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hyperforin dcha (MedChemExpress)

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MedChemExpress hyperforin dcha
Hyperforin Dcha, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 9 article reviews

hyperforin dcha - by Bioz Stars, 2026-05

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Structures of two bioactive compounds, hyperforin (14) and hypericin (18) , examined in our chemical analysis of the H. perforatum extracts and traditional formulas.

Journal: Frontiers in Microbiology

Article Title: The Chemical and Antibacterial Evaluation of St. John's Wort Oil Macerates Used in Kosovar Traditional Medicine

doi: 10.3389/fmicb.2017.01639

Figure Lengend Snippet: Structures of two bioactive compounds, hyperforin (14) and hypericin (18) , examined in our chemical analysis of the H. perforatum extracts and traditional formulas.

Article Snippet: Additionally, an authentic standard of hyperforin DCHA (AdipoGen Corp., Sandiego CA) with ≥97% purity was analyzed by the previously described LC-FTMS method to aid in identification of this compound in the various H. perforatum preparations.

Techniques:

Journal: Frontiers in Microbiology

Article Title: The Chemical and Antibacterial Evaluation of St. John's Wort Oil Macerates Used in Kosovar Traditional Medicine

doi: 10.3389/fmicb.2017.01639

Figure Lengend Snippet: Summary of key chemical data.

Techniques:

Mass spectrometry (MS) and MS/MS analysis of the peak data for oil macerates as reported in Figure <xref ref-type=

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Journal: Frontiers in Microbiology

Article Title: The Chemical and Antibacterial Evaluation of St. John's Wort Oil Macerates Used in Kosovar Traditional Medicine

doi: 10.3389/fmicb.2017.01639

Figure Lengend Snippet: Mass spectrometry (MS) and MS/MS analysis of the peak data for oil macerates as reported in Figure 8 .

Techniques: Mass Spectrometry

Inward and outward currents at −80 and +80 mV, respectively, from HEK-293 cells, stably expressing TRPC6 cDNA (HEK-TRPC6; a, c), non-transfected HEK (HEK) cells (e) and primary mouse cortical microglial cells (g). As indicated by the bars 100 μM OAG or 100 μM flufenamic acid (FFA; a), 1, 3 or 10 μM hyperforin supplied as dicyclohexylammonium (DCHA) salt (c, e), and 10 μM hyperforin supplied as free acid in methanol (MtOH; g) were applied. Currents were normalized to the cell size and basic currents before compound application were subtracted. The corresponding current-voltage relationships (IVs) are displayed in (b, d, f) and (h). Data represent means ± S.E.M. of the indicated number of experiments (cells).

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: Inward and outward currents at −80 and +80 mV, respectively, from HEK-293 cells, stably expressing TRPC6 cDNA (HEK-TRPC6; a, c), non-transfected HEK (HEK) cells (e) and primary mouse cortical microglial cells (g). As indicated by the bars 100 μM OAG or 100 μM flufenamic acid (FFA; a), 1, 3 or 10 μM hyperforin supplied as dicyclohexylammonium (DCHA) salt (c, e), and 10 μM hyperforin supplied as free acid in methanol (MtOH; g) were applied. Currents were normalized to the cell size and basic currents before compound application were subtracted. The corresponding current-voltage relationships (IVs) are displayed in (b, d, f) and (h). Data represent means ± S.E.M. of the indicated number of experiments (cells).

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques: Stable Transfection, Expressing, Transfection

