RESUMEN
Bifurcating electron transfer flavoproteins (Bf ETFs) are important redox enzymes that contain two flavin adenine dinucleotide (FAD) cofactors, with contrasting reactivities and complementary roles in electron bifurcation. However, for both the "electron transfer" (ET) and the "bifurcating" (Bf) FADs, the only charged amino acid within 5 Å of the flavin is a conserved arginine (Arg) residue. To understand how the two sites produce different reactivities utilizing the same residue, we investigated the consequences of replacing each of the Arg residues with lysine, glutamine, histidine, or alanine. We show that absence of a positive charge in the ET site diminishes accumulation of the anionic semiquinone (ASQ) that enables the ET flavin to act as a single electron carrier, due to depression of the oxidized versus. ASQ reduction midpoint potential, E°OX/ASQ. Perturbation of the ET site also affected the remote Bf site, whereas abrogation of Bf FAD binding accelerated chemical modification of the ET flavin. In the Bf site, removal of the positive charge impaired binding of FAD or AMP, resulting in unstable protein. Based on pH dependence, we propose that the Bf site Arg interacts with the phosphate(s) of Bf FAD or AMP, bridging the domain interface via a conserved peptide loop ("zipper") and favoring nucleotide binding. We further propose a model that rationalizes conservation of the Bf site Arg even in non-Bf ETFs, as well as AMP's stabilizing role in the latter, and provides a mechanism for coupling Bf flavin redox changes to domain-scale motion.
Asunto(s)
Arginina , Flavina-Adenina Dinucleótido/análogos & derivados , Adenosina Monofosfato/metabolismo , Arginina/metabolismo , Transporte de Electrón , Flavoproteínas Transportadoras de Electrones/química , Flavoproteínas Transportadoras de Electrones/metabolismo , Flavina-Adenina Dinucleótido/química , Flavina-Adenina Dinucleótido/metabolismo , Flavinas/química , Flavinas/metabolismo , Oxidación-ReducciónRESUMEN
Two new natural diols, (2S, 3S, 4S)-4-methyl-1-phenylhexane-2,3-diol (1) and (2S, 3S)-4-methyl-1-phenylpentane-2,3-diol (2), together with five known compounds, xenocyloins B-D (3-5), lumichrome (6) and thymidine (7) were isolated from Streptomyces sp. CB09001. The absolute configurations of 1 and 2 were established by crystallographic structure analysis. The anti-inflammatory effects of 1-7 were also investigated in RAW246.7 murine macrophage cells stimulated by lipopolysaccharide. The indole derivative xenocyloin B (3) significantly inhibited inducible nitric oxide synthase expression in RAW264.7 cells and could be a potential anti-inflammatory drug lead.
Asunto(s)
Antiinflamatorios no Esteroideos/química , Antiinflamatorios no Esteroideos/farmacología , Streptomyces/química , Animales , Cristalografía por Rayos X , Evaluación Preclínica de Medicamentos , Flavinas/química , Flavinas/farmacología , Indoles/química , Indoles/farmacología , Lipopolisacáridos/farmacología , Ratones , Estructura Molecular , Óxido Nítrico Sintasa de Tipo II/antagonistas & inhibidores , Óxido Nítrico Sintasa de Tipo II/metabolismo , Células RAW 264.7 , Streptomyces/metabolismoRESUMEN
The availability of electrons to biological systems underpins the mitochondrial electron transport chain (ETC) that powers living cells. It is little wonder, therefore, that the sufficiency of electron supply is critical to cellular health. Considering mitochondrial redox activity alone, a lack of oxygen (hypoxia) leads to impaired production of adenosine triphosphate (ATP), the major energy currency of the cell, whereas excess oxygen (hyperoxia) is associated with elevated production of reactive oxygen species (ROS) from the interaction of oxygen with electrons that have leaked from the ETC. Furthermore, the redox proteome, which describes the reversible and irreversible redox modifications of proteins, controls many aspects of biological structure and function. Indeed, many major diseases, including cancer and diabetes, are now termed "redox diseases", spurring much interest in the measurement and monitoring of redox states and redox-active species within biological systems. In this Account, we describe recent efforts to develop magnetic resonance (MR) and fluorescence imaging probes for studying redox biology. These two classes of molecular imaging tools have proved to be invaluable in supplementing the structural information that is traditionally provided by MRI and fluorescence microscopy, respectively, with highly sensitive chemical information. Importantly, the study of biological redox processes requires sensors that operate at biologically relevant reduction potentials, which can be achieved by the use of bioinspired redox-sensitive groups. Since oxidation-reduction reactions are so crucial to modulating cellular function and yet also have the potential to damage cellular structures, biological systems have developed highly sophisticated ways to regulate and sense redox changes. There is therefore a plethora of diverse chemical structures in cells with biologically relevant reduction potentials, from transition metals to organic molecules to proteins. These chemical groups can be harnessed in the development of exogenous molecular imaging agents that are well-tuned to biological redox events. To date, small-molecule redox-sensitive tools for oxidative stress and hypoxia have been inspired from four classes of cellular regulators. The redox-sensitive groups found in redox cofactors, such as flavins and nicotinamides, can be used as reversible switches in both fluorescent and MR probes. Enzyme substrates that undergo redox processing within the cell can be modified to provide fluorescence or MR readout while maintaining their selectivity. Redox-active first-row transition metals are central to biological homeostasis, and their marked electronic and magnetic changes upon oxidation/reduction have been used to develop MR sensors. Finally, redox-sensitive amino acids, particularly cysteine, can be utilized in both fluorescent and MR sensors.
