Find research datasets worth reusing

Fig. 1 in Real-time fluorescence imaging of anthocyanins complexed with diphenylboric acid 2-aminoethyl inside B16-F10 melanoma cells

Fig. 1. Fluorescence spectrometric analysis of (A) AN-rich chokeberry extract (AE) (black spectrum) and in the presence of DPBA (0.2%) (red spectrum), respective of (B) cyanidin-chloride standard (CY) free (black spectrum) and in the presence of DPBA (0.2%) (red spectrum). AE concentration: 9.2 μM, CY concentration: 92 μM. Excitation wavelength: 570 nm (A, B).

Fig. 6 in Real-time fluorescence imaging of anthocyanins complexed with diphenylboric acid 2-aminoethyl inside B16-F10 melanoma cells

Fig. 6. (A) AN cytotoxicity in B16–F10 murine melanoma cells after 24 h of incubation with different concentrations of anthocyanin-extract (AE), determined with the WST-1 assay; (B) B16–F10 cells viability after 24 h of incubation with different concentrations of AE (9.2 μM), respective CY (92 μM) and their complexed forms with DPBA (0.2%).

Fig. 5 in Real-time fluorescence imaging of anthocyanins complexed with diphenylboric acid 2-aminoethyl inside B16-F10 melanoma cells

Fig. 5. Representative chromatograms of the in-vitro metabolization and cellular absorption of cyanidin and cyanidin effects on the extract of AN obtained from chokeberry fruits, showing the identified compounds after 2 and 24 h of incubation with B16–F10 cells, in the cell culture medium. The main peaks are numbered according to Fig. 2A. Chromatograms were processed at 520 nm for cyanidin detection, and at 270 nm for cyanidin breakdown products. (A). AE 2 h, (B). AE 24 h, (C). CY 2 h, (D). CY 24 h.

Fig. 8 in Real-time fluorescence imaging of anthocyanins complexed with diphenylboric acid 2-aminoethyl inside B16-F10 melanoma cells

Fig. 8. (A) Histograms showing the fluorescence intensity of cellular AE/CY@DPBA following 2 h and 24 h incubation time. (B) Fluorescence measurement of B16–F10 melanoma cells, incubated for 2 and 24 h with AE (9.2 μM) and CY (92 μM) complexed with DPBA dye (0.2%).

Fig. 4 in Real-time fluorescence imaging of anthocyanins complexed with diphenylboric acid 2-aminoethyl inside B16-F10 melanoma cells

Fig. 4. HPLC/DAD/ESI+-MS total ion chromatograms of anthocyannins identified in the aqueous chokeberry extract (AE) and recorded at 520 nm: (A) m/z = 449, specific to Cy-3-gal and Cy-3-glu; (B) m/z = 419, characteristic for Cy-3- ara and Cy-3-xyl; and (C) m/z = 287, the CY aglycon fragment. For peak identification see Table 1.

Fig. 3 in Real-time fluorescence imaging of anthocyanins complexed with diphenylboric acid 2-aminoethyl inside B16-F10 melanoma cells

Fig. 3. Representative HPLC-DAD chromatograms of chokeberry AN containing extract (A) and the cyanidin chloride standard (B), recorded at 520 nm. Identified peaks at 520 nm correspond to (A): Cy-3-gal (peak 1), Cy-3-glu (peak 2), Cy-3-ara (peak 3), Cy-3-xyl (peak 4), and Cy (peak 5); (B). Cy-chloride.

Fig. 4 in Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin

Fig. 4. Superimposed structures between Gt5,3′ acyltransferase and vinorine synthase. Superposition was performed for four amino acids around the binding pocket (Ser45, Ala179, Phe182, and Gly402 in Gt5,3′ acyltransferase). The backbone structures are shown in cyan (caffeoyl-CoA-bound Gt5,3′AT) and green (vinorine synthase), respectively. The caffeoyl-CoA molecule is shown as a stick model. (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 Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin

Fig. 5. Summary of key amino acids for acyl-CoA specificity. The acyl-CoA binding pocket is illustrated with gray elongated semicircles. The upper and lower parts are binding pockets for malonyl/acetyl-CoA and caffeoyl/ coumaroyl-CoA, respectively. Four critical positions for acyl-CoA selectivity are indicated by blue ellipse. In the vicinity of these amino acid positions, the enzymes which have corresponding amino acid(s) are listed. The malonyl-CoA selective enzymes possess either Arg at the position 45/182, Val at the position 179, or Asp/Trp at the position 401 (upper part). In contrast, the caffeoyl/ coumaroyl-CoA selective enzymes have Ala/Gly at the position 179 and Gly/ Ser at the position 401 and include Arg neither at the position 45 nor 182 (lower part). PDB-ID is indicated in parentheses for enzymes with known structure. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 7 in Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin

