Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers
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We 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.
Zhang , 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 . DOI: 10.1002/chem.201601361
Chemistry - A European Journal
© 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.201601361
DescriptionWe thank the Engineering and Physical Sciences Research Council, UK, for a research grant.
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