Asunto(s)
Medios de Contraste/química , Flavinas/química , Colorantes Fluorescentes/química , Niacinamida/análogos & derivados , Animales , Células HeLa , Humanos , Imagen por Resonancia Magnética , Ratones , Imagen Óptica , Oxidación-Reducción , Células RAW 264.7RESUMEN
The flavin-dependent monooxygenase Sam5 was previously reported to be a bifunctional hydroxylase with a coumarte 3-hydroxylase and a resveratrol 3'-hydroxylase activity. In this article, we showed the Sam5 enzyme has 3'-hydroxylation activities for methylated resveratrol (pinostilbene and pterostilbene), hydroxylated resveratrol (oxyresveratrol) and glycosylated resveratrol (piceid) as substrates. However, the use of piceid, a glycone type stilbene, as a substrate for bioconversion experiments with the Sam5 enzyme expressed in, Escherichia coli does not convert to the hydroxylated compound astringin, but it has converted in vitro enzyme reactions. Finally, we report a novel catalytic activity of Sam5 monooxygenase for the synthesis of piceatannol derivatives, 3'-hydroxylated stilbene compounds. Development of this bioproduction method for the hydroxylation of stilbenes is challenging because of the difficulty in expressing P450-type hydroxylase in E. coli and regionspecific chemical synthesis.
Asunto(s)
Flavinas/química , Flavinas/metabolismo , Oxigenasas de Función Mixta/metabolismo , Estilbenos/química , Estilbenos/metabolismo , Dinitrocresoles/metabolismo , Escherichia coli/metabolismo , Glucósidos/metabolismo , Hidroxilación , Extractos Vegetales/metabolismo , ResveratrolRESUMEN
Aspergillus fumigatus is a human pathogen responsible for deadly infections in immune-compromised patients. A potential strategy for treating A. fumigatus infections is by targeting the biosynthesis of cell wall components, such as galactofuranase, which is absent in humans. Galactofuranose biosynthesis is initiated by the flavoenzyme UDP-galactopyranose mutase (UGM), which converts UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf). UGM requires the reduced form of the flavin for activity, which is obtained by reacting with NADPH. We aimed to identify inhibitors of UGM by screening a kinase inhibitor library using ThermoFAD, a flavin fluorescence thermal shift assay. The screening assay identified flavopiridol as a compound that increased the melting temperature of A. fumigatus UGM. Further characterization showed that flavopiridol is a non-competitive inhibitor of UGM and docking studies suggest that it binds in the active site. This compound does not inhibit the prokaryotic UGM from Mycobacteria tuberculosis.
