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dc.contributor.authorZhang, Qingzhi
dc.contributor.authorDall'Angelo, Sergio
dc.contributor.authorFleming, Ian N.
dc.contributor.authorSchweiger, Lutz F.
dc.contributor.authorZanda, Matteo
dc.contributor.authorO'Hagan, David
dc.date.accessioned2017-07-04T23:33:39Z
dc.date.available2017-07-04T23:33:39Z
dc.date.issued2016-07-25
dc.identifier.citationZhang , Q , Dall'Angelo , S , Fleming , I N , Schweiger , L F , Zanda , M & O'Hagan , D 2016 , ' Last-step enzymatic [ 18 F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers ' Chemistry - A European Journal , vol. 22 , no. 31 , pp. 10998–11004 . https://doi.org/10.1002/chem.201601361en
dc.identifier.issn1521-3765
dc.identifier.otherPURE: 244261593
dc.identifier.otherPURE UUID: 86cc3506-1f1a-4684-be5b-c903ca067fac
dc.identifier.otherBibtex: urn:a60426cbb295a36e5f8da8c8cfbdf064
dc.identifier.otherScopus: 84978919513
dc.identifier.urihttp://hdl.handle.net/10023/11146
dc.descriptionWe thank the Engineering and Physical Sciences Research Council, UK, for a research grant.en
dc.description.abstractWe report a last-step fluorinase-catalyzed [18F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [18F]-radiolabeled RGD peptides, which retained high affinity to cancer-cell relevant αvβ3 integrins.
dc.language.isoeng
dc.relation.ispartofChemistry - A European Journalen
dc.rights© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://dx.doi.org/10.1002/chem.201601361en
dc.subject18F labelingen
dc.subjectBarbas linkeren
dc.subjectBioconjugationen
dc.subjectChemical biologyen
dc.subjectRGD peptideen
dc.subjectQD Chemistryen
dc.subjectNDASen
dc.subject.lccQDen
dc.titleLast-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkersen
dc.typeJournal articleen
dc.description.versionPostprinten
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1002/chem.201601361
dc.description.statusPeer revieweden
dc.date.embargoedUntil2017-07-04


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