Fig. 1: Neuroinflammatory regulation and binding site of tubulin inhibitor. | Experimental & Molecular Medicine

Fig. 1: Neuroinflammatory regulation and binding site of tubulin inhibitor.

From: Phenotype-based screening rediscovered benzopyran-embedded microtubule inhibitors as anti-neuroinflammatory agents by modulating the tubulin–p65 interaction

Fig. 1

a Chemical structure of initial hit compound 1. b Dose-dependent inhibition of cellular NO release by 1 against lipopolysaccharide (LPS) treatment in BV-2 microglial cells (n = 6). c Binding sites of known tubulin modulators; Taxol (orange), colchicine (purple), and vinblastine (blue). d Chemical structures of the target ID probe of 1 and known microtubule modulators. e Photoaffinity-based competition assay showed that 1 bound to the colchicine-binding site. Purified tubulin was cross-linked with the target ID probe of 1 under UV irradiation in the presence or absence of known tubulin modulators. Tubulin was further labeled with Cy5-azide through a Click reaction. f Docking analysis of compound 1 using cocrystal structures of tubulin with its binders. Left panel: colchicine (purple) and 1 (cyan) bind to the same site of tubulin. Middle panel: Structural similarity of compound 1 (gray) and colchicine (orange). Right panel: Expected interactions between 1 and amino acid residues of tubulin.

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