Asunto(s)
Aspergillus fumigatus/enzimología , Evaluación Preclínica de Medicamentos/métodos , Inhibidores Enzimáticos/química , Flavonoides/química , Transferasas Intramoleculares/antagonistas & inhibidores , Piperidinas/química , Espectrometría de Fluorescencia/métodos , Activación Enzimática , Flavinas/química , Transferasas Intramoleculares/análisis , Mapeo de Interacción de Proteínas , TemperaturaRESUMEN
The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into the mechanisms behind the sensitivity of this enzyme toward visible light. We propose that a pocket on the si-face of the isoalloxazine ring accommodates oxygen that reacts with photo-excited FAD generating superoxide and a flavin radical that oxidize the isoalloxazine ring C7α methyl group and a nearby tyrosine residue. This tyrosine and key residues surrounding the oxygen pocket are conserved in enzymes from related bacteria, including pathogens such as Staphylococcus aureus. Photo-sensitivity may thus be a widespread feature among bacterial TrxR with the described characteristics, which affords applications in clinical photo-therapy of drug-resistant bacteria.
Asunto(s)
Lactococcus lactis/enzimología , Lactococcus lactis/efectos de la radiación , Luz , Estrés Oxidativo , Procesos Fotoquímicos , Reductasa de Tiorredoxina-Disulfuro/química , Reductasa de Tiorredoxina-Disulfuro/metabolismo , Flavina-Adenina Dinucleótido/metabolismo , Flavinas/química , Flavinas/metabolismo , Redes y Vías Metabólicas , Modelos Moleculares , Conformación Molecular , Oxidación-Reducción , Relación Estructura-ActividadRESUMEN
This article describes discovery of a novel and new class of cholinesterase inhibitors as potential therapeutics for Alzheimer's disease. A series of novel isoalloxazine derivatives were synthesized and biologically evaluated for their potential inhibitory outcome for both acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). These compounds exhibited high activity against both the enzymes AChE as well as BuChE. Of the synthesized compounds, the most potent isoalloxazine derivatives (7m and 7q) showed IC50 values of 4.72 µM and 5.22 µM respectively against AChE; and, 6.98 µM and 5.29 µM respectively against BuChE. These two compounds were further evaluated for their anti-aggregatory activity for ß-amyloid (Aß) in presence and absence of AChE by performing Thioflavin-T (ThT) assay and Congo red (CR) binding assay. In order to evaluate cytotoxic profile of these two potential compounds, cell viability assay of SH-SY5Y human neuroblastoma cells was performed. Further, to understand the binding behavior of these two compounds with AChE and BuChE enzymes, docking studies have been reported.
Asunto(s)
Inhibidores de la Colinesterasa/síntesis química , Flavinas/química , Acetilcolinesterasa/química , Acetilcolinesterasa/metabolismo , Enfermedad de Alzheimer/tratamiento farmacológico , Enfermedad de Alzheimer/patología , Sitios de Unión , Butirilcolinesterasa/química , Butirilcolinesterasa/metabolismo , Línea Celular Tumoral , Supervivencia Celular/efectos de los fármacos , Inhibidores de la Colinesterasa/uso terapéutico , Inhibidores de la Colinesterasa/toxicidad , Evaluación Preclínica de Medicamentos , Flavinas/uso terapéutico , Flavinas/toxicidad , Humanos , Simulación del Acoplamiento Molecular , Estructura Terciaria de Proteína , Relación Estructura-ActividadRESUMEN
Long grains of Hordeum vulgare and Sorghum bicolor were individually fermented with Monascus purpureus MTCC 369 under solid state fermentation. The aqueous extract of Monascus which fermented H. vulgare and S. bicolor was found to contain five different new metabolites. Silica gel column chromatography of the aqueous extract with a linear gradient of ethyl acetate, acetonitrile and carbon tetrachloride (v/v) yielded five new metabolites named benzopranyl capriate (9H-1-isoprenyl-benzopyran-5-isopropanoic acid-6-ol-6-n-decanoate), shorghumoic acid (n-octadec-8,11-dien-7α-ol-1-oic acid) and sorghumflavin A (2-n-butyloxo-6-ß-hydroxy-7-ß-isoprenyl ankaflavin) from Monascus-fermented S. bicolor, while hordeumflavin B (2-n-undecanyloxo-7-ß-isoprenyl ankaflavin) and vulgaredilone (2-dodecanyl-7-ß isopranyl monoscodilone) from Monascus-fermented H. vulgare.
