Chemical Proteomics Core Facility
Our facility is specialized in supporting drug discovery and development by identifying the key players of the drug/compound action, including direct and indirect interactions with the drug/compound as well as its mechanism of action.
What we offer
Our facility is specialized on the identification and characterization of proteins primarily involved in drug responses, including mechanism of actions and/or direct interactions, induced changes in proteome assembly and protein modification.
We can tailor our service on specific scientific goal(s) in the area of chemical proteomics, by providing and combining different methods.
Our current focus is unbiased mass spectrometry-based and proteome-wide approaches to probe the effects of small molecules, e.g. drugs compounds, on cells and organisms, as well as the properties of proteins using small molecules as probes. We have two unbiased quantitative proteomics methods which do not need any chemical modification of the drug/compound:
- FITExP (Functional Identification of Target by Expression Proteomics), recently invented in our laboratory, which enables to reveal target and mechanism of action proteins by studying the specific regulation of the proteome in response to a certain compound, e.g. the response of mammalian cancer cells to an anticancer drug.
- TPP (Thermal Protein Profiling), which enables the identification, throughout the whole proteome, of proteins with compound-induced variations in thermal stability, as potential direct or indirect players in the action of the drug/compound.
The combined application of FITExP and TPP provides unprecedented insight into the drug-target interactions and mechanism of action.
- Mass-spectrometry based proteomics for identification of compound-target interactions after affinity capture approaches
- Determination of the compound-protein binding site by hydrogen-deuterium exchange mass spectrometry (HDX MS).
Our services can include
- Consultation and experiment planning
- Cell culture and drug / compound treatments
- Cells / tissue sample processing, MS-based proteomics and identification of compounds-target(s) interactions and/or mechanism(s) of action
- Elucidation of interaction interface using hydrogen/deuterium exchange mass spectrometry
- MS-analysis and complete data analysis of results
- Functional data analysis and interpretation
- Tables and figures of final data
Study aims we can help you with
- Target Identification
- Discovery of Mechanism of Action
- Elucidation of Interaction Binding Site
- Change in Redox State
- Mechanism of Cell Death
- MS Orbitrap Q Exactive HF, Thermo Scientific
- MS Orbitrap Q Exactive Plus, Thermo Scientific
- MS Orbitrap Q Exactive, Thermo Scientific.
- MS Orbitrap Fusion, Thermo Scientific
- MS LTQ Orbitrap Elite, Thermo Scientific
Peptide separation technologies:
- HiRIEF (High Resolution Isoelectric Focusing)
- Liquid Chromatography (nanoUPLC/HPLC/FPLC)
How to book our service
Please feel free to contact us or come visit us to receive help and find out about feasibility and details for your project. We can customize and tailor our services on your specific case.
The Chemical Proteomics Core Facility is part of the national infrastructure for biological mass spectrometry BioMS. We can support your project and cover relevant costs of it by national funding.
Please submit your project request via the BioMS portal:
- Please tick "Chemical proteomics” in the application
- In the field BioMS contact, please specify: “Zubarev/Gaetani”
Department of Medical Biochemistry and Biophysics (MBB)
Biomedicum, A9, floor 9
171 65 Solna
The Chemical Proteomics Core Facility at Karolinska Institutet is located at the Department of Medical Biochemistry and Biophysics (MBB). Together with the Proteogenomics facility at SciLifeLab, we constitute the Chemical Proteomics & Proteogenomics facility, which is the Stockholm node of BioMS, the Swedish national infrastructure for biological mass spectrometry. We are part of the Division of Physiological Chemistry I, headed by Roman Zubarev.