Chemoenzymatic n.c.a synthesis of the coenzyme UDP-2-deoxy-2-[18F]fluoro-α-D-glucopyranose as substrate of glycosyltransferases
✍ Scribed by Olaf Prante; Kurt Hamacher; Heinz H. Coenen
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- French
- Weight
- 156 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0022-2135
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✦ Synopsis
Abstract
The development of ^18^F‐labelling methods adopted to proteins and bioactive peptides is of great interest in radiopharmaceutical sciences. In order to provide ^18^F‐labelled sugars as a polar prosthetic group for an enzymatic ^18^F‐labelling procedure, an appropriate nucleotide activated sugar is needed. Here, we present the radiosynthesis of n.c.a. UDP‐2‐deoxy‐2‐[^18^F]fluoro‐α‐D‐glucopyranose (UDP‐[^18^F]FDG) as a substrate for glycosyltransferases. The MacDonald synthesis of [^18^F]FDG‐1‐phosphate was successfully combined with an enzymatic activation to obtain UDP‐[^18^F]FDG directly in an aqueous medium located in the void volume of a solid phase cartridge. The radiochemical yield of UDP‐[^18^F]FDG was 20% (based on [^18^F]fluoride) after a total synthesis time of 110 min. Thus, an intermediate was provided for the enzymatic transfer of [^18^F]FDG using UDP‐[^18^F]FDG as glycosyl donor making use of a suitable glycosyltransferase. This would represent a highly selective and mild ^18^F‐labelling method for glycosylated biomolecules. Copyright © 2007 John Wiley & Sons, Ltd.