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• W4313648639 abstract "The platforms based on immobilization of transmembrane proteins have become an effective way to study drug-protein interaction and identify new leads for drug discovery. Herein, we exploited the protein superglue (i.e. SpyTag-SpyCatcher chemistry) for site-specific, oriented, and in-situ one-step beta2-adrenoceptor (β2-AR) immobilization. SpyCatcher was used as a fusion tag at the C-terminal of β2-AR and the macroporous silica gels were functionalized with the SpyTag peptide. Immobilization was realized by immersing the gels into the E.coli cell lysate containing β2-AR-SpyCatcher. Characterization of the functionalized gels was performed by X-ray photoelectron spectroscopy and fluorescence microscopy. Adsorption energy distribution calculation, injection amount dependent analysis (IADA) and nonlinear chromatographic were used for receptor-ligand interaction analysis. The affinity rank order of four ligands to the receptor was tulobuterol> chlorprenaline> salbutamol> terbutaline, which showed highly consistent with data from the radioligand binding assay and the β2-AR column prepared by HaloTag technology. Magnolol and honokiol were screened from Cortex Magnoliae Officinalis and proved to promote the expression of the receptor in human airway smooth muscle cells. Our work unraveled the great potential to generate good bioactivity of the immobilized β2-AR through Spy toolbox. This technology can be extended to the immobilization of other functional proteins, providing a better alternative in the field of bioanalysis, biosensing, and separation science." @default.
• W4313648639 created "2023-01-07" @default.
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• W4313648639 date "2023-02-01" @default.
• W4313648639 modified "2023-10-12" @default.
• W4313648639 title "Protein superglue inspired in-situ one-step site-specific immobilization of beta2-adrenoceptor and its application in bioactive compound screening from Cortex Magnoliae Officinalis" @default.
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• W4313648639 doi "https://doi.org/10.1016/j.chroma.2023.463780" @default.
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