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opennotspecifiedApr 2022View details →

Fig. 3 in Undescribed ecdysteroids and phenolic glycosides from the roots of Cyathula officinalis Kuan and their anti-inflammatory activity in LPS-induced RAW 264.7 macrophages in vitro

Fig. 3. NMR calculation results of two plausible stereoisomers of 1 at the B3LYP-D3 (BJ)/6-31G** level.

opennotspecifiedOct 2022View details →

Fig. 3 in Undescribed specialised metabolites from the endophytic fungus Emericella sp. XL029 and their antimicrobial activities

Fig. 3. Key NOESY correlations of compounds 2–7. (Asterisk (*) indicates the partial structures of compounds).

opennotspecifiedApr 2022View details →

Fig. 5 in Undescribed ecdysteroids and phenolic glycosides from the roots of Cyathula officinalis Kuan and their anti-inflammatory activity in LPS-induced RAW 264.7 macrophages in vitro

Fig. 5. Effects of different concentrations (10, 20, 40 μM)) of 1 on LPS-stimulated release of (A) TNF-α, (B) IL-6, and (C) IL-1β in RAW 264.7 cells. The values represent the mean ± SD of three independent experiments, and differences between the mean values were assessed by Student's t-test. ##P <0.01 vs. the control group, *P <0.05 vs. the LPS group, **P <0.01 vs. the LPS group.

opennotspecifiedApr 2022View details →

Fig. 4 in Undescribed ecdysteroids and phenolic glycosides from the roots of Cyathula officinalis Kuan and their anti-inflammatory activity in LPS-induced RAW 264.7 macrophages in vitro

Fig. 4. Effect of 1–6 (40 μM) on NO release in LPS-induced RAW 264.7 cells in vitro. Dexamethasone was used as a positive control in this experiment, and the concentration was 5 μM. The data represent the mean ± SD of three independent experiments.

opennotspecifiedMar 2022View details →

Fig. 3. 4 in Undescribed polyether ionophores from Streptomyces cacaoi and their antibacterial and antiproliferative activities

Fig. 3. 4 treatment results in proteasome inhibition and ER stress. A) Proteasomal activity was determined via Suc-Leu-Leu-Val-Tyr AMC. 1 μM Mg132 was used as a proteasome inhibitor. Reported values were normalized to cells treated with vehicle. Error bars represent standard deviation. p-values were calculated with respect to the vehicle-treated cells (****p <0.0001). B) The level of K48-linked ubiquitinated proteins was determined by IB. C) After cells were treated with 4 or vehicle for 24 h, soluble and insoluble protein fractions were prepared, then the levels of K48-linked ubiquitinated proteins were investigated. D) Following A549 cells were treated with 10 and 20 μM 4 or vehicle for 24 h, CHOP and BIP protein levels were determined via IB. E) ROS production was determined via 2′,7′-Dichlorodihydrofluorescein diacetate (DCFH). 200 mM H2O2 was used as a positive control (1 h). Error bars represent standard deviation and p-values were calculated with respect to vehicle-treated cells. (**p = 0.009, ***p = 0.0002, ****p <0.0001).

opennotspecifiedMar 2022View details →

Fig. 2. 4 in Undescribed polyether ionophores from Streptomyces cacaoi and their antibacterial and antiproliferative activities

Fig. 2. 4 triggers apoptosis and inhibits autophagic flux similar to K41-A. (A–D) A549 cells were treated with 4 (10 and 20 μM), K41-A (7 and 14 μM), or vehicle for 24 h. A) Expression level of cleaved and full length of PARP-1 was analyzed via immunoblotting (IB). (* indicate overexposure of full-length PARP-1.) B) Conversion of LC3-I to LC3-II, C) p62 level, and D) Atg-7 levels were determined via IB. (E-F) A549 cells which stably express mCherry-GFP-LC3 probe were treated with 20 μM 4, 14 μM K41-A or vehicle. Additionally, 100 ng/mL Bafilomycin was used as positive control which blocks autophagic flux. E) The mCherry-GFP-LC3 expression was visualized by fluorescence microscopy and the representative data are shown. F) Percentage of autophagosomes (mCherry+/GFP+, yellow puncta) and autolysosomes (mCherry+/GFP, red puncta) number were quantified by counting at least 40 cells. Error bars represent standard deviation and p-values were calculated with respect to vehicle-treated cells.

