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 (H2 18O) of [ 18F]fluoride generated by the cyclotron and has the capacity to isotopically label peptides of choice for positron emission tomography (PET).
|Number of pages||6|
|Journal||Angewandte Chemie International Edition|
|Early online date||2 Jul 2014|
|Publication status||Published - 18 Aug 2014|
- bioconjugated peptides
- enzyme catalysis
- positron emission tomography
FingerprintDive into the research topics of 'A localized tolerance in the substrate specificity of the fluorinase enzyme enables "last-step" 18F fluorination of a RGD peptide under ambient aqueous conditions'. Together they form a unique fingerprint.
- School of Medicine, Medical Sciences & Nutrition, Medical Education - Senior Lecturer (Scholarship)
- Institute of Medical Sciences
- Aberdeen Biomedical Imaging Centre
Person: Academic Related - Scholarship