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Titles listRegulation of the HLA-B27 / TCR interaction by enzymatically stable β-peptidic peptidomimetics
Titles listRegulation of the HLA-B27 / TCR interaction by enzymatically stable β-peptidic peptidomimetics
Doctoral Thesis
unige:47384 
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Regulation of the HLA-B27 / TCR interaction by enzymatically stable β-peptidic peptidomimetics |
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| Defense | Thèse de doctorat : Univ. Genève, 2014 - Sc. 4766 - 2014/05/22 | |
| Abstract | The aim of the present study was to analyze the interactions between HLA-B27-binding β-octa- and β-nona-peptides, which may contain up to three α amino-acid residues, and the cognate T-cell receptor specifically targeting the dominant HIV-derived HLA-B27-restricted viral epitope KK10 (KRWIILGLNK). To this end, the IFNγ production by the T cells was quantified by ELISPOT assays in the presence or absence of several β-peptidic compounds, designed to bind to B27, and to study the interference with TCR recognition. In the presence of the B27-KK10 natural α-peptide IFNγ secretion by the CD8+ T-cell line was observed at millimolar concentrations. In contrast, a dose-dependent reduction of IFNγ secretion was found, following co-incubation with HLA-B27 specific β-peptides.Suppression of T cell activity was demonstrated starting at 10-fold higher concentrations of the β-peptidic additives as compared to the α-peptide. Certain α- and β-peptides, which did not interfere with the IFNγ response of HLA-B27-restricted CD8+ T cells, were used as negative controls. | |
| Keywords | Peptide — ELISPOT — Immunology — HLA-B27 — Peptidomimetics — TCR — B27-KK10 — β-peptidic compounds | |
| Identifiers | URN: urn:nbn:ch:unige-473848 | |
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| Research group | Groupe Seebach Jorg Dieter (transplantation et immunologie) (856) | |
| Citation (ISO format) | HEYRANI NOBARI, Ruhollah. Regulation of the HLA-B27 / TCR interaction by enzymatically stable β-peptidic peptidomimetics. Université de Genève. Thèse, 2014. https://archive-ouverte.unige.ch/unige:47384 |
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