Combined Mass Spectrometry System - Drug Discovery and Development

BioTrove, Inc. presented data at the 57th American Society for Mass Spectrometry Conference on Mass Spectrometry in Philadelphia, Pennsylvania demonstrating the compatibility of its RapidFire Mass Spectrometry (RF-MS) system with Agilent Technologies Inc.’s Time-of-Flight (TOF) mass spectrometer system for high-throughput screening of protein inhibitors and examination of drug-drug interaction assays. Combining the two platforms, drug discovery researchers can now perform high-throughput drug-drug interaction and label-free kinase assays using whole protein substrates.

These data were presented by Drs. William A. LaMarr and Michelle V. Romm. Dr. LaMarr showed that the RapidFire/Time-of-Flight system provides researchers accurate mass data for high-throughput analysis of CYP inhibition assays. The use of accurate mass measurements afforded by the Agilent TOF-MS has the potential to streamline the workflow in other in vitro ADME applications such as metabolic stability assays by eliminating the bottleneck of MS method development.

Dr. Romm’s presentation demonstrated that the RapidFire/Time-of-Flight system provides a high-throughput screening interface for the label-free detection of whole protein kinase activity at per sample throughputs under 10 seconds. The ability to use whole protein substrates in kinase assays enables researchers to investigate challenging kinase targets, such as those that have multiple phosphorylation sites or kinases that auto-phosphorylate, that are problematic to study with optical or radiometric assay formats.

The integration of RapidFire with Agilent’s state-of-the-art Time-of-Flight technology provides scientists a new tool to accelerate and expand on possibilities in drug discovery and disease research. These combined technologies provide scientists an end-to-end solution for high-throughput drug discovery and ADME screening.

The RapidFire/Time-of-Flight system allows for the analysis of whole proteins in their native state, rather than fragmented peptide substrates, including methylases and demethylases, ubiquitinases, acetylases and deacetylases, kinases, and phosphatases.

Source: Biotrove