Carborane as an alternative efficient hydrophobic tag for protein degradation

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Carborane as an alternative efficient hydrophobic tag for protein degradation
Y Asawa; K Nishida; K Kawai; K Domae; Hyun Seung Ban; A Kitazaki; H Asami; J Y Kohno; S Okada; H Tokuma; D Sakano; S Kume; M Tanaka; H Nakamura
Bibliographic Citation
Bioconjugate Chemistry, vol. 32, no. 11, pp. 2377-2385
Publication Year
Carboranes 1 and 2 were designed and synthesized for hydrophobic tag (HyT)-induced degradation of HaloTag fusion proteins. The levels of the hemagglutinin (HA)-HaloTag2-green fluorescent protein (EGFP) stably expressed in Flp-In 293 cells were significantly reduced by HyT13, HyT55, and carboranes 1 and 2, with expression levels of 49, 79, 43, and 65%, respectively, indicating that carborane is an alternative novel hydrophobic tag (HyT) for protein degradation under an intracellular environment. To clarify the mechanism of HyT-induced proteolysis, bovine serum albumin (BSA) was chosen as an extracellular protein and modified with maleimide-conjugated m-carborane (MIC). The measurement of the ζ-potentials and the lysine residue modification with fluorescein isothiocyanate (FITC) of BSA-MIC conjugates suggested that the conjugation of carborane induced the exposure of lysine residues on BSA, resulting in the degradation via ubiquitin E3 ligase-related proteasome pathways in the cell.
Amer Chem Soc
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Division of Biomedical Research > Biotherapeutics Translational Research Center > 1. Journal Articles
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