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Stitched peptides as potential cell permeable inhibitors of oncogenic DAXX protein
DAXX (Death Domain Associated Protein 6), initially identified as a potentiator of apoptosis, is known to play crucial roles in several vital biological pathways, including chromatin remodeling, transcription regulation, DNA repair, and innate immunity. Its increased expression has been observed in diverse, epidemiologically prevalent cancers
ReadEngineering an Autonomous VH Domain to modulate intracellular pathways and to Interrogate the eIF4F Complex
Approaches have been devised to increase the discovery rate of intrabodies but often these yield results that aren’t functional in cells. Here the authors engineer and optimise an autonomous and disulphide-free human VH domain for intracellular expression, and they identify several VH domain binders against eIF4E.
ReadStructural insights reveal a recognition feature for tailoring hydrocarbon stapled-peptides against the eukaryotic translation initiation factor 4E protein
Stapled-peptides have emerged as an exciting class of molecules which can modulate protein–protein interactions. We have used a structure-guided approach to rationally develop a set of hydrocarbon stapled-peptides with high binding affinities and residence times against the oncogenic eukaryotic translation initiation factor 4E (eIF4E) protein.
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