ArticleJournal of immunological methods2016
Differential scanning fluorimetry based assessments of the thermal and kinetic stability of peptide-MHC complexes.
Article in Journal of immunological methods, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Duration of Initial Viremia Modulates Functional Properties of HIV-specific T Cell Receptors.Research square · 2026Article
- A Framework for Comparing Mouse Neoantigen Immunogenicity.bioRxiv : the preprint server for biology · 2026Article
- Duration of Initial Viremia Modulates Functional Properties of HIV-specific T Cell Receptors.bioRxiv : the preprint server for biology · 2026Article
- Computational Methods for Cancer Neoantigen Prediction.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Probing Thermal Transitions of Peptide-Major Histocompatibility Complexes by Differential Scanning Fluorimetry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- High-throughput screening for class I peptide MHC binding via yeast surface display.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Aurora 2.0: A fluorogenic dye library for expanding the capability of protein-adaptive differential scanning fluorimetry (paDSF).SLAS discovery : advancing life sciences R & D · 2025Article
- Identification and biophysical characterization of Plasmodium peptide binding by common African HLAs.Scientific reports · 2025Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Nature communications · 2025Article
- Polymorphic residues in HLA-B that mediate HIV control distinctly modulate peptide interactions with both TCR and KIR molecules.Structure (London, England : 1993) · 2024Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Research square · 2024Article
- Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024Review
- Structural and physical features that distinguish tumor-controlling from inactive cancer neoepitopes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange.Nature chemical biology · 2023Article
- High-throughput characterization of HLA-E-presented CD94/NKG2x ligands reveals peptides which modulate NK cell activation.Nature communications · 2023Article
- Intracellular trafficking of HLA-E and its regulation.The Journal of experimental medicine · 2023Article
- Effects of HLA single chain trimer design on peptide presentation and stability.Frontiers in immunology · 2023Article
- Impact of peptide:HLA complex stability for the identification of SARS-CoV-2-specific CD8Frontiers in immunology · 2023Article
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Authors and funding
10 authors.
Funding
Abstract
Measurements of thermal stability by circular dichroism (CD) spectroscopy have been widely used to assess the binding of peptides to MHC proteins, particularly within the structural immunology community. Although thermal stability assays offer advantages over other approaches such as IC50 measurements, CD-based stability measurements are hindered by large sample requirements and low throughput. Here we demonstrate that an alternative approach based on differential scanning fluorimetry (DSF) yields results comparable to those based on CD for both class I and class II complexes. As they require much less sample, DSF-based measurements reduce demands on protein production strategies and are amenable for high throughput studies. DSF can thus not only replace CD as a means to assess peptide/MHC thermal stability, but can complement other peptide-MHC binding assays used in screening, epitope discovery, and vaccine design. Due to the physical process probed, DSF can also uncover complexities not observed with other techniques. Lastly, we show that DSF can also be used to assess peptide/MHC kinetic stability, allowing for a single experimental setup to probe both binding equilibria and kinetics.
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