Selective hydrogenation of furfural to cyclopentanone over Cu-Ni-Al hydrotalcite-based catalysts

Hongyan Zhu,Guomin Xiao,Minghao Zhou,Zuo Zeng,Rui Xiao 한국화학공학회 2014 Korean Journal of Chemical Engineering Vol.31 No.4

A series of Cu-Ni-Al hydrotalcites derived oxides with a (Cu+Ni)/Al mole ratio of 3 with varied Cu/Nimole ratio (from 0.017 to 0.5, with a Cu ratio of 0.0125 to 0.25) were prepared by co-precipitation method, then appliedto the hydrogenation of furfural in aqueous. Their catalytic performance for liquid phase hydrogenation of furfural toprepare cyclopentanone was described in detail, considering reaction temperature, catalyst composition, reaction timeand so on. The yield of cyclopentanone was influenced by the mole ratio of Cu-Ni-Al based heterogeneous catalystand depended on the reaction conditions. The yield of cyclopentanone was up to 95.8% when the reaction was carriedout under 413 K with H2 pressure of 40 bar for 8 h. The catalysts were characterized by X-ray powder diffraction (XRD),scanning electron microscope (SEM) and H2 temperature-programmed reduction (H2-TPR).

Potential Vaccine Targets against Rabbit Coccidiosis by Immunoproteomic Analysis

Hongyan Song,Ronglian Dong,Baofeng Qiu,Jin Jing,Shunxing Zhu,Chun Liu,Yingmei Jiang,Shengcun Wang,Jin Miao,Yixiang Shao 대한기생충학열대의학회 2017 The Korean Journal of Parasitology Vol.55 No.1

Ginsenoside compound K inhibits nuclear factor-kappa B by targeting Annexin A2

Yushi Wang,Hongyan Zhu,He Liu,Yang Li,Bing Zhao,Ying-Hua Jin 고려인삼학회 2019 Journal of Ginseng Research Vol.43 No.3

Background: Ginsenoside compound K(C-K), a major metabolite of ginsenoside, exhibits anticancer activityin various cancer cells and animal models. A cell signaling study has shown that C-K inhibitednuclear factor-kappa B (NF-kB) pathway in human astroglial cells and liver cancer cells. However, themolecular targets of C-K and the initiating events were not elucidated. Methods: Interaction between C-K and Annexin A2 was determined by molecular docking and thermalshift assay. HepG2 cells were treated with C-K, followed by a luciferase reporter assay for NF-lB,immunofluorescence imaging for the subcellular localization of Annexin A2 and NF-lB p50 subunit,coimmunoprecipitation of Annexin A2 and NF-lB p50 subunit, and both cell viability assay and plateclone formation assay to determine the cell viability. Results: Both molecular docking and thermal shift assay positively confirmed the interaction betweenAnnexin A2 and C-K. This interaction prevented the interaction between Annexin A2 and NF-lB p50subunit and their nuclear colocalization, which attenuated the activation of NF-lB and the expression ofits downstream genes, followed by the activation of caspase 9 and 3. In addition, the overexpression ofAnnexin A2-K320A, a C-K binding-deficient mutant of Annexin A2, rendered cells to resist C-K treatment,indicating that C-K exerts its cytotoxic activity mainly by targeting Annexin A2. Conclusion: This study for the first time revealed a cellular target of C-K and the molecular mechanismfor its anticancer activity.

Ginsenoside compound K inhibits nuclear factor-kappa B by targeting Annexin A2

Wang, Yu-Shi,Zhu, Hongyan,Li, He,Li, Yang,Zhao, Bing,Jin, Ying-Hua The Korean Society of Ginseng 2019 Journal of Ginseng Research Vol.43 No.3

Background: Ginsenoside compound K(C-K), a major metabolite of ginsenoside, exhibits anticancer activity in various cancer cells and animal models. A cell signaling study has shown that C-K inhibited nuclear factor-kappa B ($NF-{\kappa}B$) pathway in human astroglial cells and liver cancer cells. However, the molecular targets of C-K and the initiating events were not elucidated. Methods: Interaction between C-K and Annexin A2 was determined by molecular docking and thermal shift assay. HepG2 cells were treated with C-K, followed by a luciferase reporter assay for $NF-{\kappa}B$, immunofluorescence imaging for the subcellular localization of Annexin A2 and $NF-{\kappa}B$ p50 subunit, coimmunoprecipitation of Annexin A2 and $NF-{\kappa}B$ p50 subunit, and both cell viability assay and plate clone formation assay to determine the cell viability. Results: Both molecular docking and thermal shift assay positively confirmed the interaction between Annexin A2 and C-K. This interaction prevented the interaction between Annexin A2 and $NF-{\kappa}B$ p50 subunit and their nuclear colocalization, which attenuated the activation of $NF-{\kappa}B$ and the expression of its downstream genes, followed by the activation of caspase 9 and 3. In addition, the overexpression of Annexin A2-K320A, a C-K binding-deficient mutant of Annexin A2, rendered cells to resist C-K treatment, indicating that C-K exerts its cytotoxic activity mainly by targeting Annexin A2. Conclusion: This study for the first time revealed a cellular target of C-K and the molecular mechanism for its anticancer activity.

