The purpose of this study is to find out if an investigational combination drug called Lovaza (made with fish oils)+Curcumin C3 Complex (made from a root called curcumin) can help reduce the size of lung nodules. Researchers also want to find out if the combination of Lovaza+Curcumin C3 Complex is safe and tolerable.

开始日期2019-06-05

申办/合作机构

H. Lee Moffitt Cancer Center & Research Institute, Inc.

100 项与 Curcumin C3 complex 相关的临床结果

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100 项与 Curcumin C3 complex 相关的转化医学

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100 项与 Curcumin C3 complex 相关的专利（医药）

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项与 Curcumin C3 complex 相关的文献（医药）

2025-01-01·Colloids and Surfaces B: Biointerfaces

Heating-driven self-assembled glycyrrhizin nanomicelles loading bisdemethoxycurcumin: Preparation, characterization, and efficacy evaluation on experimental dry eye

Article

作者: Jie, Ying ; Tian, Lei ; Meng, Qingqian ; Yu, Linrong ; Li, Mengshuang ; Wu, Xianggen

In this study, a simple but novel preparation method was developed by heating a mixture of dipotassium glycyrrhizinate (DG) and bisdemethoxycurcumin (BDMC) in aqueous solution, and a DG self-assembled nanomicelles-loading BDMC (named B@DNM) ophthalmic solution was successfully fabricated with this heating-driven process. AutoDock simulation analysis revealed that Pi-Alkyl hydrophobic interactions between BDMC and DG played important role in this self-assembled B@DNM. The optimized B@DNM, with a DG:BDMC mass ratio of 40:1 and heating time of 6 h, had a high encapsulation efficacy of 96.70 ± 0.13 % and particle sizes of 117.50 ± 6.07 nm. The apparent solubility of BDMC in B@DNM was significantly improved from bare BDMC (10.40 ± 0.16 μg/ml to 1405.60 ± 6.78 μg/ml) in artificial tears after 4 h incubation. B@DNM had great storage stability as an aqueous ophthalmic solution. B@DNM showed significantly improved in vitro antioxidant activity. Ex vivo hen's egg test-chorioallantoic membrane assay and long-term in vivo mouse eye tolerance evaluation showed that B@DNM had good ocular safety profiles. B@DNM showed improved in vivo corneal permeation profiles in the mouse eyes. Topical administration of B@DNM achieved a significantly improved efficacy on a mouse model of dry eye disease (DED), including accelerating corneal wound healing, restoring corneal sensitivity, and inhibiting corneal neovascularization. Regulation of the high mobility group box 1 signal pathway was involved in B@DNM's strong therapeutic effects. These findings demonstrate that heating is a simple method to prepare ocular nanoformulation with DG, and B@DNM might be a potential ocular drug for treating DED.

2024-11-01·International Journal of Biological Macromolecules

Insights into inhibitory action and interaction of bisdemethoxycurcumin on tyrosinase: Spectroscopic and docking analysis

Article

作者: Zhou, Huan ; Min, Xiaofeng ; Xu, Xuetao ; Su, Zhicheng ; Li, Dongli ; Kou, Xianke

Bisdemethoxycurcumin (BDMC), a demethoxy derivative of curcumin, has garnered interest for its potential anti-tyrosinase properties, which are crucial for applications in food preservation and cosmetic industries. Despite its recognized bioactive effects, the detailed inhibitory action and interaction of BDMC on tyrosinase and its application in anti-browning processes remain unclear. This study aims to dissect the molecular interactions of BDMC with tyrosinase, elucidate its inhibition mechanism, and assess its efficacy in preventing browning, thereby underpinning its potential as a natural anti-browning agent. Employing a battery of spectroscopic techniques, we characterized the interaction of BDMC with tyrosinase. The anti-browning properties of BDMC were evaluated on fresh-cut apples, and its effect on enzymatic activities related to browning was also investigated. The results indicate that BDMC interacts with tyrosinase in a reversible mixed-type inhibition manner with an IC₅₀ value of 12.5 ± 0.2 μM. Surface Plasmon Resonance (SPR) results indicated that BDMC presented good binding affinity toward tyrosinase. Fluorescence quenching results showed that BDMC could quench the fluorescence of tyrosinase in a static process. Synchronous fluorescence, circular dichroism spectra, and three-dimensional fluorescence results indicated that interaction of BDMC against tyrosinase resulted in changes of tyrosinase on microenvironment and conformation, thus causing decrease of tyrosinase activity. Copper-chelating results presented that BDMC could chelate to copper with stoichiometric ratio of 1: 2. Molecular docking provided intricate details of how BDMC interacted with tyrosinase. Moreover, BDMC exhibited anti-browning capability on fresh cut apples, and could regulate PPO, POD, and APX activities. The comprehensive analysis proposed in this study consolidated the theoretical basis of BDMC as a tyrosinase inhibitor and supported its potential anti-browning application.

2024-09-01·Journal of Biological Chemistry

Curcumin degradation in a soil microorganism: Screening and characterization of a β-diketone hydrolase

Article

作者: Kumano, Takuto ; Kobayashi, Michihiko ; Hassaninasab, Azam ; Ishigami, Kana ; Kishi, Katsuhiro ; Hashimoto, Yoshiteru

Curcumin is a plant-derived secondary metabolite exhibiting antitumor, neuroprotective, antidiabetic activities, and so on. We previously isolated Escherichia coli as an enterobacterium exhibiting curcumin-converting activity from human feces, and discovered an enzyme showing this activity (CurA) and named it NADPH-dependent curcumin/dihydrocurcumin reductase. From soil, here, we isolated a curcumin-degrading microorganism (No. 34) using the screening medium containing curcumin as the sole carbon source and identified as Rhodococcus sp. A curcumin-degrading enzyme designated as CurH was purified from this strain and characterized, and compared with CurA. CurH catalyzed hydrolytic cleavage of a carbon-carbon bond in the β-diketone moiety of curcumin and its analogs, yielding two products bearing a methyl ketone terminus and a carboxylic acid terminus, respectively. These findings demonstrated that a curcumin degradation reaction catalyzed by CurH in the soil environment was completely different from the one catalyzed by CurA in the human microbiome. Of all the curcumin analogs tested, suitable substrates for the enzyme were curcuminoids (i.e., curcumin and bisdemethoxycurcumin) and tetrahydrocurcuminoids. Thus, we named this enzyme curcuminoid hydrolase. The deduced amino acid sequence of curH exhibited similarity to those of members of acetyl-CoA C-acetyltransferase family. Considering results of oxygen isotope analyses and a series of site-directed mutagenesis experiments on our enzyme, we propose a possible catalytic mechanism of CurH, which is unique and distinct from those of enzymes degrading β-diketone moieties such as β-diketone hydrolases known so far.

100 项与 Curcumin C3 complex 相关的药物交易

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