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dc.contributor.authorScherman, Oren
dc.contributor.authorMcCune, Jade
dc.contributor.authorChen, xiaoyi
dc.contributor.authorHuang, Zehuan
dc.contributor.authorSokolowski, kamil
dc.contributor.authorSala Lang, Renata
dc.contributor.authorMcLean, Alan
dc.contributor.authorWu, Guanglu
dc.contributor.authorKing, Katherine
dc.date.accessioned2022-06-10T01:05:51Z
dc.date.available2022-06-10T01:05:51Z
dc.date.issued2022-05-18
dc.identifier.issn0002-7863
dc.identifier.other35535953
dc.identifier.otherPMC9121384
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/337972
dc.description.abstractPeptide dimerization is ubiquitous in natural protein conjugates and artificial self-assemblies. A major challenge in artificial systems remains achieving quantitative heterodimerization of peptides, critical for next-generation biomolecular purification and formulation of therapeutics. Here, we employ a synthetic host to simultaneously encapsulate an aromatic peptide and a non-canonical L-perfluorophenylalanine-containing peptide through embedded polar-π interactions, thus constructing an unprecedented series of heteropeptide dimers. To demonstrate the utility, this heteropeptide dimerization strategy was applied to achieve on-resin recognition of N-terminal aromatic residues in peptides as well as insulin, both exhibiting high recycling efficiency (> 95%). This research unveils a generic approach to exploit quantitative heteropeptide dimers for the design of supramolecular (bio)systems.
dc.languageeng
dc.publisherAmerican Chemical Society
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourcenlmid: 7503056
dc.sourceessn: 1520-5126
dc.subjectPeptides
dc.subjectOligopeptides
dc.subjectProteins
dc.subjectDimerization
dc.titleOn-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization
dc.typeArticle
dc.date.updated2022-06-10T01:05:51Z
prism.endingPage8479
prism.issueIdentifier19
prism.publicationNameJournal of the American Chemical Society
prism.startingPage8474
prism.volume144
dc.identifier.doi10.17863/CAM.85378
dcterms.dateAccepted2022-04-18
rioxxterms.versionofrecord10.1021/jacs.2c02287
rioxxterms.versionVoR
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidChen, Xiaoyi [0000-0001-9833-1390]
dc.contributor.orcidScherman, Oren A [0000-0001-8032-7166]
dc.identifier.eissn1520-5126
pubs.funder-project-idEuropean Commission Horizon 2020 (H2020) Marie Sk?odowska-Curie actions (845640)
pubs.funder-project-idEPSRC (2342310)
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/L027151/1)
pubs.funder-project-idEuropean Research Council (726470)
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/R512461/1)
cam.issuedOnline2022-05-10


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International