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opennotspecifiedAug 2021View details →

Fig. 3 in Unique localization of jasmonic acid-related compounds in developing Phaseolus vulgaris L. (common bean) seeds revealed through desorption electrospray ionization-mass spectrometry imaging

Fig. 3. LC-ESI-MS analysis of JA-related compounds in the extracts from the radicle and seed coat of developing Phaseolus vulgaris seeds. Base peak chromatogram of m/z 277.2173 ±10 ppm for (a) radicle and (b) seed coat, m/z 291.1966 ± 10 ppm for (c) radicle and (d) seed coat, and m/z 293.2122 ± 10 ppm for (e) radicle and seed coat, respectively. Peaks with arrow indicates JA-related compounds: (a) and (b) αLA, (c) and (d) OPDA, and (e) and (f) OPC-8:0. Compound names are defined in Table 1.

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).

Fig. 4 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 4. Docking of compounds 3, 9, 11, and 15 in human lipase enzyme. The original structure of the lipase enzyme (1LPB) contains the inhibitor methoxyundecylphosphinic acid (MUP, carbons coloured purple (A)). The docking results in lipase enzyme (B-E, green surface) with compounds 3 (pink, B), 9 (cyan, C), 11 (magenta, D), and 15 (green, E) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (S169, D193, and H280). Residues making hydrogen bonds with the ligands are indicated (B–E). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 3 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 3. Docking of compounds 3, 9, 11, and 15 in human α-amylase and α-glucosidase enzymes. The original structures of α-amylase (1XD0) and α-glucosidase (3TOP) enzymes contain the inhibitor acarbose (carbons coloured in orange and hexoses numbered in A and F, respectively). The docking results in α-amylase (B-E, light grey surface) and α-glucosidase (G-J, beige) enzymes with compounds 3 (pink, B and G), 9 (cyan, C and H), 11 (magenta, D and I), and 15 (green, E and J) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (R210, D212, E248, and R352 in α-amylase; D1420, E1423, and D1526 in α-glucosidase enzyme). Residues making hydrogen bonds with the ligands are indicated (B- E and G-J). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

opennotspecifiedDec 2021View details →

Fig. 8. Compound 4 inhibited IL-1 in Guaianolides from Artemisia codonocephala suppress interleukine-1β secretion in macrophages

Fig. 8. Compound 4 inhibited IL-1β production in THP-1 macrophages. (A) Immunofluorescence staining of IL-1β was performed. Scale bar = 10 μm. (B) The protein level of IL-1β in the culture medium from THP-1 cells was determined by ELISA. (C) Cleaved IL- 1β, NLRP3 and Caspase 1 in the supernatant or lysates of THP-1 cells were detected by western blotting. GAPDH was used as an internal loading control. (D) Expression of autophagy related proteins were detected by Western blotting. GAPDH was used as an internal loading control. (E) Expression of autophagy related proteins in THP-1 cells treated with or without 10 μM compound 4 and 5 mM 3-MA. GAPDH was used as an internal loading control. (F) mRFP- GFP-LC3 puncta were measured using a confocal microscope. Scale bar = 5 μm. (G) The levels of IL-1β in the culture medium from THP-1 cells treated with or without 10 μM compound 4 and 5 mM 3-MA. Data are expressed as means ± SD (n = 6). ###P <0.001, LPS + ATP vs. control, **P <0.01 and ***P <0.001, 4 vs. LPS + ATP.

opennotspecifiedOct 2021View details →

Fig. 5. Compounds 2 and 17 in Isolation, identification, and activity evaluation of diterpenoid alkaloids from Aconitum sinomontanum

Fig. 5. Compounds 2 and 17 exhibited potent inhibitory effects on the capsaicin mediated activation of TRPV1 channels expressed in HEK-293 cells. (A) Inhibition rate by compounds on the capsaicin mediated activation of TRPV1 channels expressed in HEK-293 cells. Compounds 1, 2, and 17 were evaluated at the concentration of 10 μM, the other compounds were evaluated at the concentration of 100 μM. (B) Activation of TRPV1 by capsaicin (0.5 μM), and inhibition of TRPV1 current by compound 2. Data are presented as the means ± SEM from three independent tests.

