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auriculasin  (MedChemExpress)


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    Structured Review

    MedChemExpress auriculasin
    BD directly bound to PIM1. (A) A comprehensive analysis of the results of the XP docking and MMGBSA analysis revealed the top five ranked natural products marked in red. (B) The IC 50 value of Scutellarein, <t>Auriculasin,</t> Emodin, BD, and Cordycepin detected by CCK8 assays. (C) The molecular formula of BD. (D, E) The 3D and 2D structure determination of BD and PIM1 protein by molecular docking analysis. The molecular docking results showed that BD targeted PIM1 by forming hydrophobic interactions with residues ILE74 and VAL69 while forming two hydrogen bonds with residue ARG73 and one hydrogen bond with residue ASP202. The hydrogen bonds are illustrated as yellow dotted lines. (F) RMSD plots throughout the 100 ns MD simulation. The horizontal coordinate represents the Root Mean Square Deviation (RMSD), while the horizontal coordinate indicates the time. (G) RMSF plots throughout the 100 ns MD simulation. The horizontal coordinate represents Root Mean Square Fluctuation (RMSF) while the horizontal coordinate represents the Residue Index. (H) Interaction fraction of the PIM1/BD complex. The horizontal coordinate represents the interactions fraction, and the horizontal coordinate represents the amino acid site. (I, J) The binding affinity of BD to PIM1 was evaluated by surface plasmon resonance (SPR) analysis. The figures displayed the real-time sensorgrams for SPR kinetic analysis of the bindings of BD (0.19–50.0 μmol/L) to PIM1. The experiment adopts multi-cycle operation, and the response signal takes the analysis time as the horizontal coordinate and the response value (RU) as the vertical coordinate. (K) BD-PIM1 binding was analyzed within HSFs through cellular thermal shift assay and Western blot assay (n = 3 independent experiments). (L) Western blot analysis revealed the effect of BD on alleviating PIM1 expression within HSFs. (M) Immunofluorescence analysis investigated the effect of BD on decreasing PIM1 expression within HSFs. Scale bar = 100 μm. (N) IP assays illustrated the effect of BD on promoting ubiquitin-proteasome-mediated PIM1 degradation within HSFs which were pre-treated with MG132 (10 μM). (O) Western blot analysis revealed the impacts of BD, MG132 (10 μM), or BD combined with MG132 treatment on PIM1 protein expression within HSFs. Data are expressed as mean ± SD. Experiments (L) and (O) were analyzed with one-way ANOVA with Tukey's multiple comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.
    Auriculasin, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/auriculasin/product/MedChemExpress
    Average 93 stars, based on 2 article reviews
    auriculasin - by Bioz Stars, 2026-02
    93/100 stars

    Images

    1) Product Images from "Targeting PIM1 by Bruceine D attenuates skin fibrosis via myofibroblast ferroptosis"

    Article Title: Targeting PIM1 by Bruceine D attenuates skin fibrosis via myofibroblast ferroptosis

