The first enzymatic method for C–18F bond formation: the synthesis of 5′‐[18F]‐fluoro‐5′‐deoxyadenosine for imaging with PET

Laurent Martarello (Corresponding Author), Christoph Schaffrath, Hai Deng, Antony D. Gee, Andrew Lockhart, David O’Hagan (Corresponding Author)

Research output: Contribution to journalArticle

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Abstract

The use of the key enzyme involved in carbon–fluorine bond formation in Streptomyces cattleya catalysing the formation of 5′‐fluoro‐5′‐deoxyadenosine (5′‐FDA) from fluoride ion and S‐adenosyl‐l‐methionine (SAM) was explored for its potential application in fluorine‐18 labelling of the adenosine derivative. Enzymatic radiolabelling of [18F]‐5′‐FDA was successfully carried out starting from SAM and [18F]HF when the concentration of the enzyme preparation was increased from sub‐mg/ml values to mg/ml values. The purity of the enzyme had no measurable effect on the radiochemical yield of the reaction and the radiochemical purity of [18F]‐5′‐FDA. Copyright © 2003 John Wiley & Sons, Ltd.
Original languageEnglish
Pages (from-to)1181-1189
Number of pages9
JournalJournal of Labelled Compounds and Radiopharmaceuticals
Volume46
Issue number13
Early online date8 Oct 2003
DOIs
Publication statusPublished - Nov 2003

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Imaging techniques
Enzymes
Streptomyces
Fluorides
Adenosine
Labeling
Ions
Derivatives

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The first enzymatic method for C–18F bond formation: the synthesis of 5′‐[18F]‐fluoro‐5′‐deoxyadenosine for imaging with PET. / Martarello, Laurent (Corresponding Author); Schaffrath, Christoph ; Deng, Hai; Gee, Antony D.; Lockhart, Andrew; O’Hagan, David (Corresponding Author).

In: Journal of Labelled Compounds and Radiopharmaceuticals, Vol. 46, No. 13, 11.2003, p. 1181-1189.

Research output: Contribution to journalArticle

Martarello, Laurent ; Schaffrath, Christoph ; Deng, Hai ; Gee, Antony D. ; Lockhart, Andrew ; O’Hagan, David. / The first enzymatic method for C–18F bond formation: the synthesis of 5′‐[18F]‐fluoro‐5′‐deoxyadenosine for imaging with PET. In: Journal of Labelled Compounds and Radiopharmaceuticals. 2003 ; Vol. 46, No. 13. pp. 1181-1189.
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abstract = "The use of the key enzyme involved in carbon–fluorine bond formation in Streptomyces cattleya catalysing the formation of 5′‐fluoro‐5′‐deoxyadenosine (5′‐FDA) from fluoride ion and S‐adenosyl‐l‐methionine (SAM) was explored for its potential application in fluorine‐18 labelling of the adenosine derivative. Enzymatic radiolabelling of [18F]‐5′‐FDA was successfully carried out starting from SAM and [18F]HF when the concentration of the enzyme preparation was increased from sub‐mg/ml values to mg/ml values. The purity of the enzyme had no measurable effect on the radiochemical yield of the reaction and the radiochemical purity of [18F]‐5′‐FDA. Copyright {\circledC} 2003 John Wiley & Sons, Ltd.",
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