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Updated: Aug 20, 2026

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry
Published on: June 8, 2021
Mass spectrometric characterization of peptides derived by peptic cleavage of bovine beta-casein
Christian E H Schmelzer1, Regina Schöps, Renate Ulbrich-Hofmann
1Institute of Pharmaceutics and Biopharmaceutics, Martin Luther University Halle-Wittenberg, Wolfgang-Langenbeck-Strasse 4, 06120 Halle (Saale), Germany.
Abstract:
This study investigated the digestion of the milk protein beta-casein with pepsin under gastro-analogous conditions. Peptide sequences were identified using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with post-source decay as well as liquid chromatography-tandem mass spectrometry by means of database searching. The new software tool, Mascot Distiller, improved the identification rate remarkably. In the case of small peptides, such as di- and tri-peptides, which are promising candidates for intestinal absorption and possible biological effects, identification was possible only after spectrum simulation and manual matching. A list of 41 identified peptides having 2-36 amino acids is given, and unexpected cleavage sites for pepsin are reported. Sequence coverage was 75%.
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