    Journal: Redox Biology

    doi: 10.1016/j.redox.2025.103619

    BD directly bound to PIM1. (A) A comprehensive analysis of the results of the XP docking and MMGBSA analysis revealed the top five ranked natural products marked in red. (B) The IC 50 value of Scutellarein, Auriculasin, Emodin, BD, and Cordycepin detected by CCK8 assays. (C) The molecular formula of BD. (D, E) The 3D and 2D structure determination of BD and PIM1 protein by molecular docking analysis. The molecular docking results showed that BD targeted PIM1 by forming hydrophobic interactions with residues ILE74 and VAL69 while forming two hydrogen bonds with residue ARG73 and one hydrogen bond with residue ASP202. The hydrogen bonds are illustrated as yellow dotted lines. (F) RMSD plots throughout the 100 ns MD simulation. The horizontal coordinate represents the Root Mean Square Deviation (RMSD), while the horizontal coordinate indicates the time. (G) RMSF plots throughout the 100 ns MD simulation. The horizontal coordinate represents Root Mean Square Fluctuation (RMSF) while the horizontal coordinate represents the Residue Index. (H) Interaction fraction of the PIM1/BD complex. The horizontal coordinate represents the interactions fraction, and the horizontal coordinate represents the amino acid site. (I, J) The binding affinity of BD to PIM1 was evaluated by surface plasmon resonance (SPR) analysis. The figures displayed the real-time sensorgrams for SPR kinetic analysis of the bindings of BD (0.19–50.0 μmol/L) to PIM1. The experiment adopts multi-cycle operation, and the response signal takes the analysis time as the horizontal coordinate and the response value (RU) as the vertical coordinate. (K) BD-PIM1 binding was analyzed within HSFs through cellular thermal shift assay and Western blot assay (n = 3 independent experiments). (L) Western blot analysis revealed the effect of BD on alleviating PIM1 expression within HSFs. (M) Immunofluorescence analysis investigated the effect of BD on decreasing PIM1 expression within HSFs. Scale bar = 100 μm. (N) IP assays illustrated the effect of BD on promoting ubiquitin-proteasome-mediated PIM1 degradation within HSFs which were pre-treated with MG132 (10 μM). (O) Western blot analysis revealed the impacts of BD, MG132 (10 μM), or BD combined with MG132 treatment on PIM1 protein expression within HSFs. Data are expressed as mean ± SD. Experiments (L) and (O) were analyzed with one-way ANOVA with Tukey's multiple comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.
    Figure Legend Snippet: BD directly bound to PIM1. (A) A comprehensive analysis of the results of the XP docking and MMGBSA analysis revealed the top five ranked natural products marked in red. (B) The IC 50 value of Scutellarein, Auriculasin, Emodin, BD, and Cordycepin detected by CCK8 assays. (C) The molecular formula of BD. (D, E) The 3D and 2D structure determination of BD and PIM1 protein by molecular docking analysis. The molecular docking results showed that BD targeted PIM1 by forming hydrophobic interactions with residues ILE74 and VAL69 while forming two hydrogen bonds with residue ARG73 and one hydrogen bond with residue ASP202. The hydrogen bonds are illustrated as yellow dotted lines. (F) RMSD plots throughout the 100 ns MD simulation. The horizontal coordinate represents the Root Mean Square Deviation (RMSD), while the horizontal coordinate indicates the time. (G) RMSF plots throughout the 100 ns MD simulation. The horizontal coordinate represents Root Mean Square Fluctuation (RMSF) while the horizontal coordinate represents the Residue Index. (H) Interaction fraction of the PIM1/BD complex. The horizontal coordinate represents the interactions fraction, and the horizontal coordinate represents the amino acid site. (I, J) The binding affinity of BD to PIM1 was evaluated by surface plasmon resonance (SPR) analysis. The figures displayed the real-time sensorgrams for SPR kinetic analysis of the bindings of BD (0.19–50.0 μmol/L) to PIM1. The experiment adopts multi-cycle operation, and the response signal takes the analysis time as the horizontal coordinate and the response value (RU) as the vertical coordinate. (K) BD-PIM1 binding was analyzed within HSFs through cellular thermal shift assay and Western blot assay (n = 3 independent experiments). (L) Western blot analysis revealed the effect of BD on alleviating PIM1 expression within HSFs. (M) Immunofluorescence analysis investigated the effect of BD on decreasing PIM1 expression within HSFs. Scale bar = 100 μm. (N) IP assays illustrated the effect of BD on promoting ubiquitin-proteasome-mediated PIM1 degradation within HSFs which were pre-treated with MG132 (10 μM). (O) Western blot analysis revealed the impacts of BD, MG132 (10 μM), or BD combined with MG132 treatment on PIM1 protein expression within HSFs. Data are expressed as mean ± SD. Experiments (L) and (O) were analyzed with one-way ANOVA with Tukey's multiple comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.