Asunto(s)
Flavinas/aislamiento & purificación , Hordeum/química , Monascus/metabolismo , Extractos Vegetales/análisis , Semillas/química , Sorghum/química , Fermentación , Flavinas/química , Estructura Molecular , Semillas/metabolismo , AguaRESUMEN
The root accumulation and excretion of riboflavin (Rbfl) and Rbfl derivatives have been studied in the model legume species Medicago truncatula, grown in hydroponics in two different Fe deficiency conditions, with and without CaCO(3). Using high resolution mass spectrometry techniques coupled to liquid chromatography, three different flavin derivatives not previously reported in plants, putatively identified as 7-hydroxy-Rbfl, 7α-hydroxy-Rbfl and 7-carboxy-Rbfl, were found along with Rbfl in Fe-deficient M. truncatula roots. In the presence of CaCO(3) most of the flavins were accumulated in the roots, whereas in the absence of CaCO(3) there was partial export to the nutrient solution. The major flavins in roots and nutrient solution were Rbfl and 7-hydroxy-Rbfl, respectively. Flavins were located in the root cortex and epidermal cells, preferentially in a root region near the apex that also exhibited increased ferric chelate reductase (FCR) activity. Six out of 15 different species of horticultural interest showed root increases in both Rbfl (four of them also having Rbfl derivatives) and FCR. No significant correlation was found between Rbfl and either phosphoenolpyruvate carboxylase or FCR activities, whereas the latter two showed a good correlation between them. The possible roles of Rbfl and Rbfl derivatives in roots and nutrient solutions are discussed. Medicago truncatula is proposed as a model system for flavin studies.
Asunto(s)
Flavinas/metabolismo , Deficiencias de Hierro , Medicago truncatula/metabolismo , Raíces de Plantas/metabolismo , Ácidos/metabolismo , Transporte Biológico , Cromatografía Líquida de Alta Presión , FMN Reductasa/metabolismo , Flavinas/análisis , Flavinas/química , Fluorescencia , Iones , Espectrometría de Masas , Medicago truncatula/enzimología , Medicago truncatula/crecimiento & desarrollo , Oxidación-Reducción , Fosfoenolpiruvato Carboxilasa/metabolismo , Filogenia , Extractos Vegetales/química , Análisis de Componente Principal , Estándares de Referencia , Riboflavina/metabolismo , Soluciones , Especificidad de la Especie , Espectrofotometría UltravioletaRESUMEN
The antimalarial drug methylene blue (MB) affects the redox behaviour of parasite flavin-dependent disulfide reductases such as glutathione reductase (GR) that control oxidative stress in the malaria parasite. The reduced flavin adenine dinucleotide cofactor FADH(2) initiates reduction to leucomethylene blue (LMB), which is oxidised by oxygen to generate reactive oxygen species (ROS) and MB. MB then acts as a subversive substrate for NADPH normally required to regenerate FADH(2) for enzyme function. The synergism between MB and the peroxidic antimalarial artemisinin derivative artesunate suggests that artemisinins have a complementary mode of action. We find that artemisinins are transformed by LMB generated from MB and ascorbic acid (AA) or N-benzyldihydronicotinamide (BNAH) in situ in aqueous buffer at physiological pH into single electron transfer (SET) rearrangement products or two-electron reduction products, the latter of which dominates with BNAH. Neither AA nor BNAH alone affects the artemisinins. The AA-MB SET reactions are enhanced under aerobic conditions, and the major products obtained here are structurally closely related to one such product already reported to form in an intracellular medium. A ketyl arising via SET with the artemisinin is invoked to explain their formation. Dihydroflavins generated from riboflavin (RF) and FAD by pretreatment with sodium dithionite are rapidly oxidised by artemisinin to the parent flavins. When catalytic amounts of RF, FAD, and other flavins are reduced in situ by excess BNAH or NAD(P)H in the presence of the artemisinins in the aqueous buffer, they are rapidly oxidised to the parent flavins with concomitant formation of two-electron reduction products from the artemisinins; regeneration of the reduced flavin by excess reductant maintains a catalytic cycle until the artemisinin is consumed. In preliminary experiments, we show that NADPH consumption in yeast GR with redox behaviour similar to that of parasite GR is enhanced by artemisinins, especially under aerobic conditions. Recombinant human GR is not affected. Artemisinins thus may act as antimalarial drugs by perturbing the redox balance within the malaria parasite, both by oxidising FADH(2) in parasite GR or other parasite flavoenzymes, and by initiating autoxidation of the dihydroflavin by oxygen with generation of ROS. Reduction of the artemisinin is proposed to occur via hydride transfer from LMB or the dihydroflavin to O1 of the peroxide. This hitherto unrecorded reactivity profile conforms with known structure-activity relationships of artemisinins, is consistent with their known ability to generate ROS in vivo, and explains the synergism between artemisinins and redox-active antimalarial drugs such as MB and doxorubicin. As the artemisinins appear to be relatively inert towards human GR, a putative model that accounts for the selective potency of artemisinins towards the malaria parasite also becomes apparent. Decisively, ferrous iron or carbon-centered free radicals cannot be involved, and the reactivity described herein reconciles disparate observations that are incompatible with the ferrous iron-carbon radical hypothesis for antimalarial mechanism of action. Finally, the urgent enquiry into the emerging resistance of the malaria parasite to artemisinins may now in one part address the possibilities either of structural changes taking place in parasite flavoenzymes that render the flavin cofactor less accessible to artemisinins or of an enhancement in the ability to use intra-erythrocytic human disulfide reductases required for maintenance of parasite redox balance.