Fig. 7. HPLC profiles of the reaction mixtures of delphinidin 3,5,3′-triglucoside and caffeoyl CoA with recombinant Gt5,3′ acyltransferase (A), EGAT (B), GEAT (C) and Eg5 acyltransferase (D). The representative reaction of three independent reactions is shown. The average ratios of the produced gentiodelphin to delphinidin 3- glucoside 5-caffeoyl-glucoside 3′-glucoside were 9.33%, 4.66%, 0.73%, and 0.58%, respectively.

Fig. 3 in Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin

Fig. 3. Caffeoyl-CoA binding site. The backbone structures are depicted as tubes, and the amino acid residues and caffeoyl-CoA are depicted as sticks. (A) Caffeoyl group interactions. Hydrogen bonds are indicated by dashed lines. (B) Backbone movement. The backbone structures of the apo and complexed form of Gt5,3′ acyltransferase are shown in blue and gray, respectively. The backbone shifts are indicated by arrows upon caffeoyl-CoA binding. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6. Delphinidin3,5,3 in Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin

Fig. 6. Delphinidin3,5,3′-triglucoside interaction model. The surface models are shown in blue (N-lobe) and green (C-lobe), respectively. (A) Putative binding site of delphinidin 3,5,3′-triglucoside. The binding site is indicated by magenta dots. (B) Docking models for Gt5,3′ acyltransferase•delphinidin 3,5,3′- triglucoside. Delphinidin 3,5,3′-triglucoside molecules are depicted by the stick model directing the position 5 to the bottom (left panel) and the position 3' (right panel). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 2 in Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin

Fig. 2. Molecular structure of Gt5,3′ acyltransferase. The structure is depicted by a ribbon model. The secondary structures are colored in pink (α-helices) and blue (β-strand). The caffeoyl-CoA molecule is shown as stick model, and the electron densities are contoured at 2.5σ. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6 in Characterization of the PRODUCTION of ANTHOCYANIN PIGMENT 1 Arabidopsis dominant mutant using DLEMMA dual isotope labeling approach

Fig. 6. Differential analysis of phenylpropanoid pathway metabolites between WT and pap1-D mutant Arabidopsis leaves. (A) Representation of differential metabolites found between WT and pap1-D in leaves. The data represents geometric fold change mean + standard deviation (SD) of four biological replicates. (B) The phenylpropanoid biosynthetic pathway and metabolites detected in the course of this study. The enzymes highlighted in red are those regulated by the PAP1 transcription factor according to the previous report from Tohge et al. (2005). Dash line denotes multiple enzymatic reactions in the pathway. PAL, phenylalanine ammonia-lyase; C4H, cinnamate 4-hydroxylase; 4CL, 4-coumarate-CoA ligase; CHS, chalcone synthase; CHI, chalcone isomerase; F3H, flavanone 3-hydroxylase; F3′H, flavonoid 3′-hydroxylase; FLS, flavonol synthase; FGT, flavonol glycosyltransferase; DFR, dihydroflavonol reductase; ANS, anthocyanidin synthase; AGT, anthocyani(di)n glycosyltransferase; AAT, anthocyanin acyltransferase. GST, glutathione S-transferase. The pathway was modified from Tohge et al. (2005).

Fig. 5 in Characterization of the PRODUCTION of ANTHOCYANIN PIGMENT 1 Arabidopsis dominant mutant using DLEMMA dual isotope labeling approach

Fig. 5. Linear correlation between labeling efficiency and metabolite location in the phenylpropanoid pathway. The number next to each point corresponds to metabolite location shown in Table 1. 'L' stands for location, the number after 'L' indicates its location in the phenylpropanoid pathway. The number in the bracket is used to distinguish metabolites that are at the same pathway location; LE: labeling efficiency. The color scale represents different percentage of labeling efficiency.