The interaction of serum albumin with ginsenoside Rh2 resulted in the downregulation of ginsenoside Rh2 cytotoxicity

Lin, Yingjia,Li, Yang,Song, Zhi-Guang,Zhu, Hongyan,Jin, Ying-Hua The Korean Society of Ginseng 2017 Journal of Ginseng Research Vol.41 No.3

Background: Ginsenoside Rh2 (G-Rh2) is a ginseng saponin that is widely investigated because of its remarkable antitumor activity. However, the molecular mechanism by which (20S) G-Rh2 triggers its functions and how target animals avoid its cytotoxic action remains largely unknown. Methods: Phage display was used to screen the human targets of (20S) G-Rh2. Fluorescence spectroscopy and UV-visible absorption spectroscopy were used to confirm the interaction of candidate target proteins and (20S) G-Rh2. Molecular docking was utilized to calculate the estimated free energy of binding and to structurally visualize their interactions. MTT assay and immunoblotting were used to assess whether human serum albumin (HSA), bovine serum albumin (BSA), and bovine serum can reduce the cytotoxic activity of (20S) G-Rh2 in HepG2 cells. Results: In phage display, (20S) G-Rh2-beads and (20R) G-Rh2-beads were combined with numerous kinds of phages, and a total of 111 different human complementary DNAs (cDNA) were identified, including HSA which had the highest rate. The binding constant and number of binding site in the interaction between (20S)-Rh2 and HSA were $3.5{\times}10^5M^{-1}$ and 1, and those in the interaction between (20S) G-Rh2 and BSA were $1.4{\times}10^5M^{-1}$ and 1. The quenching mechanism is static quenching. HSA, BSA and bovine serum significantly reduced the proapoptotic effect of (20S) G-Rh2. Conclusion: HSA and BSA interact with (20S) G-Rh2. Serum inhibited the activity of (20S) G-Rh2 mainly due to the interaction between (20S) G-Rh2 and serum albumin (SA). This study proposes that HSA may enhance (20S) G-Rh2 water solubility, and thus might be used as nanoparticles in the (20S) G-Rh2 delivery process.

The interaction of serum albumin with ginsenoside Rh2 resulted in the downregulation of ginsenoside Rh2 cytotoxicity

Yingjia Lin,Yang Li,Zhi-Guang Song,Hongyan Zhu,Ying-Hua Jin 고려인삼학회 2017 Journal of Ginseng Research Vol.41 No.3

Background: Ginsenoside Rh2 (G-Rh2) is a ginseng saponin that is widely investigated because of its remarkable antitumor activity. However, the molecular mechanism by which (20S) G-Rh2 triggers its functions and how target animals avoid its cytotoxic action remains largely unknown. Methods: Phage display was used to screen the human targets of (20S) G-Rh2. Fluorescence spectroscopy and UV-visible absorption spectroscopy were used to confirm the interaction of candidate target proteins and (20S) G-Rh2. Molecular docking was utilized to calculate the estimated free energy of binding and to structurally visualize their interactions. MTT assay and immunoblotting were used to assess whether human serum albumin (HSA), bovine serum albumin (BSA), and bovine serum can reduce the cytotoxic activity of (20S) G-Rh2 in HepG2 cells. Results: In phage display, (20S) G-Rh2-beads and (20R) G-Rh2-beads were combined with numerous kinds of phages, and a total of 111 different human complementary DNAs (cDNA) were identified, including HSA which had the highest rate. The binding constant and number of binding site in the interaction between (20S)-Rh2 and HSA were 3.5 105 M1 and 1, and those in the interaction between (20S) G-Rh2 and BSA were 1.4 105 M1 and 1. The quenching mechanism is static quenching. HSA, BSA and bovine serum significantly reduced the proapoptotic effect of (20S) G-Rh2. Conclusion: HSA and BSA interact with (20S) G-Rh2. Serum inhibited the activity of (20S) G-Rh2 mainly due to the interaction between (20S) G-Rh2 and serum albumin (SA). This study proposes that HSA may enhance (20S) G-Rh2 water solubility, and thus might be used as nanoparticles in the (20S) G-Rh2 delivery process.