A self-assembled protein β-helix as a self-contained biofunctional motif
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,...
Saved in:
| Main Authors: | , , , , , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-05-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-59873-1 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849309735672610816 |
|---|---|
| author | 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 Maxim G. Ryadnov |
| author_facet | 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 Maxim G. Ryadnov |
| author_sort | Camilla Dondi |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-84bfa0b53fca4d80829a83fa5ad64e5f |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-84bfa0b53fca4d80829a83fa5ad64e5f2025-08-20T03:53:58ZengNature PortfolioNature Communications2041-17232025-05-0116111810.1038/s41467-025-59873-1A self-assembled protein β-helix as a self-contained biofunctional motifCamilla Dondi0Javier Garcia-Ruiz1Erol Hasan2Stephanie Rey3James E. Noble4Alex Hoose5Andrea Briones6Ibolya E. Kepiro7Nilofar Faruqui8Purnank Aggarwal9Poonam Ghai10Michael Shaw11Antony T. Fry12Antony Maxwell13Bart W. Hoogenboom14Christian D. Lorenz15Maxim G. Ryadnov16National Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryNational Physical LaboratoryLondon Centre for Nanotechnology, University College LondonDepartment of Physics, King’s College LondonNational Physical LaboratoryAbstract 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.https://doi.org/10.1038/s41467-025-59873-1 |
| spellingShingle | 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 Maxim G. Ryadnov A self-assembled protein β-helix as a self-contained biofunctional motif Nature Communications |
| title | A self-assembled protein β-helix as a self-contained biofunctional motif |
| title_full | A self-assembled protein β-helix as a self-contained biofunctional motif |
| title_fullStr | A self-assembled protein β-helix as a self-contained biofunctional motif |
| title_full_unstemmed | A self-assembled protein β-helix as a self-contained biofunctional motif |
| title_short | A self-assembled protein β-helix as a self-contained biofunctional motif |
| title_sort | self assembled protein β helix as a self contained biofunctional motif |
| url | https://doi.org/10.1038/s41467-025-59873-1 |
| work_keys_str_mv | AT camilladondi aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT javiergarciaruiz aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT erolhasan aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT stephanierey aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT jamesenoble aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT alexhoose aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT andreabriones aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT ibolyaekepiro aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT nilofarfaruqui aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT purnankaggarwal aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT poonamghai aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT michaelshaw aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT antonytfry aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT antonymaxwell aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT bartwhoogenboom aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT christiandlorenz aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT maximgryadnov aselfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT camilladondi selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT javiergarciaruiz selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT erolhasan selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT stephanierey selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT jamesenoble selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT alexhoose selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT andreabriones selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT ibolyaekepiro selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT nilofarfaruqui selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT purnankaggarwal selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT poonamghai selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT michaelshaw selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT antonytfry selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT antonymaxwell selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT bartwhoogenboom selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT christiandlorenz selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif AT maximgryadnov selfassembledproteinbhelixasaselfcontainedbiofunctionalmotif |