Inspired by challenging research questions in the field of life sciences, we introduce technologies for studying diverse complex and dynamic aspects of proteomes by means of mass spectrometry. We focus on the analysis of protein modifications such as protein processing by proteases and master the enrichment of protein N-terminal peptides, which report such processing events. Such N-terminal peptides are also the best proxies for modifications occurring on nascent protein chains.

In this respect, we study the N-terminal acetyltransferases that steer alpha-N-terminal protein acetylation in different model systems, including disease models, and characterize unexplored N-terminal proteoforms using novel protein-protein interaction technologies. Our N-terminome studies also led to an ongoing exploitation of a proteomic technology to identify disease-specific/-related proteins in complex matrices such as liquid biopsies. More recently we dived into the world of single-cell proteomics and have access to an automated sample prep station and a state-of-the-art mass spectrometer dedicated for such research.