Kiel Network of Analytical Spectroscopy and Mass Spectrometry

Systematic Proteomics and Bioanalytics

The research of the AG Systematic Proteome Research & Bioanalytics is focused on:

(A) Methodological and technological developments

Methodological and technological developments in the field of instrumental (bio)analytics, with a main focus on the coupling of ESI- and MALDI-mass spectrometry with multidimensional chromatography and the development and validation of novel analytical strategies for the analytics of peptides, proteins, peptidomes, proteomes, posttranslational modifications (e.g. phosphorylation, proteolytic processing (SFB 877), disulfide formation, and many others) and for other classes of biomolecules (e.g. metabolites).

Major topics are:

·multidimensional liquid chromatography coupled to ESI (Orbitrap or QExactive) MS, MALDI TOF/TOF MS, or ESI/MALDI ion mobility MS

  • top-down and bottom-up proteomics
  • isobaric labeling, metal labeling, label free quantification, bioinformatic methods
  • coupling of molecular (MALDI/ESI) and elemental (ICP) MS; LC-MALDI MS

       - methods for the analytics of posttranslational modifications

  • phosphorylation, proteolytic processing (SFB 877), disulfide bonds, oxidation, glycosylation, ubiquitinylation
  • fragmentation behavior in mass spectrometry (PSD, CID/HCD, ETD), enrichment techniques

       - methods for the characterization of bioactive peptides and for peptidomics 

       - novel matrices for MALDI MS: ionic liquid matrices

 (B) Application

The application of these analytical approaches on biological, biotechnological and biomedical problems, e.g.

  • the investigation of molecular events involved in inflammatory processes, in the frame of co-operations within the Cluster of Excellence “Inflammation@Interfaces”.
  • host-microbiota interactions (SFB 1182 - Origin and Function of Metaorganisms) and antimicrobial peptides,
  • recent applications as paleoproteomics.
  • the analysis of metabolites and their interaction with proteins both at single protein level and in molecular networks

 

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