Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/103526
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dc.contributor.authorAronsson, Christopheren
dc.contributor.authorDånmark, Staffanen
dc.contributor.authorZhou, Fengen
dc.contributor.authorÖberg, Peren
dc.contributor.authorEnander, Karinen
dc.contributor.authorSu, Haibinen
dc.contributor.authorAili, Danielen
dc.date.accessioned2015-10-01T07:23:10Zen
dc.date.accessioned2019-12-06T21:14:34Z-
dc.date.available2015-10-01T07:23:10Zen
dc.date.available2019-12-06T21:14:34Z-
dc.date.copyright2015en
dc.date.issued2015en
dc.identifier.citationAronsson, C., Dånmark, S., Zhou, F., Öberg, P., Enander, K., Su, H., et al. (2015). Self-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly properties. Scientific Reports, 5, 14063-.en
dc.identifier.issn2045-2322en
dc.identifier.urihttps://hdl.handle.net/10356/103526-
dc.identifier.urihttp://hdl.handle.net/10220/38765en
dc.description.abstractCoiled coils with defined assembly properties and dissociation constants are highly attractive components in synthetic biology and for fabrication of peptide-based hybrid nanomaterials and nanostructures. Complex assemblies based on multiple different peptides typically require orthogonal peptides obtained by negative design. Negative design does not necessarily exclude formation of undesired species and may eventually compromise the stability of the desired coiled coils. This work describe a set of four promiscuous 28-residue de novo designed peptides that heterodimerize and fold into parallel coiled coils. The peptides are non-orthogonal and can form four different heterodimers albeit with large differences in affinities. The peptides display dissociation constants for dimerization spanning from the micromolar to the picomolar range. The significant differences in affinities for dimerization make the peptides prone to thermodynamic social self-sorting as shown by thermal unfolding and fluorescence experiments, and confirmed by simulations. The peptides self-sort with high fidelity to form the two coiled coils with the highest and lowest affinities for heterodimerization. The possibility to exploit self-sorting of mutually complementary peptides could hence be a viable approach to guide the assembly of higher order architectures and a powerful strategy for fabrication of dynamic and tuneable nanostructured materials.en
dc.language.isoenen
dc.relation.ispartofseriesScientific Reportsen
dc.rightsThis work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/en
dc.titleSelf-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly propertiesen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science and Engineeringen
dc.identifier.doihttp://dx.doi.org/10.1038/srep14063en
dc.description.versionPublished versionen
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