif whose structure-function relationships remain unexploited is formed by parallel β-strands arranged in a helical repetitive pattern, termed a β-helix. Herein we reconstitute a protein β-helix by design and endow it with biological function. Unlike β-helical proteins, which are contiguous covalent structures, this β-helix self-assembles from an elementary sequence of 18 amino acids. Using a combination of experimental and computational methods, we demonstrate that the resulting assemblies are discrete cylindrical structures exhibiting conserved dimensions at the nanoscale. We provide evidence for the structures to form a carpet-like three-dimensional scaffold promoting and inhibiting the growth of human and bacterial cells, respectively, while being able to mediate intracellular gene delivery. The study introduces a self-assembled β-helix as a self-contained bio- and multi-functional motif for exploring and exploiting mechanistic biology.

Date: 2025
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-59873-1 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-59873-1

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-59873-1

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().