Development of ultrahigh resolution FTICR mass spectrometry methods for clinical proteomics

Abstract

Fourier transform ion cyclotron resonance (FTICR) MS provides (a) ultrahigh mass resolving power that allows the analysis of large proteins and complex mixtures; (b) ultrahigh mass measurement accuracy and precision that allow a more reliable identification of the detected species; (c) a wide dynamic range that is favourable for the detection of low abundant components. Despite these excellent characteristics, MALDI-FTICR MS has been rarely used for peptide and protein profiling of large cohorts of samples. In this thesis, the development and application of novel MALDI-FTICR-MS methods for high-throughput analysis of human serum peptides and proteins is described. Due to the large biological variability of human serum, the analysis of a large cohort is needed to obtain reliable statistical results.