We are always looking to collaborate
We value collaboration in our group. More than 90% of our published
work has been done with at least one collaborator, from either
academia or industry.
We are open to collaborate, support, teach and learn, to increase the
depth of our research and that of others. Feel free to contact us to
talk about how we can benefit from each other’s knowledge and
resources.
The BioMS group offers access to it’s collaborators to high-end
technologies and data analysis infrastructure, and will be given
support for design, execution and interpreting of their research.
Each project will be custom made planned and organized, to
ensure the most optimal protocol for the specific samples or
research questions.
Optimized for your Question
Quantitative proteomics
Quantitative proteomics uses mass spectrometry to identify and measure the abundance of thousands of proteins within a biological sample simultaneously. This is typically achieved through approaches such as label-free quantification or isotope labeling, which allow comparison across different conditions or time points. The technique provides a global view of protein expression, enabling the understanding how cells respond to stimuli, disease, or treatment. It is most often used in projects focusing on biomarker discovery, drug response studies, and systems biology. By capturing proteome-wide changes, it helps link molecular alterations to biological function.
Post-Translational Modifications
Mass spectrometry is highly effective for detecting and quantifying post-translational modifications, which are chemical changes that occur to proteins after synthesis. These include phosphorylation, glycosylation, ubiquitination, or acetylation, all of which regulate protein activity, localization, and interactions. Optimized enrichment strategies are used to isolate modified peptides before analysis, including Fe-IMAC or TiO2 enrichment. This approach allows precise mapping of modification sites and their relative abundance under different conditions. Studying PTMs is used in projects to understand signaling pathways, disease mechanisms, and regulatory processes at the molecular level.
Affinity Purification-MS
Affinity purification coupled with mass spectrometry (AP-MS) is used to identify protein–protein interactions within cells. In this method, a target protein is selectively isolated along with its binding partners using specific affinity tags or antibodies. The co-purified proteins are then analyzed by mass spectrometry to determine the composition of protein complexes. This approach is used in projects focusing on mapping interaction networks and identifying functional partners of proteins. It is particularly valuable for studying signaling pathways, molecular complexes, and mechanisms of disease.
Immune Peptidomics
Mass spectrometry-based immune peptidomics focuses on identifying peptides presented by human leukocyte antigen (HLA) molecules on cell surfaces. These peptides represent fragments of intracellular proteins and are crucial for immune system recognition. By isolating HLA complexes and analyzing the bound peptides, it can be determined which antigens are being presented. This technique is used in projects of cancer immunotherapy, vaccine development, and infectious disease research. It enables the discovery of neoantigens and other immune targets for personalized medicine.
Characterization of intact protein complexes
Mass spectrometry can also be used to analyze intact protein complexes in their native or near-native states, often referred to as native mass spectrometry. This approach preserves non-covalent interactions, allowing the study of the composition, stoichiometry, and architecture of protein assemblies. It provides insight into how proteins interact within complexes and how these interactions change under different conditions. Such analysis can be used in projects understanding molecular machines like ribosomes, proteasomes, and signaling complexes. It can be used to study protein complex formation and stability.
