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Fig. 17 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 17. The potential structure-activity relationships of lignans in antitumor, anti-inflammatory and antioxidant effects.

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Fig. 16 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 16. Structure based activity distribution. (A) The proportion of pharmacological activities; (B) distribution of bioactivities in different classification.

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Fig. 15 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 15. Distribution of molecular resources analysis. (A) Main classifications of lignans; (B) distribution of lignan subclass structures; (C) distribution of lignans in top eight families.

opennotspecifiedJul 2022View details →

Fig. 4. Compounds 1, 21 in Six C21 steroidal glycosides from Cynanchum wallichii Wight roots and their multidrug resistance reversal activities

Fig. 4. Compounds 1, 21, and 25 can reverse drug resistance by decreasing P-gp, NF-κB, and c-jun gene and protein expression. (A–C) MDR1, NFκB, and JUN gene expression in MCF-ADR and HepG2-ADM cells following co-treatment with 1, 21, and 25 and Doxorubicin. (D–E) MDR1, NFκB, and Jun protein expression in MCFADR and HepG2-ADM cells treated with 1, 21, and 25 in combination with DOX.

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. 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.)

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.

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.