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Enzymatic transhalogenation of dendritic RGD peptide constructs with the fluorinase

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Dendrimer_Paper_Jan_2016.pdf (2.474Mb)
Date
21/03/2016
Author
Thompson, Stephen
Fleming, Ian
O'Hagan, David
Keywords
Fluorinase enzyme
Fluorination
cRGD dendrimers
αVβ3 integrins
[18F]fluoride
QD Chemistry
NDAS
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Abstract
The substrate scope of fluorinase enzyme mediated transhalogenation reactions is extended. Substrate tolerance allows a peptide cargo to be tethered to a 5'-chloro-5'-deoxynucleoside substrate for transhalogenation by the enzyme to a 5'-fluoro-5'-deoxynucleoside. The reaction is successfully extended from that previously reported for a monomeric cyclic peptide (cRGD) to cargoes of dendritic scaffolds carrying two and four cyclic peptide motifs. The RGD peptide sequence is known to bind upregulated αVβ3 integrin motifs on the surface of cancer cells and it is demonstrated that the fluorinated products have a higher affinity to αVβ3 integrin than their monomeric counterparts. Extending the strategy to radiolabelling of the peptide cargoes by tagging the peptides with [18F]fluoride was only moderately successful due to the poor water solubility of these higher order peptide scaffolds although the strategy holds promise for peptide constructs with improved solubility.
Citation
Thompson , S , Fleming , I & O'Hagan , D 2016 , ' Enzymatic transhalogenation of dendritic RGD peptide constructs with the fluorinase ' , Organic & Biomolecular Chemistry , vol. 14 , no. 11 , pp. 3120-3129 . https://doi.org/10.1039/C6OB00239K
Publication
Organic & Biomolecular Chemistry
Status
Peer reviewed
DOI
https://doi.org/10.1039/C6OB00239K
ISSN
1477-0520
Type
Journal article
Rights
Copyright 2016 the Authors. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://dx.doi.org/10.1039/C6OB00239K
 
Copyright 2016 the Authors. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://dx.doi.org/10.1039/C6OB00239K
Description
The authors thank EPSRC and the Scottish Imaging Network (SINAPSE) for grants. DO’H thanks the Royal Society for a Wolfson Research Merit Award and ST is grateful to the John and Kathleen Watson Scholarship for financial support.
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  • University of St Andrews Research
URI
http://hdl.handle.net/10023/10303

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