opennotspecifiedDec 2021View details →

Fig. 1 in Plant-cyanobacteria interactions: Beneficial and harmful effects of cyanobacterial bioactive compounds on soil-plant systems and subsequent risk to animal and human health

Fig. 1. Cyanobacterial active compounds induce negative, (A) ROS and enzyme activities such as superoxide dismutase (SOD), glutathione peroxidase (GPx), peroxidase (POD); and positive effects (B) expression of stress responsive genes (Ssglc and slr1562) that can have a positive effect on increasing plants' stress tolerance.

Fig. 5 in Seasonal variation of phenolic compounds in Zostera marina (Zosteraceae) from the Baltic Sea

Fig. 5. Amounts of individual flavonoids A), total flavonoids B), total phenolic acids C) and total phenolics D) in leaves of Zostera. Marina.

Fig. 4 in Seasonal variation of phenolic compounds in Zostera marina (Zosteraceae) from the Baltic Sea

Fig. 4. Chemical structure and HMBC key correlations of the methanolysis derivative 22 of 7′′,8′′ -didehydrosalvianolic acid B.

Fig. 1 in Seasonal variation of phenolic compounds in Zostera marina (Zosteraceae) from the Baltic Sea

Fig. 1. HPLC profile of crude water-methanol (1:1) leaf extracts of Zostera marina collected in Kiel coast. Compound numbers correspond to compounds in Fig. 2. Column: Phenomenex Luna Omega C18, 1.6 μm, 100 × 2.1 mm column; mobile phase A: 0.5% trifluoroacetic acid in water; mobile phase B: 100% acetonitrile; linear gradient: 0 min 10% B, 25 min 20% B, 40 min 50% B, 40.1 min 10% B, 55 min 10% B, stop; flow rate: 0.200 ml/min; injection volume: 5 μl; oven temperature: 30 ◦ C.

Fig. 6 in Seasonal variation of phenolic compounds in Zostera marina (Zosteraceae) from the Baltic Sea

Fig. 6. Relative content (%) of flavonoids A) and phenolic acids B) detected for each sampling period.

Fig. 2 in Seasonal variation of phenolic compounds in Zostera marina (Zosteraceae) from the Baltic Sea

Fig. 2. Structures of the flavonoids found in Zostera species. 1, apigenin; 2, apigenin 7-O-sulfate; 3, apigenin 7-O-glucoside; 4, apigenin 7-O-(6′′ -malonyl) glucoside; 5, luteolin; 6, luteolin 3′-O-sulfate; 7, luteolin 7-O-glucoside; 8, luteolin 7-O-(6′′ -malonyl) glucoside; 9, luteolin 7-O-sulfate; 10, luteolin 7,3′-O-disulfate; 11, diosmetin; 12, chrysoeriol; 13, diosmetin 3′-O-sulfate; 14, diosmetin 7-O-(6′′ -malonyl) glucoside; 15, diosmetin 7-O-sulfate; 16, chrysoeriol 7-O-sulfate; 17, diosmetin 7,3′-O-disulfate; 18, zosteric acid; 19, caffeic acid; 20, rosmarinic acid; 21, 7′′,8′′ -didehydrosalvianolic acid B.

Fig. 5 in Distribution of enzymatic and alkaline oxidative activities of phenolic compounds in plants

Fig. 5. UV chromatograms (280 nm) of non-oxidized (grey) and oxidized (black) samples of selected species, illustrating enzymatic oxidative activities of various types of compounds. Dihydroxysubstituted compounds, such as quercetin glycosides and caffeic acid derivatives, are oxidized more efficiently than their monohydroxysubstituted counterparts, i.e. kaempferol glycosides and coumaric acid derivatives.

