Heterotrimetallic Organic Framework Assembled with Fe^III/Ba^II/Na^I and Schiff Base: Structure and Visible Photocatalytic Degradation of Chlorophenols

A porous heterotrimetallic organic framework, [BaNa­(FeL)₂(μ₂-OH)­(H₂O)]·DMF·2H₂O (<b>1</b>) [H₄L = 1,2-cyclohexanediamino-<i>N</i>,<i>N</i>′-bis­(3-methyl-5-carboxysalicylidene)], has been synthesized and characterized. Each Fe^III ion is embedded in the internal [N₂O₂] pocket of an L^4– anion and further bridged by a μ₂-OH anion to give an (FeL)₂(μ₂-OH) dimer. The external carboxylate groups of L^4– anions coordinate to Ba^II and Na^I atoms to generate a three-dimensional periodic network. The sorption properties and UV–vis spectrum of <b>1</b> have been studied. The photodegradation of 2-chlorophenol (2-CP), 3-CP, and 4-CP by <b>1</b> at different pH values under visible light has also been systematically investigated

Heterotrimetallic Organic Framework Assembled with Fe^III/Ba^II/Na^I and Schiff Base: Structure and Visible Photocatalytic Degradation of Chlorophenols

A porous heterotrimetallic organic framework, [BaNa­(FeL)₂(μ₂-OH)­(H₂O)]·DMF·2H₂O (<b>1</b>) [H₄L = 1,2-cyclohexanediamino-<i>N</i>,<i>N</i>′-bis­(3-methyl-5-carboxysalicylidene)], has been synthesized and characterized. Each Fe^III ion is embedded in the internal [N₂O₂] pocket of an L^4– anion and further bridged by a μ₂-OH anion to give an (FeL)₂(μ₂-OH) dimer. The external carboxylate groups of L^4– anions coordinate to Ba^II and Na^I atoms to generate a three-dimensional periodic network. The sorption properties and UV–vis spectrum of <b>1</b> have been studied. The photodegradation of 2-chlorophenol (2-CP), 3-CP, and 4-CP by <b>1</b> at different pH values under visible light has also been systematically investigated

Model of the effect of MFHAS1 on TLR2 signaling pathway in response to TLR2 stimulation for 6–24 h.

<p>Model of the effect of MFHAS1 on TLR2 signaling pathway in response to TLR2 stimulation for 6–24 h.</p

IL-6 and TNF-α production after stimulation with Pam3CSK4 by knockdown of <i>Mfhas1</i> using shMFHAS1.

<p>(A, B) RAW 264.7 macrophages were transfected with shMFHAS1 or pCDH empty vector or HIS-MFHAS1 plasmid, and 24 h post-transfected cells were treated with 10 ng/mL Pam3CSK4. Cell supernatant was collected after 6, 12, and 24 h posttreatment, and IL-6 (A) and TNF-α (B) production were measured by ELISA. (C, D) RAW 264.7 macrophages were transfected with shMFHAS1 or pCDH empty vector, and 24 h post-transfected cells were untreated or treated with 10 ng/mL Pam3CSK4 (C), or 50 ng/mL LPS (D). At 6 h and 24 h posttreatment, IL-6 expression was measured by RT-PCR and normalized to β-actin. (E, F) The knockdown efficiency of shMFHAS1 at 6 h and 24 h was assessed by RT-PCR (E) and western blotting (F). Values are the means ± SD from at least three independent experiments. *<i>P</i> < 0.05.</p

MFHAS1 does not affect transcription factor IRF-7 and IFN-β expression.

<p>(A) HEK293 and 293-MFHAS1 cells were transiently transfected with 100 ng TLR2 or 100 ng TLR2/50 ng CD14 expression plasmids, the pFR luciferase reporter gene along with plasmid expressing IRF7-Gal4 3 ng. Then these 24 h post-transfected cells were treated with mock, 100 ng/mL or 10μg/mL Pam3CSK4 for 24 h, and luciferase reporter gene activity was measured. (B) HEK293 and 293-MFHAS1 cells were transiently transfected with 100 ng TLR2 expression plasmids, and 24 h post-transfected cells were untreated or treated with 100 ng/mL Pam3CSK4 for 24 h. IFN-β mRNA expression was assayed by quantitative RT-PCR. (C) The relative IFN-β mRNA level was normalized to GAPDH. Values are the means ± SD from at least three independent experiments. *<i>p</i> < 0.05, **<i>p</i> < 0.01, or ***<i>p</i> < 0.001.</p

Gender, age, blood IL-6 and MFHAS1 concentrations in septic patients and controls.

