EPSRC-Royal Society Fellowship Engagement (2013): Site-specific fluorination of peptides and proteins

Lead Research Organisation: University of Cambridge
Department Name: Chemistry

Abstract

Please refer to attached Royal Society application

Planned Impact

Please refer to attached Royal Society application
 
Description We have discovered a new method that enable the installation of a fluorine atom at a defined position within a protein structure. This now enables to create fluorinated proteins without disrupting the function of the protein. This chemistry was performed using F19. Efforts to translate this chemistry to "hot" F18 has not been successful however because of incompatible "hot" reaction conditions that led to protein denaturation. We continue our efforts in order to develop such a method in order to be to radiolabel tumour neovasculature specific antibodies to selectively image tumours in vivo using PET.
Exploitation Route The lessons we learn in terms of the requirements of selective fluorination - the need for late stage fluorination under mild conditions will guide us and others to develop such a method that if successful can be used with 18F and in combination with PET imaging be applied for the early detection of cancer.
Sectors Pharmaceuticals and Medical Biotechnology

 
Description We have discussed our data with pharmaceutical companies interested in fluorination. These were preliminary discussions and further discussions will happen once we are able to translate our cold to hot chemistry.
First Year Of Impact 2017
Sector Pharmaceuticals and Medical Biotechnology
 
Title Site-specific fluorination of proteins 
Description Our method involves the introduction of F19 site-specifically into a protein tagged with a non-canonical amino acid under biocompatible conditions. 
Type Of Material Technology assay or reagent 
Provided To Others? No  
Impact This method is not being translated into F18 with the hope to be useful to label proteins and antibodies specific for cancer without altering their targeting capacity.