    Techniques Used: Residue, Binding Assay, SPR Assay, Thermal Shift Assay, Western Blot, Expressing, Immunofluorescence, Comparison



    Similar Products

    auriculasin  (MedChemExpress)
    93
    MedChemExpress auriculasin
    BD directly bound to PIM1. (A) A comprehensive analysis of the results of the XP docking and MMGBSA analysis revealed the top five ranked natural products marked in red. (B) The IC 50 value of Scutellarein, <t>Auriculasin,</t> Emodin, BD, and Cordycepin detected by CCK8 assays. (C) The molecular formula of BD. (D, E) The 3D and 2D structure determination of BD and PIM1 protein by molecular docking analysis. The molecular docking results showed that BD targeted PIM1 by forming hydrophobic interactions with residues ILE74 and VAL69 while forming two hydrogen bonds with residue ARG73 and one hydrogen bond with residue ASP202. The hydrogen bonds are illustrated as yellow dotted lines. (F) RMSD plots throughout the 100 ns MD simulation. The horizontal coordinate represents the Root Mean Square Deviation (RMSD), while the horizontal coordinate indicates the time. (G) RMSF plots throughout the 100 ns MD simulation. The horizontal coordinate represents Root Mean Square Fluctuation (RMSF) while the horizontal coordinate represents the Residue Index. (H) Interaction fraction of the PIM1/BD complex. The horizontal coordinate represents the interactions fraction, and the horizontal coordinate represents the amino acid site. (I, J) The binding affinity of BD to PIM1 was evaluated by surface plasmon resonance (SPR) analysis. The figures displayed the real-time sensorgrams for SPR kinetic analysis of the bindings of BD (0.19–50.0 μmol/L) to PIM1. The experiment adopts multi-cycle operation, and the response signal takes the analysis time as the horizontal coordinate and the response value (RU) as the vertical coordinate. (K) BD-PIM1 binding was analyzed within HSFs through cellular thermal shift assay and Western blot assay (n = 3 independent experiments). (L) Western blot analysis revealed the effect of BD on alleviating PIM1 expression within HSFs. (M) Immunofluorescence analysis investigated the effect of BD on decreasing PIM1 expression within HSFs. Scale bar = 100 μm. (N) IP assays illustrated the effect of BD on promoting ubiquitin-proteasome-mediated PIM1 degradation within HSFs which were pre-treated with MG132 (10 μM). (O) Western blot analysis revealed the impacts of BD, MG132 (10 μM), or BD combined with MG132 treatment on PIM1 protein expression within HSFs. Data are expressed as mean ± SD. Experiments (L) and (O) were analyzed with one-way ANOVA with Tukey's multiple comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.
    Auriculasin, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/auriculasin/product/MedChemExpress
    Average 93 stars, based on 1 article reviews
    auriculasin - by Bioz Stars, 2026-02
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    BD directly bound to PIM1. (A) A comprehensive analysis of the results of the XP docking and MMGBSA analysis revealed the top five ranked natural products marked in red. (B) The IC 50 value of Scutellarein, Auriculasin, Emodin, BD, and Cordycepin detected by CCK8 assays. (C) The molecular formula of BD. (D, E) The 3D and 2D structure determination of BD and PIM1 protein by molecular docking analysis. The molecular docking results showed that BD targeted PIM1 by forming hydrophobic interactions with residues ILE74 and VAL69 while forming two hydrogen bonds with residue ARG73 and one hydrogen bond with residue ASP202. The hydrogen bonds are illustrated as yellow dotted lines. (F) RMSD plots throughout the 100 ns MD simulation. The horizontal coordinate represents the Root Mean Square Deviation (RMSD), while the horizontal coordinate indicates the time. (G) RMSF plots throughout the 100 ns MD simulation. The horizontal coordinate represents Root Mean Square Fluctuation (RMSF) while the horizontal coordinate represents the Residue Index. (H) Interaction fraction of the PIM1/BD complex. The horizontal coordinate represents the interactions fraction, and the horizontal coordinate represents the amino acid site. (I, J) The binding affinity of BD to PIM1 was evaluated by surface plasmon resonance (SPR) analysis. The figures displayed the real-time sensorgrams for SPR kinetic analysis of the bindings of BD (0.19–50.0 μmol/L) to PIM1. The experiment adopts multi-cycle operation, and the response signal takes the analysis time as the horizontal coordinate and the response value (RU) as the vertical coordinate. (K) BD-PIM1 binding was analyzed within HSFs through cellular thermal shift assay and Western blot assay (n = 3 independent experiments). (L) Western blot analysis revealed the effect of BD on alleviating PIM1 expression within HSFs. (M) Immunofluorescence analysis investigated the effect of BD on decreasing PIM1 expression within HSFs. Scale bar = 100 μm. (N) IP assays illustrated the effect of BD on promoting ubiquitin-proteasome-mediated PIM1 degradation within HSFs which were pre-treated with MG132 (10 μM). (O) Western blot analysis revealed the impacts of BD, MG132 (10 μM), or BD combined with MG132 treatment on PIM1 protein expression within HSFs. Data are expressed as mean ± SD. Experiments (L) and (O) were analyzed with one-way ANOVA with Tukey's multiple comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.

