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Dokument Type: Article
metadata.dc.title: Opening opportunities for Kd determination and screening of MHC peptide complexes
Authors: Kopicki, Janine-Denise 
Saikia, Ankur 
Niebling, Stephan 
Günther, Christian 
Anjanappa, Raghavendra 
Garcia-Alai, Maria 
Springer, Sebastian 
Uetrecht, Charlotte 
Institute: Fakultät V - Lebenswissenschaftliche Fakultät 
Free keywords: High-throughput screening, Mass spectrometry, MHC class I, Molecular biophysics
Dewey Decimal Classification: 610 Medizin, Gesundheit
GHBS-Clases: VVL
Issue Date: 2022
Publish Date: 2023
Source: Communications biology ; 5, article number 488. -
An essential element of adaptive immunity is selective binding of peptide antigens by major histocompatibility complex (MHC) class I proteins and their presentation to cytotoxic T lymphocytes. Using native mass spectrometry, we analyze the binding of peptides to an empty disulfide-stabilized HLA-A*02:01 molecule and, due to its unique stability, we determine binding affinities of complexes loaded with truncated or charge-reduced peptides. We find that the two anchor positions can be stabilized independently, and we further analyze the contribution of additional amino acid positions to the binding strength. As a complement to computational prediction tools, our method estimates binding strength of even low-affinity peptides to MHC class I complexes quickly and efficiently. It has huge potential to eliminate binding affinity biases and thus accelerate drug discovery in infectious diseases, autoimmunity, vaccine design, and cancer immunotherapy.
Finanziert im Rahmen der DEAL-Verträge durch die Universitätsbibliothek Siegen
URN: urn:nbn:de:hbz:467-24432
Appears in Collections:Geförderte Open-Access-Publikationen

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