| dc.rights.license | CC-BY-NC-ND | |
| dc.contributor.advisor | Stahl, B. | |
| dc.contributor.author | Cerezin, Lara | |
| dc.date.accessioned | 2025-02-07T01:00:56Z | |
| dc.date.available | 2025-02-07T01:00:56Z | |
| dc.date.issued | 2025 | |
| dc.identifier.uri | https://studenttheses.uu.nl/handle/20.500.12932/48490 | |
| dc.description.sponsorship | Utrecht University | |
| dc.language.iso | EN | |
| dc.subject | This study explores how the cow's milk allergen beta-lactoglobulin is processed by B-lymphocytes. Using a mass spectrometry-based approach, peptides from beta-lactoglobulin were analyzed in B-lymphocytes after immunoprecipitation. The study successfully optimized methodology by reducing polyethylene glycol contamination and bovine-derived peptide interference, highlighting the need for further optimization to compare non-modified and glycan-modified BLG presentation. | |
| dc.title | Optimizing Mass Spectrometry Analysis for HLA-DR Proteomics: Insights into BLG-Derived Peptide Presentation and PEG Contamination Mitigation | |
| dc.type.content | Master Thesis | |
| dc.rights.accessrights | Open Access | |
| dc.subject.keywords | food allergy; cow’s milk allergy; B-lymphocytes; beta-lactoglobulin; HLA-DR peptide presentation; immunopeptidomics; polyethylene glycol; proteomics; mass spectrometry | |
| dc.subject.courseuu | Drug Innovation | |
| dc.thesis.id | 42852 | |
