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
Publications
Albuquerque IS
(2015)
An artificial CO-releasing metalloprotein built by histidine-selective metallation.
in Chemical communications (Cambridge, England)
Alcock L
(2018)
Norbornene probes for the study of cysteine oxidation
Alcock L
(2018)
Norbornene probes for the study of cysteine oxidation
in Tetrahedron
Alcock LJ
(2019)
Norbornene Probes for the Detection of Cysteine Sulfenic Acid in Cells.
in ACS chemical biology
Amgarten B
(2015)
Collagen labelling with an azide-proline chemical reporter in live cells.
in Chemical communications (Cambridge, England)
Bernardim B
(2016)
Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents.
in Nature communications
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. |