Fig. 2 in Distribution of enzymatic and alkaline oxidative activities of phenolic compounds in plants

Fig. 2. Plant families arranged according to APG IV, and their phenolic compound classes and total phenolic levels. The dash () and one, two or three asterisks denote different average quantity levels depending on the compound class as follows: FC and ET: <1, 1–30, 31–60 and>60 mg/g; GA: <1, 1–10, 11–20 and>20 mg/ g; PC and PD: <1, 1–15, 16–30 and>30 mg/g; KA, QU and QA: <1, 1–5, 6–10 and>10 mg/g. For the oxidative activity column, dashes and asterisk represent the following: () No activity. The phenolic content of the samples is low overall (total phenolics concentration 10 mg/g or less) with no major peaks present, or the compounds are not affected by the oxidative conditions, the peak area variation remaining within ±10%. (*) Weak activity. The area of most major peaks have reduced by ca. 10–30%. (**) Moderate activity. The areas of most major peaks have reduced by ca. 30–60%. (***) High activity. The areas of most major peaks have reduced by>60%. Abbreviations: FC: Folin-Ciocalteu assay (i.e. total phenolics), HT: hydrolysable tannins, GA: gallic acid derivatives, ET: ellagitannins, PA: proanthocyanidins, PC: procyanidins, PD: prodelphinidins, FL: flavonols, KA: kaempferols, QU: quercetins, QA: quinic acid derivatives, Enz: enzymatic oxidative activity, pH10: alkaline oxidative activity at pH 10. a Myricetin has been left out because of its low quantity in the sample set. It was detected in 20 families, with a maximum concentration of 7 mg/g.

Fig. 4 in Distribution of enzymatic and alkaline oxidative activities of phenolic compounds in plants

Fig. 4. UV chromatograms (280 nm) of non-oxidized (grey) and oxidized (black) samples of selected species, illustrating alkaline oxidative activities of various types of compounds. Monohydroxysubstituted compounds, such as kaempferol glycosides, are inactive. The same applies for compounds containing a catechol moiety, e.g. catechin, quercetin glycosides and procyanidins. However, if the catechol moiety is at the end of an alkane chain, as is the case with e.g. rosmarinic acid, rubranoside A, and oregonin, the alkaline oxidative activity is greatly increased. Myricetin glycosides, prodelphinidins, gallic acid derivatives and ellagitannins – all containing a pyrogallol moiety – are highly active and oxidize completely.

Fig. 3 in Distribution of enzymatic and alkaline oxidative activities of phenolic compounds in plants

Fig. 3. Phenolic compound structures quantified using MRM methods of Engstr¨om et al. (2015, 2014), and how the measurements are related to each other.

Fig. 1 in Distribution of enzymatic and alkaline oxidative activities of phenolic compounds in plants

Fig. 1. The content of phenolic compounds, recorded at 280 nm, in nonoxidized (grey) and enzymatically oxidized (black) Trifolium pratense flowers. The peak area of clovamide has decreased by 91%, likely due to oxidation, whereas flavonols only have lost ca. 11% of their peak areas. A moderate, 26% decrease in total phenolics suggests that the sample retains most of its phenolic compounds, supporting these observations.

opennotspecifiedOct 2020View details →

Fig. 7. Compounds 1a, 1b, 4a and 4b reduced H2O2-induced apoptosis. The cells were treated with 1a, 1b, 4a and 4b in Lignans and neolignans with isovaleroyloxy moiety from Solanum lyratum Thunb.: Chiral resolution, configurational assignment and neuroprotective effects

Fig. 7. Compounds 1a, 1b, 4a and 4b reduced H2O2-induced apoptosis. The cells were treated with 1a, 1b, 4a and 4b at 50 μM for 48 h. The nuclear changes were determined by Hoechst 33258 staining observed with a fluorescence microscope. Arrows: apoptotic cells. Scale bar: 50 μm.