dryad32/100

Transformable nano-antibiotics for mechanotherapy and immune activation against drug-resistant Gram-negative bacteria

<p><span>The dearth of antibiotic candidates against Gram-negative bacteria and the rise of antibiotic resistance create a global health concern. The challenge lies in the unique Gram-negative bacterial outer membrane that provides the impermeable barrier for antibiotics and sequesters antigen presentation. We designed a transformable nano-antibiotics (TNA) which can transform from nontoxic nanoparticles to bactericidal nanofibrils with reasonable rigidity (Young's modulus, 21.6 ± 5.9 MPa) after targeting β-barrel assembly machine A (BamA) and lipid polysaccharides (LPS) of Gram-negative bacteria. After morphological transformation, the TNA can penetrate and damage the bacterial envelope, disrupt electron transport and multiple conserved biosynthetic and metabolic pathways, burst bacterial antigen release from the outer membrane, and subsequently activate innate and adaptive immunity. TNA kills Gram-negative bacteria in vitro and in vivo with undetectable resistance through multiple bactericidal modes of action. TNA-treatment-induced vaccination results in rapid and long-lasting immune responses, protecting against lethal re-infections.</span></p>

opencc-zeroAug 2023View details →

Fig. 8 in Five undescribed steroids from Talaromyces stipitatus and their cytotoxic activities against hepatoma cell lines

Fig. 8. Nuclear morphology changes in Hep3B cells assessed by fluorescence microscopy using DAPI staining. Cells were incubated for 48 h with (a) 0.2% DMSO; (b) compound 4 at 5 μM; (c) compound 8 at 5 μM; and (d) sorafenib at 3.5 μM. Arrows show apoptotic cells. The results are representative of three different experiments.

Fig. 6 in Five undescribed steroids from Talaromyces stipitatus and their cytotoxic activities against hepatoma cell lines

Fig. 6. Cell cycle phases of Hep3B cells. Cells were treated for 24 h with (a) 0.2% DMSO; (b) compound 4 at 5 μM; (c) compound 8 at 5 μM; and (d) sorafenib at 3.5 μM. After labeling with PI staining solution, the cells were subjected to flow cytometry. Diagrams of the cell cycle phases are shown ***p <0.001 compared with the control group.

Fig. 7 in Five undescribed steroids from Talaromyces stipitatus and their cytotoxic activities against hepatoma cell lines

Fig. 7. Apoptosis in Hep3B cells induced by compounds 4 and 8. Cells were treated with (a, e) 0.1% DMSO (control); (b, f) compound 4 at 5 μM; (c, g) compound 8 at 5 μM, and (d, h) sorafenib at 3.5 μM for a period of 24 and 48 h. The four subpopulations indicate Q4, viable; Q3, early apoptotic; Q2, late apoptotic; and Q1, necrotic. Quantification of the percentage of cells in each quadrant is shown. ***p <0.001, ****p <0.0001 compared with the control group.

Fig. 3 in A detailed DFT-based study of the free radical scavenging activity and mechanism of daphnetin in physiological environments

Fig. 3. Transition states geometries related to the reactions of DAP with HO•, HOO•, and NO • in water.

Fig. 5 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 5. Effects of 2 (A), 3 (B), and 6 (C) on RANKL-induced osteoclastogenesis in BMMs. These compounds inhibit RANKL-induced differentiation of BMMs into osteoclast. Mouse BMMs were seeded into 96 well-plates in the presence of M-CSF (30 ng/mL) and RANKL (100 ng/mL) with or without different concentrations (0, 3, 10, 30 μM) of 2, 3, and 6 for 6 days, and then cells were stained for TRAP. The quantities of TRAP-positive multinucleated (>5 nuclei) osteoclasts were determined following image capture (magnification, ×40). Data were presented as the mean ±SE (P <0.05).

