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A localized tolerance in the substrate specificity of the fluorinase enzyme enables "last-step" 18F fluorination of a RGD peptide under ambient aqueous conditions
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dc.contributor.author | Thompson, Stephen | |
dc.contributor.author | Zhang, Qingzhi | |
dc.contributor.author | Ónega, Mayca | |
dc.contributor.author | McMahon, Stephen | |
dc.contributor.author | Fleming, Ian | |
dc.contributor.author | Ashworth, Sharon | |
dc.contributor.author | Naismith, Jim | |
dc.contributor.author | Passchier, Jan | |
dc.contributor.author | O'Hagan, David | |
dc.date.accessioned | 2015-07-01T23:10:40Z | |
dc.date.available | 2015-07-01T23:10:40Z | |
dc.date.issued | 2014-08-18 | |
dc.identifier | 159437966 | |
dc.identifier | 7352c66b-d385-499d-89e5-8ecbf6d5179f | |
dc.identifier | 84906101904 | |
dc.identifier | 000340526400013 | |
dc.identifier.citation | Thompson , S , Zhang , Q , Ónega , M , McMahon , S , Fleming , I , Ashworth , S , Naismith , J , Passchier , J & O'Hagan , D 2014 , ' A localized tolerance in the substrate specificity of the fluorinase enzyme enables "last-step" 18 F fluorination of a RGD peptide under ambient aqueous conditions ' , Angewandte Chemie International Edition , vol. 53 , no. 34 , pp. 8913-8918 . https://doi.org/10.1002/anie.201403345 | en |
dc.identifier.issn | 1433-7851 | |
dc.identifier.other | ORCID: /0000-0002-0510-5552/work/68281238 | |
dc.identifier.uri | https://hdl.handle.net/10023/6894 | |
dc.description | The authors thank the ERC, EPSRC and the Scottish Imaging Network (SINAPSE) for grants, and the John and Kathleen Watson Scholarship (S.T.) for financial support. | en |
dc.description.abstract | A strategy for last-step 18F fluorination of bioconjugated peptides is reported that exploits an “Achilles heel” in the substrate specificity of the fluorinase enzyme. An acetylene functionality at the C-2 position of the adenosine substrate projects from the active site into the solvent. The fluorinase catalyzes a transhalogenation of 5′-chlorodeoxy-2-ethynyladenosine (ClDEA) to 5′-fluorodeoxy-2-ethynyladenosine (FDEA). Extending a polyethylene glycol linker from the terminus of the acetylene allows the presentation of bioconjugation cargo to the enzyme for 18F labelling. The method uses an aqueous solution (H218O) of [18F]fluoride generated by the cyclotron and has the capacity to isotopically label peptides of choice for positron emission tomography (PET). | |
dc.format.extent | 6 | |
dc.format.extent | 1002238 | |
dc.language.iso | eng | |
dc.relation.ispartof | Angewandte Chemie International Edition | en |
dc.subject | Bioconjugated peptides | en |
dc.subject | Enzyme catalysis | en |
dc.subject | Fluorinase | en |
dc.subject | Fluorine-18 | en |
dc.subject | Positron emission tomography | en |
dc.subject | QD Chemistry | en |
dc.subject | BDC | en |
dc.subject | R2C | en |
dc.subject.lcc | QD | en |
dc.title | A localized tolerance in the substrate specificity of the fluorinase enzyme enables "last-step" 18F fluorination of a RGD peptide under ambient aqueous conditions | en |
dc.type | Journal article | en |
dc.contributor.sponsor | EPSRC | en |
dc.contributor.sponsor | BBSRC | 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/10.1002/anie.201403345 | |
dc.description.status | Peer reviewed | en |
dc.date.embargoedUntil | 2015-07-02 | |
dc.identifier.url | http://onlinelibrary.wiley.com/doi/10.1002/anie.201403345/suppinfo | en |
dc.identifier.grantnumber | EP/I034734/1 | en |
dc.identifier.grantnumber | BB/C000080/1 | en |
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