News
Cisplatin is the most widely used anti-cancer drug, and the side-effects of cisplatin chemotherapy are largely due to side reactions of cisplatin with other molecules in the body, chiefly proteins. In a joint publication between the O'Connor group and the Sadler group, it's reported that the anticancer drug, cisplatin, can act as a protein crosslinker which is of use in the field of proteomics. Cisplatin has novel features as a protein crosslinker: 1) it's charged, so it improves the sensitivity of any modified peptides over non-reacted peptides, 2) it targets methionine and histidine primarily, which are residues that are not targetted by traditional crosslinkers, 3) it has an unusual isotopic pattern compared to typical peptides or peptide crosslinkers, which can be used as a signature to flag those peptides which are modified with platinum, 4) it has a fixed arm-length of about 4.5 Angstroms, but has the potential for addition of other chemical moities to extend the arm-length. This observation allows new kinds of proteomics that focuses on those proteins which are modified by cisplatin directly - thus potentially profiling all molecules which are directly responsible for the deleterious side-effects in chemotherapy. This paper has just been published in Analytical Chemistry: http://pubs.acs.org/doi/abs/10.1021/ac200861k