Fig. 3 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 3. Calculated and experimental ECD spectra of 1 (left) and experimental ECD spectrum of 2–7 (right) in MeOH.

Fig. 2 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 2. Key HMBC (blue arrows) and COSY (black bold) correlations for compounds 1–3 and 5–8. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6. Compound 6 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 6. Compound 6 suppresses resorption pits in BMMs. BMMs were incubated with M-CSF (30 ng/mL) and RANKL (100 ng/mL) on Corning OsteoAssay Surface 24 well-plates and treated with indicated concentrations of compound 6 for seven days. The cells were washed, and the pit area was determined by using Image J software. Data are presented as the mean ±SE (P <0.05).

Fig. 4 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 4. Antiosteoclastogenic effect from isolated compounds. (A) RAW264.7 cells were cultured into 96 well-plates under stimulation of RANKL (100 ng/mL) with or without indicated compounds (10 μM) for four days, then the cells were stained for TRAP. The quantities of TRAP-positive multinucleated (>5 nuclei) osteoclasts were presented as the mean ±SE (P <0.01, versus vehicle-treated control; n =3). (B) RAW264.7 cells were plated in 96 well-plates and incubated with M-CSF (30 ng/mL) in the presence of indicated concentrations of isolated compounds for 48 h. Cell viability was measured by MTT assay. Data were presented as the mean ±SE (P <0.01, versus vehicle-treated control; n =3).

Fig. 3 in Polyacetylene glucosides from the florets of Carthamus tinctorius and their anti-inflammatory activity

Fig. 3. The inhibitory effect of compound 1 against LPS-induced NO production in RAW264.7 cells. (A) The content of NO in RAW264.7 cells in the blank control group, model group (1 μg/mL LPS), and compound 1 group [LPS (1 μg/mL) + compound 1 (3.13, 6.25, 12.5, 25, or 50 μM)]. (B) The inhibition rates of compound 1 and positive control (curcumin) against LPS-induced NO production in RAW264.7 cells. Results are presented as the mean ± SEM for three individual experiments. ##P <0.01 vs. control group; *P <0.05, **P <0.01 vs. model group.

Fig. 4 in Acylphloroglucinol derivatives with ATP citrate lyase inhibitory activities from Syzygium oblatum Wall.

Fig. 4. (A) The predicted binding mode of 1 with ACLY and the ligand is shown as yellow sticks. (B) A two-dimensional plot showing the interactions between 1 and the surrounding amino acids. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 5 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 5. Docking of compounds 3, 9, 11 and 15 in human lipase. The structure of lipase (green surface) with the residues lining the binding pocket (sticks with white carbons) and the catalytic resides (S169, D193 and H280 in yellow). The docking results in lipase with compounds 3 (pink, A), 9 (cyan, B), 11 (magenta, C) and 15 (green, D) are shown with their main interacting residues labelled, hydrogen bonds and binding energies. (E) Zoom in on the superimposition of the docked compounds 3, 9, 11 and 15 (coloured as in A-D) with the position of the aromatic rings encircled and the residues, which interact with all compounds of them, are labelled. (F) The original structure of lipase (1LPB) contains the inhibitor methoxy-undecylphosphinic acid (MUP in purple). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 2 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 2. In vitro inhibition activities.α-Amylase inhibition (A) andα-glucosidase inhibition (B) by acarbose and the pure active compounds. (C) Pancreatic lipase inhibition by orlistat and the pure active compounds. In each test, data are expressed as IC50 values in μM and values with the same letter (a–h) are not significantly different at p ≤ 0.05 level, according to a one-way analysis of variance (ANOVA).