Kornumagerskov0502

This study aimed to determine the anti-obesity effects and mechanisms of Cerasus humilis polyphenol (CHP) in C57BL/6 obese mice and 3T3-L1 cells. High-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used for the qualitative and quantitative identification of CHP components. The obese mice, induced by feeding high-fat diet (HFD), were treated with CHP (250 mg/kg/day) by gavage for 12 weeks. Orlistat was gavaged at 15.6 mg/kg bw/day, as a positive control group. The analysis revealed that the main components of CHP were procyanidin B2, cyanidin-3-glucoside, and pelargonidin-3-glucoside. CHP dietary supplementation significantly reduced body weight and improved blood lipid measurements in HFD-fed mice (p less then 0.01). Moreover, it inhibited mRNA expression of miR-122, Srebp-1c, and Cpt1a (p less then 0.01) and reduced hepatic lipid deposition, as seen by hematoxylin and eosin staining. CHP downregulated the protein expression of PPARγ and C/EBPα in HFD-induced obese mice and inhibited adipocyte differentiation (p less then 0.01). Compared with the HFD group, CHP supplementation had an obvious anti-inflammatory effect (decreased protein expression, such as TNF-α, IL-6, and MCP1), reducing leptin levels and TNF-α secretion in serum and cells (p less then 0.01). CHP significantly inhibited the expression of miR-27a/b (53.3 and 29.9%, p less then 0.01) in mice retroperitoneal white adipocytes, enhancing the expression of the target gene Prdm16 and significantly upregulating Sirt1 (105.5%, p less then 0.01) compared with the HFD group. Moreover, CHP supplementation effectively improved oxidative stress (ROS, T-AOC, SOD, CAT, and GSH-Px) induced by HFD in obese mice (p less then 0.01). Thus, CHP mitigates adipocyte differentiation, browning of white adipocytes, and reduction of inflammation and antioxidant activity to reduce obesity. Consequently, these results provide novel insights into the anti-obesity roles of CHP in HFD-induced obesity.Cerium-based materials such as ceria are increasingly used in catalytic reactions. We report here the synthesis of the first Ce-based metal-organic layer (MOL), Ce6-BTB, comprising Ce6 secondary building units (SBUs) and 1,3,5-benzenetribenzoate (BTB) linkers, and its functionalization for photocatalytic hydrogen evolution reaction (HER). Ce6-BTB was postsynthetically modified with photosensitizing [(MBA)Ir(ppy)2]Cl or [(MBA)Ru(bpy)2]Cl2 (MBA = 2-(5'-methyl-[2,2'-bipyridin]-5-yl)acetate, ppy = 2-phenylpyridine, bpy = 2,2'-bipyridine) to afford Ce6-BTB-Ir or Ce6-BTB-Ru MOLs, respectively. The proximity of photosensitizing ligands and Ce6 SBUs in the MOLs facilitates electron transfer to drive photocatalytic HER under visible light with turnover numbers of 1357 and 484 for Ce6-BTB-Ir and Ce6-BTB-Ru, respectively. Photophysical and electrochemical studies revealed a novel dual photoexcitation pathway whereby the excited photosensitizers in the MOL are reductively quenched and then transfer electrons to Ce6 SBUs to generate CeIII centers, which are further photoexcited to CeIII* species for HER.Electrochemical capacitor and capacitive deionization store energy through the interface layer formed between electrodes and electrolytes. The crystalline form and surface potential of the oxide electrode can be changed in order to improve the capacitance. By characterizing the surface property and crystalline form of the TiO2 thin-film electrode at different sintering temperatures, it is showed that each electrode has its own surface potential which is affected by the crystalline structure. At elevated sintering temperature, TiO2 transfers from anatase to rutile with an increased surface potential. The electrochemical tests show that the electrode capacitance increases from 19.50 to 41.82 mF/cm2. Therefore, rutile TiO2 has a higher surface potential and better capacitive performance when used on a positive electrode compared with anatase TiO2. In general, the relation between the surface potential, the crystalline forms, and the capacitive performance is achieved in this work. We hope it can promote the investigation of oxide materials in the application for electrochemical capacitors and capacitive deionization.Metallic cluster catalysts have many thermodynamically accessible isomers with diverse active sites and low reaction barriers, and lately a strong hypothesis emerged that the many catalyst states collectively drive the catalysis. However, it remained a hypothesis that catalyst isomerization is actually kinetically feasible under the current reaction conditions. Using high-temperature dynamics simulations and sampling, a range of orientations, and vibrational energy distributions, we probe how thermal effects and molecular events affect cluster catalyst dynamics. https://www.selleckchem.com/products/AZD1152-HQPA.html We show that even such a delicate affair as the dissociation or scattering of a methane molecule on the heavy and thus slow Pt13 cluster triggers substantial isomerization of the catalyst, far beyond thermal at 700 K. A kinetic coupling between the methane activity and cluster catalyst dynamics is observed. In return, the thermal dynamics of the cluster affects the methane reaction and scattering probabilities. Hence, molecular events at the surfaces of fluxional cluster catalysts should facilitate the population of an ensemble of catalyst states under the current reaction conditions, with implications for available active sites, reaction mechanisms, and apparent rates.Skp1 is an adapter that links F-box proteins to cullin-1 in the Skp1/cullin-1/F-box (SCF) protein family of E3 ubiquitin ligases that targets specific proteins for polyubiquitination and subsequent protein degradation. Skp1 from the amoebozoan Dictyostelium forms a stable homodimer in vitro with a Kd of 2.5 μM as determined by sedimentation velocity studies yet is monomeric in crystal complexes with F-box proteins. To investigate the molecular basis for the difference, we determined the solution NMR structure of a doubly truncated Skp1 homodimer (Skp1ΔΔ). The solution structure of the Skp1ΔΔ dimer reveals a 2-fold symmetry with an interface that buries ∼750 Å2 of predominantly hydrophobic surface. The dimer interface overlaps with subsite 1 of the F-box interaction area, explaining why only the Skp1 monomer binds F-box proteins (FBPs). To confirm the model, Rosetta was used to predict amino acid substitutions that might disrupt the dimer interface, and the F97E substitution was chosen to potentially minimize interference with F-box interactions.