Our latest pre-print is now online, where we evaluated two peptide ligands of the cardiac ryanodine receptor (RyR) as super-resolution imaging probes. The research was conducted in collaboration with one of our industrial partners, Badrilla Ltd., during the industrial internship of iCASE PhD student Tom Sheard funded through the DiMeN DTP.
The peptides used were the scorpion venom toxin imperacalcin, and CPVT-mimicking DPc10. We evaluated the specificity of the fluorescent peptide conjugates for the target RyR2 in fluorescent imaging experiments, in terms of colocalisation with RyR2 immunolabelling, with confocal and expansion microscopy.
We also performed structural work looking at the DPc10 binding site on RyR2 atomic models to learn more about the peptide’s mechanism of disturbance (DPc10 binding to RyR2 causes domain unzipping and destabilises the channel).
Thanks to the host company Badrilla, the DiMeN DTP for funding Tom’s industrial placement, and the other authors for help with the research.
Access the pre-print in bioRxiv at: https://www.biorxiv.org/content/10.1101/2020.06.26.131854v1.
Feedback on all contents of the work is welcomed.
Follow Tom on twitter : @tmdsheard. https://twitter.com/TMDSheard