To identify selectively interacting proteins of a drug molecule, it is coupled to caprotec’s Capture Compound scaffold and incubated with human cell lysates, subcellular fractions or whole cells.
Later, interacting proteins are isolated and identified via Liquid Chromatography-Mass Spectrometry/Mass. Among the protein targets that demonstrated specific binding of Roche’s drug molecule were some which show activity in pathways commensurate with the phenotypic profile of the candidate drug molecule.
Hubert Koster, CEO of caprotec, said: “The results of this drug-protein profiling study confirm again the capability of our CCMS technology to directly isolate a functional subset of proteins from a complex biological sample for the identification of previously unknown interactions with small molecules.
“This fills a crucial technological gap in the arsenal of methods available for optimizing drug structures and to select the most promising candidate drugs before entering the clinical trial process as well as drug safety assessment.”
Stephan Rover, scientific expert for discovery chemistry at Roche, said: “This project demonstrated that the CCMS technology is robust and yields high quality results that are complementary to our internal research efforts. We are very pleased with the outcome of this collaboration.”