Richard King   Richard C. King, Ph.D., graduated from SUNY College of Environmental Science and Forestry at Syracuse with a B.S. in Chemistry in 1986. He obtained his Ph.D. in Analytical Chemistry from Drexel University. He joined the Department of Drug Metabolism at Merck Research Laboratories, West Point, Pennsylvania in 1994 where he worked in Preclinical Drug Metabolism with responsibilities related to bioanalysis and new technology development and implementation until 2008. In the fall of 2008 Dr. King became one of the founding members of PharmaCadence Analytical Services, LLC of Hatfield PA. Dr. King’s research interests cover a number of key areas in quantitative analysis by mass spectrometry including, ion formation mechanisms, ion chemistry, data processing, separation science, and automation.

Skyline: Everyday tool for protein quantification

Quantification of proteins and peptides by mass spectrometry is gaining utility in several areas of pharmaceutical and medical research. From therapeutic antibodies to endogenous peptide biomarkers, the importance of rapid and reliable protein and peptide quantification by LC-MS is changing the way pharmaceutical and medical researchers think about their studies. One of the functions of our analytical services company is to develop SRM assays for target proteins. The tool we routinely use to help rapidly develop these assays is Skyline. The workflow supported by Skyline has proven to be an effective and efficient way to develop useful quantitative LC-MS/MS protein assays. In addition to the use in targeted quantitative assay development, we also use Skyline to help characterize synthetic protein modifications often a key to successful biotherapeutic development. We present two examples of using Skyline in our daily work. The first is a description of assays developed to quantify several important UGT enzymes in human liver microsomes and the second is an example of using Skyline to characterize the relative extent of synthetic linker modification at lysine residues of a model protein.