nonaarginine has been researched along with nickel-nitrilotriacetic-acid* in 1 studies
1 other study(ies) available for nonaarginine and nickel-nitrilotriacetic-acid
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Simple and efficient knockdown of His-tagged proteins by ternary molecules consisting of a His-tag ligand, a ubiquitin ligase ligand, and a cell-penetrating peptide.
We designed and synthesized hybrid molecules for a protein knockdown method based on the recognition of a His-tag fused to a protein of interest (POI). The synthesized target protein degradation inducers contained three functional moieties: a His-tag ligand (nickel nitrilotriacetic acid [Ni-NTA]), an E3 ligand (bestatin [BS] or MV1), and a carrier peptide (Tat or nonaarginine [R9]). The designed hybrid molecules, BS-Tat-Ni-NTA, MV1-Tat-Ni-NTA, BS-R9-Ni-NTA, and MV1-R9-Ni-NTA, efficiently degraded His-tagged cellular retinoic acid binding protein 2 via the ubiquitin-proteasome system (UPS). This system will become a useful tool for research into selective protein degradation inducers that act via the UPS. Topics: Cell Line; Cell-Penetrating Peptides; Dose-Response Relationship, Drug; Histidine; Humans; Leucine; Ligands; Molecular Structure; Nitrilotriacetic Acid; Oligopeptides; Organometallic Compounds; Receptors, Retinoic Acid; Structure-Activity Relationship; Ubiquitin-Protein Ligases | 2017 |