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Enzymatic transhalogenation of dendritic RGD peptide constructs with the fluorinase
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dc.contributor.author | Thompson, Stephen | |
dc.contributor.author | Fleming, Ian | |
dc.contributor.author | O'Hagan, David | |
dc.date.accessioned | 2017-02-16T00:32:50Z | |
dc.date.available | 2017-02-16T00:32:50Z | |
dc.date.issued | 2016-03-21 | |
dc.identifier.citation | Thompson , S , Fleming , I & O'Hagan , D 2016 , ' Enzymatic transhalogenation of dendritic RGD peptide constructs with the fluorinase ' , Organic & Biomolecular Chemistry , vol. 14 , no. 11 , pp. 3120-3129 . https://doi.org/10.1039/C6OB00239K | en |
dc.identifier.issn | 1477-0520 | |
dc.identifier.other | PURE: 240913136 | |
dc.identifier.other | PURE UUID: 53626e4e-2a00-463e-91d9-0e933e211d19 | |
dc.identifier.other | Scopus: 84960510773 | |
dc.identifier.other | WOS: 000372175300016 | |
dc.identifier.other | ORCID: /0000-0002-0510-5552/work/68281208 | |
dc.identifier.uri | http://hdl.handle.net/10023/10303 | |
dc.description | The authors thank EPSRC and the Scottish Imaging Network (SINAPSE) for grants. DO’H thanks the Royal Society for a Wolfson Research Merit Award and ST is grateful to the John and Kathleen Watson Scholarship for financial support. | en |
dc.description.abstract | The substrate scope of fluorinase enzyme mediated transhalogenation reactions is extended. Substrate tolerance allows a peptide cargo to be tethered to a 5'-chloro-5'-deoxynucleoside substrate for transhalogenation by the enzyme to a 5'-fluoro-5'-deoxynucleoside. The reaction is successfully extended from that previously reported for a monomeric cyclic peptide (cRGD) to cargoes of dendritic scaffolds carrying two and four cyclic peptide motifs. The RGD peptide sequence is known to bind upregulated αVβ3 integrin motifs on the surface of cancer cells and it is demonstrated that the fluorinated products have a higher affinity to αVβ3 integrin than their monomeric counterparts. Extending the strategy to radiolabelling of the peptide cargoes by tagging the peptides with [18F]fluoride was only moderately successful due to the poor water solubility of these higher order peptide scaffolds although the strategy holds promise for peptide constructs with improved solubility. | |
dc.language.iso | eng | |
dc.relation.ispartof | Organic & Biomolecular Chemistry | en |
dc.rights | Copyright 2016 the Authors. 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/10.1039/C6OB00239K | en |
dc.rights | Copyright 2016 the Authors. 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/10.1039/C6OB00239K | en |
dc.subject | Fluorinase enzyme | en |
dc.subject | Fluorination | en |
dc.subject | cRGD dendrimers | en |
dc.subject | αVβ3 integrins | en |
dc.subject | [18F]fluoride | en |
dc.subject | QD Chemistry | en |
dc.subject | NDAS | en |
dc.subject | SDG 3 - Good Health and Well-being | en |
dc.subject.lcc | QD | en |
dc.title | Enzymatic transhalogenation of dendritic RGD peptide constructs with the fluorinase | en |
dc.type | Journal article | en |
dc.contributor.sponsor | EPSRC | en |
dc.contributor.sponsor | EPSRC | en |
dc.description.version | Postprint | en |
dc.description.version | Postprint | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1039/C6OB00239K | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | EP/I034734/1 | en |
dc.identifier.grantnumber | EP/M01262X/1 | en |
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