Protein labeling with the labeling precursor [18F]SiFA-SH for positron emission tomography

Proteins previously derivatized with the cross-coupling reagent sulfo-SMCC (4-(N-maleimidomethyl)cyclohexane-1-carboxylic acid 3-sulfo-N-hydroxy-succinimide ester sodium salt) can be easily labeled in high radiochemical yields with the silicon-fluoride acceptor (SiFA) reagent [18F]SiFA-SH, obtained...

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Bibliographic Details
Main Authors: Wängler, Björn (Author) , Niedermoser, Sabrina (Author) , Wängler, Carmen (Author)
Format: Article (Journal)
Language:English
Published: 04 October 2012
In: Nature protocols
Year: 2012, Volume: 7, Issue: 11, Pages: 1964-1969
ISSN:1750-2799
DOI:10.1038/nprot.2012.111
Online Access:Verlag, Volltext: http://dx.doi.org/10.1038/nprot.2012.111
Verlag, Volltext: https://www.nature.com/articles/nprot.2012.111
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Author Notes:Björn Wängler, Alexey P. Kostikov, Sabrina Niedermoser, Joshua Chin, Katy Orchowski, Esther Schirrmacher, Liuba Iovkova-Berends, Klaus Jurkschat, Carmen Wängler, Ralf Schirrmacher
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Summary:Proteins previously derivatized with the cross-coupling reagent sulfo-SMCC (4-(N-maleimidomethyl)cyclohexane-1-carboxylic acid 3-sulfo-N-hydroxy-succinimide ester sodium salt) can be easily labeled in high radiochemical yields with the silicon-fluoride acceptor (SiFA) reagent [18F]SiFA-SH, obtained via isotopic exchange, by thiol-maleimide coupling chemistry (n = 10). The specific activity of SiFA-SH obtained in a one-step labeling reaction was >18.5 GBq μmol−1 (>500 Ci mmol−1). The number of SiFA building blocks per protein molecule is defined by the previously introduced number of maleimide groups, which can be determined by a simple and convenient Ellman's assay. Not more than two maleimide groups are introduced using sulfo-SMCC, thereby keeping the modification of the protein low and preserving its biological activity.
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Physical Description:Online Resource
ISSN:1750-2799
DOI:10.1038/nprot.2012.111