Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers
View/ Open
Date
25/07/2016Author
Grant ID
EP/I034734/1
EP/M01262X/1
Keywords
Metadata
Show full item recordAbstract
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.
Citation
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 . https://doi.org/10.1002/chem.201601361
Publication
Chemistry - A European Journal
Status
Peer reviewed
ISSN
1521-3765Type
Journal article
Description
We thank the Engineering and Physical Sciences Research Council, UK, for a research grant.Collections
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.