Asunto(s)
Antimaláricos/química , Artemisininas/química , Flavinas/química , Glutatión Reductasa/metabolismo , Azul de Metileno/análogos & derivados , Proteínas Protozoarias/metabolismo , Antimaláricos/farmacología , Artemisininas/farmacología , Cristalografía por Rayos X , Azul de Metileno/química , Azul de Metileno/farmacología , Conformación Molecular , Oxidación-Reducción , Especies Reactivas de Oxígeno/metabolismo , Relación Estructura-ActividadRESUMEN
A family of 5-deazaflavin derivatives has been synthesised using a two-step convergent strategy. The biological activity of these compounds was evaluated in cells, by assessing their ability to stabilize and activate p53. These compounds may act as low molecular weight inhibitors of the E3 activity of HMD2 in tumours that retain wild-type p53. Importantly, we have demonstrated that the nitro group present in all three of the original lead compounds [1-3 (HL198C-E)] is not essential for observation of this biological activity.
Asunto(s)
Células Epiteliales/efectos de los fármacos , Flavinas/síntesis química , Flavinas/farmacología , Proteína p53 Supresora de Tumor/efectos de los fármacos , Apoptosis/efectos de los fármacos , Western Blotting , Ciclo Celular/efectos de los fármacos , Daño del ADN , Relación Dosis-Respuesta a Droga , Doxorrubicina/farmacología , Evaluación Preclínica de Medicamentos , Células Epiteliales/química , Células Epiteliales/metabolismo , Flavinas/química , Citometría de Flujo , Humanos , Estructura Molecular , Peso Molecular , Proteínas Proto-Oncogénicas c-mdm2/efectos de los fármacos , Proteínas Proto-Oncogénicas c-mdm2/fisiología , Sensibilidad y Especificidad , Estereoisomerismo , Relación Estructura-Actividad , Proteína p53 Supresora de Tumor/metabolismoRESUMEN
Chromium(VI) is a recognized toxicant whose effects have been linked to its reduction to lower oxidation states. Although Cr(VI) is reduced by several systems, it is anticipated that its reduction by nitric oxide synthase (NOS) could have significant effects in endothelial and brain cells that express high constitutive levels of the enzyme. This possibility was examined by electron paramagnetic resonance that showed the formation of a stable Cr(V) species from NOS/Cr(VI). The formation of Cr(V) was calcium/calmodulin-independent indicating that Cr(VI) to Cr(V) reduction occurs at the flavin-containing domain of NOS. Accordingly, Cr(VI) reduction by the reductase domain of NOS and the chimera protein cytochrome-P450-reductase+tail-nNOS also generated Cr(V). Activation of tetrahydrobiopterin (BH(4))-free NOS with calcium/calmodulin diminished Cr(V) steady-state levels while increasing superoxide formation. Since SOD restored Cr(V) to control levels, this result was taken as evidence for a reaction between Cr(V) and superoxide. Supplementation of NOS with BH(4) cofactor not only failed to increase Cr(V) yields but generated superoxide and hydroxyl radical. Since the holoenzyme does not generate superoxide, this reaction indicated that Cr(V) mediates the oxidation of BH(4)-bound to the enzyme. In the presence of L-arginine, however, Cr(VI) neither enhances superoxide release nor inhibits NO formation from fully active NOS. This suggests that L-arginine protects BH(4) from Cr(V)-mediated oxidation. While Cr(V) was inactive toward NO, spin trapping experiments with 5-tert-butoxycarbonyl 5-methyl-1-pyrroline N-oxide and oxygen consumption measurements showed that Cr(V) reacts with superoxide by a one-electron-transfer mechanism to generate oxygen and Cr(IV). Thus, reduction of Cr(VI) to Cr(V) by NOS occurs in resting and fully active states. It is likely that the reaction between Cr(V) and superoxide influences the cytotoxic mechanisms of Cr(VI) in cells.