Inward and outward currents at −80 and +80 mV, respectively, from primary microglial cells isolated from wild-type (a, h, k) and TRPC3/TRPC6-deficient mice (f, h). Currents were normalized to the cell size and, except in (h), basic currents before compound application were subtracted. As indicated by the bars different concentrations of hyperforin (a, f), 100 μM OAG or bath solution (no OAG; h) were applied. (b, g) and (i) display the corresponding IVs. (c) Dose-dependent changes of the normalized capacitance of the cells in (a). Sigmoidal fits of the maximal hyperforin-induced currents in (a) reveal a half-maximal concentration (EC 50 ) of 9.3 and 8.7 μM for inward (d) and outward currents (e), respectively. Microglial cells isolated from C3/C6-deficient (ko; f, g) and wild-type mice (a, b) reveal similar hyperforin-induced currents, and neither developed a specific current upon OAG application (h, i). (j) RT-PCR for TRPC6 (197 bp) and HPRT transcripts (160 bp) from 50 FACS-sorted microglial cells. Total RNA from brain served as control. (k) Hyperforin-induced currents in the presence (black) and absence of extracellular monovalent cations, replaced by NMDG + (blue), Cl − , replaced by aspartate (red), and Ca 2+ and Mg 2+ (0Ca0Mg; no substitute; green). (l) Corresponding IVs normalized to the current amplitude at 100 mV. Data represent means ± S.E.M. of the indicated number of experiments (cells).

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: Inward and outward currents at −80 and +80 mV, respectively, from primary microglial cells isolated from wild-type (a, h, k) and TRPC3/TRPC6-deficient mice (f, h). Currents were normalized to the cell size and, except in (h), basic currents before compound application were subtracted. As indicated by the bars different concentrations of hyperforin (a, f), 100 μM OAG or bath solution (no OAG; h) were applied. (b, g) and (i) display the corresponding IVs. (c) Dose-dependent changes of the normalized capacitance of the cells in (a). Sigmoidal fits of the maximal hyperforin-induced currents in (a) reveal a half-maximal concentration (EC 50 ) of 9.3 and 8.7 μM for inward (d) and outward currents (e), respectively. Microglial cells isolated from C3/C6-deficient (ko; f, g) and wild-type mice (a, b) reveal similar hyperforin-induced currents, and neither developed a specific current upon OAG application (h, i). (j) RT-PCR for TRPC6 (197 bp) and HPRT transcripts (160 bp) from 50 FACS-sorted microglial cells. Total RNA from brain served as control. (k) Hyperforin-induced currents in the presence (black) and absence of extracellular monovalent cations, replaced by NMDG + (blue), Cl − , replaced by aspartate (red), and Ca 2+ and Mg 2+ (0Ca0Mg; no substitute; green). (l) Corresponding IVs normalized to the current amplitude at 100 mV. Data represent means ± S.E.M. of the indicated number of experiments (cells).

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques: Isolation, Concentration Assay, Reverse Transcription Polymerase Chain Reaction

Inward and outward currents at −80 and +80 mV, respectively, from primary mouse microglial cells (a, d, h, j). As indicated by the bars either 10 μM hyperforin was applied at different external pH (pHx; a) or external pH was changed in the absence (h) or during 10 μM hyperforin (d) or 10 μM CCCP (j) application. Currents were normalized to the cell size and basic currents before compound application were subtracted. The corresponding IVs are displayed in (b, e, i) and (k). (c, f) and (l) show the change of the reversal potentials, during the experiments in (a, d) and (j), respectively. Note that the reversal potentials of the hyperforin- and CCCP-induced currents change with different external pH (see c, f and l), and that the IVs and the pH 5.4-dependent changes of the reversal potential are similar for hyperforin- and CCCP-induced currents (see e and k as well as f and l, respectively). In (g) all experimentally obtained values of reversal potentials of the hyperforin-induced currents (black dotes) are plotted versus the external pH (intracellular pH 7.2). The dotted red line in (g) depicts the H + reversal potentials calculated via the Nernst equation for a proton current at intracellular pH 7.2 and external pH as indicated (see experimental procedures). Data represent means ± S.E.M. of the indicated number of experiments (cells).

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: Inward and outward currents at −80 and +80 mV, respectively, from primary mouse microglial cells (a, d, h, j). As indicated by the bars either 10 μM hyperforin was applied at different external pH (pHx; a) or external pH was changed in the absence (h) or during 10 μM hyperforin (d) or 10 μM CCCP (j) application. Currents were normalized to the cell size and basic currents before compound application were subtracted. The corresponding IVs are displayed in (b, e, i) and (k). (c, f) and (l) show the change of the reversal potentials, during the experiments in (a, d) and (j), respectively. Note that the reversal potentials of the hyperforin- and CCCP-induced currents change with different external pH (see c, f and l), and that the IVs and the pH 5.4-dependent changes of the reversal potential are similar for hyperforin- and CCCP-induced currents (see e and k as well as f and l, respectively). In (g) all experimentally obtained values of reversal potentials of the hyperforin-induced currents (black dotes) are plotted versus the external pH (intracellular pH 7.2). The dotted red line in (g) depicts the H + reversal potentials calculated via the Nernst equation for a proton current at intracellular pH 7.2 and external pH as indicated (see experimental procedures). Data represent means ± S.E.M. of the indicated number of experiments (cells).