Fig. 2. A in Characterization of the PRODUCTION of ANTHOCYANIN PIGMENT 1 Arabidopsis dominant mutant using DLEMMA dual isotope labeling approach

Fig. 2. A representative example of metabolite identification using DLEMMA. (A) An isotopologue cluster was identified. All information necessary for metabolite identification such as retention time (RT), m/z values and number of labeled atoms, was depicted in a table (B) The raw MS data was first inspected (i.e. RT and m/z values) to validate the results obtained by the Miso software. (C) Elemental composition was then determined using the Masslynx software based on accurate unlabeled m/z and natural isotope patterns. Next, elemental compositions C15H16O9 was searched in SciFinder, and 108 possible candidates were found. The structural information obtained from the labeling patterns was then used to narrow down the number of candidates. Combined with MS/MS information, this metabolite was identified as sinapoyl malate.

Fig. 1 in Characterization of the PRODUCTION of ANTHOCYANIN PIGMENT 1 Arabidopsis dominant mutant using DLEMMA dual isotope labeling approach

Fig. 1. Overview of the DLEMMA workflow employed in this study. (A) Three differently labeled forms of phenylalanine (Phe) were used as feeding precursors, i.e. unlabeled, Label I (Phe-13C), and Label II (Phe-13C2H) Phe. (B) The two Arabidopsis genotype groups, WT and pap1-D, were fed with three forms of labeling 6 6 5 precursors for 24h. (C) Following feeding, the six treatments were combined (i.e. combinations A to F), in which four combinations were designed for metabolite identification and another two for semi-quantitative differential metabolite analysis. The extracts were analyzed by high resolution LC-MS in both positive and negative ion modes. (D) The LC-MS raw data was preprocessed with the R package XCMS, and next the R package Miso was used to detect and extract all Phe-derived mass features. (E) Phe-derived metabolites were identified based on retention time, m/z, MS/MS spectra, and dual-labeling patterns obtained from LC-MS analysis. (F) A combined sample matrices and label-swap approach was used to semi-quantitatively compare phenylpropanoids content between the WT and pap1- D genotypes.

Fig. 3. A in Characterization of the PRODUCTION of ANTHOCYANIN PIGMENT 1 Arabidopsis dominant mutant using DLEMMA dual isotope labeling approach

Fig. 3. A representative example demonstrating metabolite structure elucidation by DLEMMA in cases where multiple different labeling patterns are detected. An isotopologue cluster was detected with multiple different labeling patterns being observed, i.e. m/z+6, m/z+9, m/z+10, m/z+12, m/z+15, m/z+16 and m/z+19. Two possible elemental compositions were found for this metabolite. SciFinder database search revealed that only one structure matched all the 7 observed labeling patterns and this metabolite identified as Cyanidin 3-O-[2-O-(xylosyl)-6-O-(p-coumaroyl) glucoside] 5-O-malonylglucoside.

Fig. 4 in Characterization of the PRODUCTION of ANTHOCYANIN PIGMENT 1 Arabidopsis dominant mutant using DLEMMA dual isotope labeling approach

Fig. 4. Comparison of ion intensities of ferulic acid-hexose detected from phenylalanine fed and non-fed Arabidopsis leaves. (A) Extracted ion chromatogram (1) and mass spectrum (2) of ferulic acid-hexose from non-fed WT Arabidopsis. (B) Extracted ion chromatogram (1) and mass spectrum (2) of ferulic acid-hexose from unlabeled Phe fed WT Arabidopsis. Two isomers of ferulic acid-hexose, eluting at 6.10 and 6.66 min, were detected. The representative mass spectra are from ferulic acid-hexose isomer I (RT = 6.10 min). Peak areas of two ferulic acid-hexose isomers were used to compare their contents between non-fed and un-labeled Phe fed leaves.

opennotspecifiedJan 2021View details →

Fig. 7 in Identification of anthocyanin and other flavonoids from the green-blue petals of Puya alpestris (Bromeliaceae) and a clarification of their coloration mechanism

Fig. 7. In vitro reconstruction of the petal color using the purified anthocyanin (preternatin C5, 1), flavonol (myricetin 3,3′,5′-tri-O-glucoside, 2), and flavone (luteolin 4′-O-glucoside, 4). The absorption spectra of the mixture of 1 and 2 (1:0, 1:1 and 1:3, A–C), and 1 and 4 (1:0, 1:1 and 1:3, E–G) were measured after being dissolved in three McIlvaine buffers (pH 5.6, 6.2 and 6.8). (D and H) Photographs of the mixed solutions shown in B and F, respectively. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)