Asunto(s)
Cromatos/química , Cromo/metabolismo , Células Endoteliales/metabolismo , Óxido Nítrico Sintasa/metabolismo , Superóxidos/metabolismo , Animales , Arginina/farmacología , Biopterinas/análogos & derivados , Biopterinas/farmacología , Encéfalo/citología , Encéfalo/metabolismo , Calcio/metabolismo , Calmodulina/metabolismo , Sistema Enzimático del Citocromo P-450/metabolismo , Flavinas/química , Radical Hidroxilo/metabolismo , Oxidación-Reducción , Oxígeno/metabolismo , Factores de TiempoRESUMEN
The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). The reduction by NADPH of the two domains was studied by rapid-mixing, stopped-flow spectroscopy. For the FAD/NADPH domain, the results indicate that FAD is reduced by NADPH to generate the two-electron-reduced form (FADH(2)) and the reoxidation of the reduced FAD proceeds via a neutral (blue) semiquinone with molecular oxygen or ferricyanide, indicating that the reduced FAD is oxidized in two successive one-electron steps. The neutral (blue) semiquinone form, as an intermediate in the air-oxidation, was unstable in the presence of O(2). The purified FAD/NADPH domain prepared under our experimental conditions was activated by NADP(+) but not NAD(+). These results indicate that this domain exists in two states; an active state and a resting state, and the enzyme in the resting state can be activated by NADP(+). For the FAD/FMN domain, the reduction of the FAD-FMN pair of the oxidized enzyme with NADPH proceeded by both one-electron equivalent and two-electron equivalent mechanisms. The formation of semiquinones from the FAD-FMN pair was greatly increased in the presence of Ca(2+)/CaM. The air-stable semiquinone form, FAD-FMNH(.), was further rapidly reduced by NADPH with an increase at 520 nm, which is a characteristic peak of the FAD semiquinone. Results presented here indicate that intramolecular one-electron transfer from FAD to FMN is activated by the binding of Ca(2+)/CaM.
Asunto(s)
Calmodulina/química , Flavinas/química , Neuronas/enzimología , Óxido Nítrico Sintasa/química , Sitios de Unión , Calcio/metabolismo , Calmodulina/metabolismo , ADN Complementario/metabolismo , Transporte de Electrón , Electrones , Electroforesis en Gel de Poliacrilamida , Ferricianuros/química , Flavina-Adenina Dinucleótido/química , Flavoproteínas/metabolismo , Humanos , Cinética , Modelos Químicos , NADP/química , NADPH-Ferrihemoproteína Reductasa/metabolismo , Óxido Nítrico Sintasa/metabolismo , Oxígeno/química , Oxígeno/metabolismo , Unión Proteica , Estructura Terciaria de Proteína , Quinonas/metabolismo , Proteínas Recombinantes/química , Espectrofotometría , Factores de TiempoRESUMEN
Separation of the extract of the underground tubers of Cyperus conglomeratus Rottb. (family Cyperaceae) afforded, in addition to known compounds, two novel flavans, which were identified, by one and two dimensional NMR, MS and IR spectra, as 5-hydroxy-7,3',5'-trimethoxyflavan and 5,7-dihydroxy-3',5'-dimethoxy-6-prenylflavan.
Asunto(s)
Flavinas/química , Flavonoides/química , Plantas Medicinales/química , Flavinas/aislamiento & purificación , Espectroscopía de Resonancia Magnética , Espectrometría de Masas , Raíces de Plantas/química , Espectrofotometría InfrarrojaRESUMEN
Camelliatannin D (1), a new complex tannin which inhibits Ca release from mouse calvaria, was isolated from the leaves and fruits of Camellia japonica L. (Theaceae). This tannin is the first example of complex tannin composed of a dimeric hydrolyzable tannin and a flavan-3-ol.