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques:

(a, c) Relative changes of the fluorescence ratio (F 490 /F 450 ) of the pH-sensitive dye BCECF-AM in HEK cells. As indicated by the bars different concentrations of hyperforin or 1% DMSO (a), or 20 mM NH 4 Cl (c) were applied. External NH 4 Cl induces intracellular alkalization and thus increase of F 490 /F 450 (c). The sigmoidal fit of the relative decrease of the BCECF ratio at different hyperforin concentrations, calculated at 200 s in respect to the control application of DMSO, reveal a half-maximal concentration (EC 50 ) of 8.5 μM (b). Normalized capacitance (e), intracellular pH changes (F 490 /F 450 ; f), inward and outward currents at −80 mV and +80 mV, respectively, normalized to the cell size (g), and reversal potential (h) before and during 10 μM hyperforin, measured in HEK cells with the free acid of BCECF in the patch pipette. (d) depicts the changes of the holding potential (V h ), providing the driving force for the currents. IVs, extracted at the indicated time points (see arrowheads in g) before and during 10 μM hyperforin, are displayed in (i) and (j), respectively. Data represent means ± S.E.M. of the indicated number of experiments (cells).

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: (a, c) Relative changes of the fluorescence ratio (F 490 /F 450 ) of the pH-sensitive dye BCECF-AM in HEK cells. As indicated by the bars different concentrations of hyperforin or 1% DMSO (a), or 20 mM NH 4 Cl (c) were applied. External NH 4 Cl induces intracellular alkalization and thus increase of F 490 /F 450 (c). The sigmoidal fit of the relative decrease of the BCECF ratio at different hyperforin concentrations, calculated at 200 s in respect to the control application of DMSO, reveal a half-maximal concentration (EC 50 ) of 8.5 μM (b). Normalized capacitance (e), intracellular pH changes (F 490 /F 450 ; f), inward and outward currents at −80 mV and +80 mV, respectively, normalized to the cell size (g), and reversal potential (h) before and during 10 μM hyperforin, measured in HEK cells with the free acid of BCECF in the patch pipette. (d) depicts the changes of the holding potential (V h ), providing the driving force for the currents. IVs, extracted at the indicated time points (see arrowheads in g) before and during 10 μM hyperforin, are displayed in (i) and (j), respectively. Data represent means ± S.E.M. of the indicated number of experiments (cells).

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques: Fluorescence, Concentration Assay, Transferring

(a) Inward and outward currents at −80 and +80 mV, respectively, from tight lipid bilayers at the tip of a patch pipette. As indicated by the bars either 10 μM hyperforin, 100 μM CCCP or 1% DMSO were applied. (b) depicts the current-voltage relationship (IV) of the basic current measured from the tight lipid bilayer. In (c) the corresponding IVs from the experiments in (a) are displayed after subtraction of the basic current (see b). Note that 10 μM hyperforin induced a significant conductance in the lipid bilayer. The protonophore CCCP (100 μM) yields a significant but much smaller current, and 1% DMSO did not result in any current at all (blue IV trace on top of x-axis in c). Data represent means ± S.E.M. of the indicated number of lipid bilayer experiments.

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: (a) Inward and outward currents at −80 and +80 mV, respectively, from tight lipid bilayers at the tip of a patch pipette. As indicated by the bars either 10 μM hyperforin, 100 μM CCCP or 1% DMSO were applied. (b) depicts the current-voltage relationship (IV) of the basic current measured from the tight lipid bilayer. In (c) the corresponding IVs from the experiments in (a) are displayed after subtraction of the basic current (see b). Note that 10 μM hyperforin induced a significant conductance in the lipid bilayer. The protonophore CCCP (100 μM) yields a significant but much smaller current, and 1% DMSO did not result in any current at all (blue IV trace on top of x-axis in c). Data represent means ± S.E.M. of the indicated number of lipid bilayer experiments.

