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Last‐Step Enzymatic [ 18 F]‐Fluorination of Cysteine‐Tethered RGD Peptides Using Modified Barbas Linkers
Author(s) -
Zhang Qingzhi,
Dall'Angelo Sergio,
Fleming Ian N.,
Schweiger Lutz F.,
Zanda Matteo,
O'Hagan David
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201601361
Subject(s) - linker , cysteine , peptide , chemistry , moiety , substrate (aquarium) , combinatorial chemistry , peg ratio , integrin , enzyme , stereochemistry , biochemistry , cell , oceanography , finance , computer science , economics , geology , operating system
We report a last‐step fluorinase‐catalyzed [ 18 F]‐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 [ 18 F]‐radiolabeled RGD peptides, which retained high affinity to cancer‐cell relevant α v β 3 integrins.
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