    Journal: Redox Biology

    Article Title: Targeting PIM1 by Bruceine D attenuates skin fibrosis via myofibroblast ferroptosis

    doi: 10.1016/j.redox.2025.103619

    Figure Lengend Snippet: BD directly bound to PIM1. (A) A comprehensive analysis of the results of the XP docking and MMGBSA analysis revealed the top five ranked natural products marked in red. (B) The IC 50 value of Scutellarein, Auriculasin, Emodin, BD, and Cordycepin detected by CCK8 assays. (C) The molecular formula of BD. (D, E) The 3D and 2D structure determination of BD and PIM1 protein by molecular docking analysis. The molecular docking results showed that BD targeted PIM1 by forming hydrophobic interactions with residues ILE74 and VAL69 while forming two hydrogen bonds with residue ARG73 and one hydrogen bond with residue ASP202. The hydrogen bonds are illustrated as yellow dotted lines. (F) RMSD plots throughout the 100 ns MD simulation. The horizontal coordinate represents the Root Mean Square Deviation (RMSD), while the horizontal coordinate indicates the time. (G) RMSF plots throughout the 100 ns MD simulation. The horizontal coordinate represents Root Mean Square Fluctuation (RMSF) while the horizontal coordinate represents the Residue Index. (H) Interaction fraction of the PIM1/BD complex. The horizontal coordinate represents the interactions fraction, and the horizontal coordinate represents the amino acid site. (I, J) The binding affinity of BD to PIM1 was evaluated by surface plasmon resonance (SPR) analysis. The figures displayed the real-time sensorgrams for SPR kinetic analysis of the bindings of BD (0.19–50.0 μmol/L) to PIM1. The experiment adopts multi-cycle operation, and the response signal takes the analysis time as the horizontal coordinate and the response value (RU) as the vertical coordinate. (K) BD-PIM1 binding was analyzed within HSFs through cellular thermal shift assay and Western blot assay (n = 3 independent experiments). (L) Western blot analysis revealed the effect of BD on alleviating PIM1 expression within HSFs. (M) Immunofluorescence analysis investigated the effect of BD on decreasing PIM1 expression within HSFs. Scale bar = 100 μm. (N) IP assays illustrated the effect of BD on promoting ubiquitin-proteasome-mediated PIM1 degradation within HSFs which were pre-treated with MG132 (10 μM). (O) Western blot analysis revealed the impacts of BD, MG132 (10 μM), or BD combined with MG132 treatment on PIM1 protein expression within HSFs. Data are expressed as mean ± SD. Experiments (L) and (O) were analyzed with one-way ANOVA with Tukey's multiple comparison test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001.

    Article Snippet: Reagents and Drugs used were recombinant Human TGF-β1 Protein (MCE, HY-P7118), Bruceine D (MCE, HY-N3014), Auriculasin (MCE, HY-N2911), Emodin (MCE, HY-14393), Cordycepin (MCE, HY-N0262), Scutellarein (MCE, HY-N0752), MG-132 (MCE, HY-13259), SGI-1776 (MCE, HY-13287), SEL-24 (MCE, HY-120758), SMI-4a (MCE, HY-16576A), TP-3654 (MCE, HY-101126), LGH447 (MCE, HY-19322), AZD1208 (MCE, HY-15604), Ferrostatin-1 (MCE, HY-100579), Liproxstatin-1 (MCE, HY-12726), Deferoxamine (MCE, HY-B0988), Necrosulfonamide (MCE, HY-100573), Z-VAD-FMK (MCE, HY-16658B), t-BHP (Sigma-Aldrich, 458139), RSL3 (MCE, HY-100218A), Bleomycin (Thermo Fisher, R25001).

    Techniques: Residue, Binding Assay, SPR Assay, Thermal Shift Assay, Western Blot, Expressing, Immunofluorescence, Comparison