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques: Transferring

(a) Inward and outward currents at −80 and +80 mV, respectively, from primary mouse chromaffin cells. The bar indicates application of 10 μM hyperforin. Currents were normalized to the cell size and basic currents before application were subtracted. (b) shows the corresponding IV. (c) Confocal picture of FFN511-dependent fluorescence in a chromaffin cell. (d, e) Relative changes of the FFN511-dependent fluorescence (F400, normalized to the value at start of application) in chromaffin cells from wild-type (d) and TRPC6-deficient mice (e). At the indicated time (arrow) 0.1% DMSO, 10 μM hyperforin or 70 mM KCl were applied in (d), and 0.1% DMSO, 10 μM hyperforin or 10 μM CCCP in (e). (f) depicts the statistical analysis of the remaining fluorescence (F400 in d and e) at 1400 s. The asterisks (* p < 0.05; ** p < 0.01) denote a significant difference to the corresponding control in 0.1% DMSO. (g) Representative pictures of FFN511-dependent fluorescence at the start and 1450 s after application of 0.1% DMSO (upper set) or 10 μM hyperforin (lower set) in chromaffin cells. The right panel shows the transmission image of the respective chromaffin cells. HEK cells do not reveal a significant fluorescence after FFN511 loading (h). (i) FFN511-dependent fluorescence (F400) in chromaffin cells after 15 min FFN511 incubation in the absence (0.1% DMSO control normalized to 100%) and presence of 10 μM hyperforin. Data represent means ± S.E.M. of the indicated number of experiments (cells) in (a) and (b), and of the indicated number (n) of experiments including x cells (n/x) in (d, e, f) and (i).

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: (a) Inward and outward currents at −80 and +80 mV, respectively, from primary mouse chromaffin cells. The bar indicates application of 10 μM hyperforin. Currents were normalized to the cell size and basic currents before application were subtracted. (b) shows the corresponding IV. (c) Confocal picture of FFN511-dependent fluorescence in a chromaffin cell. (d, e) Relative changes of the FFN511-dependent fluorescence (F400, normalized to the value at start of application) in chromaffin cells from wild-type (d) and TRPC6-deficient mice (e). At the indicated time (arrow) 0.1% DMSO, 10 μM hyperforin or 70 mM KCl were applied in (d), and 0.1% DMSO, 10 μM hyperforin or 10 μM CCCP in (e). (f) depicts the statistical analysis of the remaining fluorescence (F400 in d and e) at 1400 s. The asterisks (* p < 0.05; ** p < 0.01) denote a significant difference to the corresponding control in 0.1% DMSO. (g) Representative pictures of FFN511-dependent fluorescence at the start and 1450 s after application of 0.1% DMSO (upper set) or 10 μM hyperforin (lower set) in chromaffin cells. The right panel shows the transmission image of the respective chromaffin cells. HEK cells do not reveal a significant fluorescence after FFN511 loading (h). (i) FFN511-dependent fluorescence (F400) in chromaffin cells after 15 min FFN511 incubation in the absence (0.1% DMSO control normalized to 100%) and presence of 10 μM hyperforin. Data represent means ± S.E.M. of the indicated number of experiments (cells) in (a) and (b), and of the indicated number (n) of experiments including x cells (n/x) in (d, e, f) and (i).