<p>Gender, age, blood IL-6 and MFHAS1 concentrations in septic patients and controls.</p

The expression of <i>MFHAS1</i> in PBMC and macrophages/monocytes after TLR2 stimulation.

<p>(A) PBMC was isolated from the peripheral blood of humane in the control group and the septic patients. The gene expression of <i>MFHAS1</i> in the PMBC was analyzed by qPCR. n = 8/group. (B) After stimulation with 10 ng/mL Pam3CSK4 for designated time, RAW 264.7 macrophages indicated a time lag in <i>Mfhas1</i> expression. The expressions of <i>MFHAS1</i> and <i>GAPDH</i> were detected by western blotting. (C) The corresponding optical density of MFHAS1 bands normalized with GAPDH. (D) After stimulation with 10ng/mL Pam3CSK4 for designated time, THP-1 indicated a time lag in <i>MFHAS1</i> expression. The expressions of <i>MFHAS1</i> and <i>GAPDH</i> were detected by western blotting. (E) The corresponding optical density of MFHAS1 bands normalized with GAPDH. Data are presented as mean ± SD in each group. Image J was used in optical density measurement otherwise as indicated. *<i>p</i> < 0.05, compared with control.</p

MFHAS1 activates NF-κB, AP-1, and IL-6 expression 24 h after stimulation with Pam3CSK4 through TLR2.

<p>(A, B) HEK 293 cells and 293-MFHAS1 cells were transiently transfected with 100 ng TLR2 or 100 ng TLR2/50 ng CD14 expression plasmids, an100 ng NF-κB luciferase reporter plasmid (A) or 20 ng AP-1 luciferase reporter plasmid (B) and 10 ng renilla plasmid. 24 h post-transfected cells were exposed to mock treatment, Pam3CSK4 100 ng/mL or 10μg/mL. At 24 h posttreatment, fold increase in luciferase activity was measured for NF-κB or AP-1 activation using dual luciferase kits. The relative luciferase activity was calculated from the ratio of NF-κB/AP-1 (firefly) activity to renilla activity. (C, D) HEK 293 cells and 293-MFHAS1 cells were transiently transfected with 100 ng TLR2 or 100 ng TLR2/50 ng CD14 expression plasmids, and 24 h post-transfected cells were untreated or exposed to Pam3CSK4 100 ng/mL. After 24 h and 36 h posttreatment, induction of IL-6 expression was assayed by quantitative RT-PCR and normalized to β-actin (C). Cell supernatant was collected and the amounts of IL-6 were determined by ELISA (D). Values are the means ± SD from at least three independent experiments. *<i>p</i> < 0.05, **<i>p</i> < 0.01, or ***<i>p</i> < 0.001.</p

Biocatalytic Synthesis of Metaxalone and Its Analogues

A biocatalytic approach for the synthesis of metaxalone and its analogues was developed based on the reaction of epoxides and cyanate catalyzed by halohydrin dehalogenase. Gram-scale synthesis of chiral and racemic metaxalone was achieved with 44% (98% ee) and 81% yields, respectively, by protein engineering of the halohydrin dehalogenase HHDHamb from Acidimicrobiia bacterium. Additionally, various metaxalone analogues were synthesized at 28–40% yields (90–99% ee) for chiral forms and 77–92% yields for racemic forms

MFHAS1 activates pJNK in a time-dependent manner.

<p>(A) RAW 264.7 macrophages were transfected with HIS-MFHAS1 or pCDH empty vector plasmid, and 24 h post-transfected cells were untreated or treated with 10 ng/mL Pam3CSK4 for 6 h or 24 h. Cells were collected and pJNK, JNK, p-p65, GAPDH and HIS-MFHAS1 protein levels were determined by western blotting. (B) Quantified data of the pJNK and p-p65 levels. Levels of pJNK normalized to JNK levels, and pJNK/p-p65 normalized to GAPDH were shown.</p