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RSS FeedsIJMS, Vol. 21, Pages 636: Disulfide-Linked Peptides for Blocking BTLA/HVEM Binding (International Journal of Molecular Sciences)

 
 

18 january 2020 16:02:08

 
IJMS, Vol. 21, Pages 636: Disulfide-Linked Peptides for Blocking BTLA/HVEM Binding (International Journal of Molecular Sciences)
 


Immune checkpoints are crucial in the maintenance of antitumor immune responses. The activation or blockade of immune checkpoints is dependent on the interactions between receptors and ligands; such interactions can provide inhibitory or stimulatory signals, including the enhancement or suppression of T-cell proliferation, differentiation, and/or cytokine secretion. B-and T-lymphocyte attenuator (BTLA) is a lymphoid-specific cell surface receptor which is present on T-cells and interacts with herpes virus item mediator (HVEM), which is present on tumor cells. The binding of HVEM to BTLA triggers an inhibitory signal which attenuates the immune response. This feature is interesting for studying the molecular interactions between HVEM and BTLA, as they may be targeted for novel immunotherapies. This work was based on the crystal structure of the BTLA/HVEM complex showing that BTLA binds the N-terminal cysteine-rich domain of HVEM. We investigated the amino acid sequence of HVEM and used molecular modeling methods to develop inhibitors of the BTLA/HVEM interaction. We synthesized novel compounds and determined their ability to interact with the BTLA protein and inhibit the formation of the BTLA/HVEM complex. Our results suggest that the HVEM (14–39) peptide is a potent inhibitor of the formation of the BTLA/HVEM protein complex.


 
171 viewsCategory: Biochemistry, Biophysics, Molecular Biology
 
IJMS, Vol. 21, Pages 638: Transcriptome Modifications in the Porcine Intramuscular Adipocytes during Differentiation and Exogenous Stimulation with TNF-? and Serotonin (International Journal of Molecular Sciences)
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