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques: Fluorescence, Transmission Assay, Incubation

(a, b) Relative changes of the SBFI fluorescence ratio (F 340 /F 380 ), representing intracellular Na + changes (a), and the BCECF fluorescence ratio (F 490 /F 450 ), representing intracellular pH changes (b), in HEK cells during the application (see arrowhead) of 30 μM (a) and 10 μM (b) hyperforin in the presence and absence of Na + (replaced by NMDG + ). In (a) 0.3% DMSO was applied as control. In (b) control experiments without application of hyperforin are shown in faint colors. Data represent means ± S.E.M. of the indicated number (n) of experiments including x cells (n/x). (c) Mechanism of monoamine uptake (left side of the model): Cellular (synaptic) uptake of monoamines (MA + ) is arranged by the plasma membrane monoamine-sodium symporter (MAT; ( 1 )). The negative membrane potential and low intracellular Na + concentration provide the driving force for cellular Na + and MA + uptake. Vesicular monoamine uptake is arranged by the vesicular monoamine-proton antiporter (VMAT; ( 2 )), moving MA + into the vesicle in exchange for two protons. The huge H + gradient and the vesicular membrane potential, both established by the vesicular proton pump (H + -ATPase) drives H + out of the vesicle and thereby promotes vesicular MA + uptake. Effects of hyperforin on monoamine uptake (right side of the model): The protonophore action of hyperforin moves H + into the cell (synapse) due to the negative membrane potential ( 3 ). In addition, hyperforin moves H + out of the vesicles, driven by the huge H + gradient and positive vesicular membrane potential ( 4 ). The dissipation of the vesicular H + gradient ruins the driving force for the vesicular VMAT-dependent MA + uptake ( 2 ). The cytosolic acidification, mediated by the hyperforin-dependent H + influx and H + release from vesicles, increases the activity of the plasma membrane sodium-proton exchanger (NHE; ( 5 )), which is driven by the Na + gradient and the negative membrane potential, and moves one H + out of the cell in exchange of one Na + into the cell. This results in an increase of cytosolic Na + concentration, reducing the driving force for the MAT-dependent cellular MA + uptake ( 1 ).

Journal: Scientific Reports

Article Title: Protonophore properties of hyperforin are essential for its pharmacological activity

doi: 10.1038/srep07500

Figure Lengend Snippet: (a, b) Relative changes of the SBFI fluorescence ratio (F 340 /F 380 ), representing intracellular Na + changes (a), and the BCECF fluorescence ratio (F 490 /F 450 ), representing intracellular pH changes (b), in HEK cells during the application (see arrowhead) of 30 μM (a) and 10 μM (b) hyperforin in the presence and absence of Na + (replaced by NMDG + ). In (a) 0.3% DMSO was applied as control. In (b) control experiments without application of hyperforin are shown in faint colors. Data represent means ± S.E.M. of the indicated number (n) of experiments including x cells (n/x). (c) Mechanism of monoamine uptake (left side of the model): Cellular (synaptic) uptake of monoamines (MA + ) is arranged by the plasma membrane monoamine-sodium symporter (MAT; ( 1 )). The negative membrane potential and low intracellular Na + concentration provide the driving force for cellular Na + and MA + uptake. Vesicular monoamine uptake is arranged by the vesicular monoamine-proton antiporter (VMAT; ( 2 )), moving MA + into the vesicle in exchange for two protons. The huge H + gradient and the vesicular membrane potential, both established by the vesicular proton pump (H + -ATPase) drives H + out of the vesicle and thereby promotes vesicular MA + uptake. Effects of hyperforin on monoamine uptake (right side of the model): The protonophore action of hyperforin moves H + into the cell (synapse) due to the negative membrane potential ( 3 ). In addition, hyperforin moves H + out of the vesicles, driven by the huge H + gradient and positive vesicular membrane potential ( 4 ). The dissipation of the vesicular H + gradient ruins the driving force for the vesicular VMAT-dependent MA + uptake ( 2 ). The cytosolic acidification, mediated by the hyperforin-dependent H + influx and H + release from vesicles, increases the activity of the plasma membrane sodium-proton exchanger (NHE; ( 5 )), which is driven by the Na + gradient and the negative membrane potential, and moves one H + out of the cell in exchange of one Na + into the cell. This results in an increase of cytosolic Na + concentration, reducing the driving force for the MAT-dependent cellular MA + uptake ( 1 ).

Article Snippet: Hyperforin-dicyclohexylammonium (-DCHA) salt was obtained from Sigma, and hyperforin dissolved as free acid in methanol from Sigma and Biomol (Cayman Chemical).

Techniques: Fluorescence, Concentration Assay, Activity Assay

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