Targeted protein quantitation by MS: strategies to achieve increased selectivity
Targeted protein quantitation by LC–MS of both endogenous and exogenous (therapeutic) proteins is an increasingly important technique in bioanalysis. In comparison to traditionally utilized immunochemical approaches, the methodology allows for a faster method development, a reduced need for specific reagents, and affords multiplexed analyses. The required selectivity against the very high biological background is commonly achieved by multiple reaction monitoring on triple quadrupole or Q-Trap instruments, however, on occasion the selectivity afforded is insufficient. This presentation will demonstrate the application of MS3, SelexIon and HR-MS to increase the selectivity in these analyses in selected case studies.
What you will learn?
- Introduction to targeted protein quantitation
- Typical performance of a targeted MS assay for protein quantitation
- Method creation and optimization of MS parameters: MRM, MS3 and SelexIon
- Advantages and disadvantages of the methodologies
Who may this interest?
- Small molecule (LC–MS) bioanalysts with an interest in large molecule quantitation
- Bioanalysts with a background in ligand-binding assays with an interest in mass spectrometry
Following a first degree in Pharmaceutical Chemistry (Fachhochschule Isny, Germany), and MSc and PhD degrees in Pharmaceutical Analysis (University of Strathclyde, Glasgow), Mark held research positions at Merck&Co (Italy), Novo Nordisk (Denmark) and Proximagen (UK). Mark’s current role with UCB Celletch (UK) allows him to pursue his interest in applying advanced mass spectrometric techniques to current bioanalytical challenges, both for small and large molecules, and in broadening the strategic input of bioanalytical sciences to the discovery and development of new medicines.
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