Analysis of primary structure of peptides and proteins – University of Copenhagen

Analysis of primary structure of peptides and proteins

The lab has a broad expertise in determination of primary peptide and proteins structure. A detailed in-depth characterization of peptide and protein primary structure including their covalent modifications and degradations and product related impurities is obtained by applying LC-MS, MALDI-MS, MS/MS techniques.

Figure 1. Using liquid chromatography and mass spectrometry for detailed characterisation of protein primary structure, including the nature and location of modifications and degradations. (Leurs et al., Eur. J. Pharm. Biopharm 2015)

Current LC-MS projects and expertise in the lab:

  • Development of MS workflows for quality control of peptides and protein drugs
  • Intact mass and top-down analysis MALDI-TOF and high-resolution QTOF mass spectrometry
  • Peptide mapping (bottom-up) by LC-MS to determine protein sequence
  • Identification of covalent modifications and degradations and determination of the location and extent of these
  • Enzymatic treatment of proteins combined with MS workflows

Figure 2. Detailed characterization of the glycan structure and disulfide bond connectivity of proteins of pharmaceutical interest. (Trabjerg et al., J. Biol. Chem 2017)

Figure 3. Experiments for analysis of protein primary structure performed on the MALDI-MS instrument in the lab.