{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360021392647242752.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1002/chem.202103025"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.202103025"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/chem.202103025"}},{"identifier":{"@type":"URI","@value":"https://chemistry-europe.onlinelibrary.wiley.com/doi/pdf/10.1002/chem.202103025"}}],"dc:title":[{"@value":"Segregated Protein–Cucurbit[7]uril Crystalline Architectures via Modulatory Peptide Tectons"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Abstract</jats:title><jats:p>One approach to protein assembly involves water‐soluble supramolecular receptors that act like glues. Bionanoarchitectures directed by these scaffolds are often system‐specific, with few studies investigating their customization. Herein, the modulation of cucurbituril‐mediated protein assemblies through the inclusion of peptide tectons is described. Three peptides of varying length and structural order were N‐terminally appended to RSL, a β‐propeller building block. Each fusion protein was incorporated into crystalline architectures mediated by cucurbit[7]uril (<jats:bold>Q7</jats:bold>). A trimeric coiled‐coil served as a spacer within a <jats:bold>Q7</jats:bold>‐directed sheet assembly of RSL, giving rise to a layered material of varying porosity. Within the spacer layers, the coiled‐coils were dynamic. This result prompted consideration of intrinsically disordered peptides (IDPs) as modulatory tectons. Similar to the coiled‐coil, a mussel adhesion peptide (Mefp) also acted as a spacer between protein–<jats:bold>Q7</jats:bold> sheets. In contrast, the fusion of a nucleoporin peptide (Nup) to RSL did not recapitulate the sheet assembly. Instead, a <jats:bold>Q7</jats:bold>‐directed cage was adopted, within which disordered Nup peptides were partially “captured” by <jats:bold>Q7</jats:bold> receptors. IDP capture occurred by macrocycle recognition of an intrapeptide Phe‐Gly motif in which the benzyl group was encapsulated by <jats:bold>Q7</jats:bold>. The modularity of these protein–cucurbituril architectures adds a new dimension to macrocycle‐mediated protein assembly. Segregated protein crystals, with alternating layers of high and low porosity, could provide a basis for new types of materials.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380021392647242755","@type":"Researcher","foaf:name":[{"@value":"Kiefer O. Ramberg"}],"jpcoar:affiliationName":[{"@value":"School of Chemistry National University of Ireland Galway University Road  Galway H91 TK33 Ireland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021392647242752","@type":"Researcher","foaf:name":[{"@value":"Francesca Guagnini"}],"jpcoar:affiliationName":[{"@value":"School of Chemistry National University of Ireland Galway University Road  Galway H91 TK33 Ireland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021392647242756","@type":"Researcher","foaf:name":[{"@value":"Sylvain Engilberge"}],"jpcoar:affiliationName":[{"@value":"School of Chemistry National University of Ireland Galway University Road  Galway H91 TK33 Ireland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021392647242757","@type":"Researcher","foaf:name":[{"@value":"Małgorzata A. Wrońska"}],"jpcoar:affiliationName":[{"@value":"School of Chemistry National University of Ireland Galway University Road  Galway H91 TK33 Ireland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021392647242754","@type":"Researcher","foaf:name":[{"@value":"Martin L. Rennie"}],"jpcoar:affiliationName":[{"@value":"School of Chemistry National University of Ireland Galway University Road  Galway H91 TK33 Ireland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021392647242753","@type":"Researcher","foaf:name":[{"@value":"Javier Pérez"}],"jpcoar:affiliationName":[{"@value":"Synchrotron SOLEIL L'Orme des Merisiers  Saint-Aubin BP 48 91192 Gif-sur-Yvette Cedex France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021392647242624","@type":"Researcher","foaf:name":[{"@value":"Peter B. Crowley"}],"jpcoar:affiliationName":[{"@value":"School of Chemistry National University of Ireland Galway University Road  Galway H91 TK33 Ireland"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"09476539"},{"@type":"EISSN","@value":"15213765"}],"prism:publicationName":[{"@value":"Chemistry – A European Journal"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"2021-09-29","prism:volume":"27","prism:number":"59","prism:startingPage":"14619","prism:endingPage":"14627"},"reviewed":"false","dc:rights":["http://creativecommons.org/licenses/by-nc-nd/4.0/"],"url":[{"@id":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.202103025"},{"@id":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/chem.202103025"},{"@id":"https://chemistry-europe.onlinelibrary.wiley.com/doi/pdf/10.1002/chem.202103025"}],"createdAt":"2021-08-25","modifiedAt":"2025-10-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360021390765178368","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Displaying a Protein Cage on a Protein Crystal by In-Cell Crystal Engineering"}]},{"@id":"https://cir.nii.ac.jp/crid/1360588380589437696","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"High-throughput structure determination of an intrinsically disordered protein using cell-free protein crystallization"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1002/chem.202103025"},{"@type":"CROSSREF","@value":"10.1021/acs.nanolett.3c02117_references_DOI_ZNHKhX7liT5ly1QYL6Q4sGCUDhr"},{"@type":"CROSSREF","@value":"10.1073/pnas.2322452121_references_DOI_ZNHKhX7liT5ly1QYL6Q4sGCUDhr"}]}