Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/9153
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dc.contributor.authorHadeler, Andries-
dc.contributor.authorSaikia, Ankur-
dc.contributor.authorZacharias, Martin-
dc.contributor.authorSpringer, Sebastian-
dc.date.accessioned2024-12-17T03:12:34Z-
dc.date.available2024-12-17T03:12:34Z-
dc.date.issued2022-
dc.identifier.urihttp://localhost:8080/xmlui/handle/123456789/9153-
dc.description.abstractComplexes of peptides with recombinant major histocompatibility complex class I molecules (rpMHCs) are an important tool for T cell detection, isolation, and activation in cancer immunotherapy. The rapid preparation of rpMHCs is aided by peptide exchange, for which several technologies exist. Here, we show peptide exchange with small-molecule alcohols and demonstrate that they accelerate the dissociation of pre-bound peptides, creating a novel method for rapid production of rpMHCs and increasing the understanding of the conformational flexibility of the MHC-bound peptides.en_US
dc.subjectPeptide exchange Small molecule Major histocompatibility complex MHC class I Fluorescence anisotropy Nanoscale differential scanning fluorimetryen_US
dc.titleRapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptideen_US
dc.typeArticleen_US
Appears in Collections:VOL 3 2022

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