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PubMed2004

Syntheses of acetylated steroid glycosides and selective cleavage of O-acetyl groups in sugar moiety.

Acetylated 3beta-O-beta-glycosyl steroid derivatives were synthesized by the reaction of a new polyhydroxysteroid 3beta,5alpha,6beta-trihydroxypregn-16-en-20-one (2) with the peracetylated 1-bromo derivatives of d-glucose and d-galactose, respectively. Subsequent protection by excess acetic anhydride in pyridine selectively gave the 6beta-O-acetylated steroid glycosides. Deprotection of the acetylated steroid glycosides separately with moderate catalysis dibutyltin oxide in methanol selectively removed all acetyl groups of sugar moiety, whereas the acetyl group of the steroid part was retained. The structures of the steroid glycosides were confirmed by mass spectrometry, NMR and IR. The complete protocol was shown to be non-destructive at all stages to the sugar moieties and the steroid nucleus. These regioselective reactions open a route to the synthesis of a series of closely related isomers of 2 and other widespread polyhydroxysteroids and steroid glycosides in marine organisms and some terrestrial species.

Acetylation↗

PubMed2005

Steroidal glycosides from Cynanchum forrestii Schlechter.

Nine new steroidal glycosides, cynaforrosides B, C, D, E, and F, based on a 13, 14: 14, 15-disecopregnane-type skeleton, cynaforrosides G, H, and I with a new aglycone named cynaforrogenin A, and cynaforroside J together with three known C21 steroidal glycosides cynatratoside A, hancoside and komaroside C were isolated from the ethanol extract of the roots of Cynanchum forrestii Schlechter. The structures of new compounds were determined on the basis of spectral and chemical evidence. Steroidal glycosides with three kinds of skeletons were isolated from this plant simultaneously. The sugar units of cynaforrosides B-I contained two moieties of glucoses and especially cynaforrosides E-I contained two glucoses with the mode of 1-->6 linkage, which were rare among steroidal glycosides of the genus Cynanchum.

Apocynaceae↗

PubMed1996

Enhanced sensitivity of the failing human myocardium to cardiac glycosides and Na(+)-channel activators.

Cardiac glycosides and Na+ -channel activators increase intracellular Na+ and thereby enhance the transport rate of the sarcolemmal Na+/Ca2+ exchanger. We tested the hypothesis of whether increased expression of the Na+/Ca2+ exchanger in failing human myocardium is accompanied by enhanced sensitivity of the failing human myocardium toward cardiac glycosides and Na+ -channel activators. We studied the positive inotropic effects of the new Na+ -channel activator BDF and the cardiac glycoside ouabain in human failing (New York Heart Association [NYHA] functional class IV, heart transplants for dilated cardiomyopathy, n = 11) and nonfailing (donor hearts, n = 5) myocardium on electrically driven left ventricular papillary muscle strips (1 Hz, 37 degrees C). The effectiveness of ouabain and BDF to increase force of contraction was similar in human nonfailing and failing myocardium. BDF was more potent to increase force of contraction in failing than in nonfailing tissue (p < 0.05). The time until maximal inotropic effect developed after ouabain was significantly shorter in NYHA IV (mean 150 +/- 16 min) than in nonfailing myocardium (mean 240 +/- 20 min). These results suggest that human failing myocardium exerts and enhanced sensitivity to cardiac glycosides and Na+ -channel activators, possibly because of enhanced expression of the Na+/Ca2+ exchanger or because of an altered intracellular Na+ -homeostasis.

Adolescent↗

PubMed2000

The application of the intermediate 2-methyl-glyco-[2,1-d]-2-oxazolines for glycoside synthesis.

The synthesis of 2-acylamino-2-deoxysugars 1,2-trans-glycosides is described via the oxazolinium salt generated from an O,N-acetylated 1,2-cis-glycosyl halide of 2-amino-2-deoxysugar under the conditions of halide-anion catalysis. This salt was then interacted with alcohol to form the corresponding 1,2-trans-glycoside. A method for removing the generated hydrogen chloride is described. The conditions of this synthesis allow glycosides with acid-labile functional groups to be obtained. Suppression of the anomerisation of 1,2-trans-glycosides was achieved by the introduction of N,N'-dicyclohexyl urea into the reaction medium.

Alcohols↗

PubMed2000

Regioselective synthesis of p-nitrophenyl glycosides of beta-D-galactopyranosyl-disaccharides by transglycosylation with beta-D-galactosidases.

The beta-D-galactosidase from porcine liver induced regiospecific transglycosylation of beta-D-galactose from beta-D-Gal-OC6H4NO2-o to OH-6 of, respectively, p-nitrophenyl glycoside acceptors of Gal, GlcNAc and GalNAc to afford beta-Gal-(1-->6)-alpha-Gal-OC6H4NO2-p, beta-Gal-(1--> 6)-beta-Gal-OC6H4NO2-p, beta-Gal-(1-->6)-alpha-GalNAc-OC6H4NO2-p, beta-Gal-(1-->6)-beta-GalNAc-OC6H4NO2-p, beta-Gal-(1-->6)-alpha-GlcNAc-OC6H4NO2-p, and beta-Gal-(1-->6)-beta-GlcNAc-OC6H4NO2-p. The enzyme showed much higher transglycosylation activity for the alpha-glycoside acceptors than the corresponding beta-glycoside acceptors. The regioselectivity of the beta-D-galactosidase from Bacillus circulans ATCC 31382 greatly depended on the nature of the acceptor. When alpha-D-GalNAc-OC6H4NO2-p and alpha-D-GlcNAc-OC6H4NO2-p were used as acceptors, the enzyme showed high potency for regioselective synthesis of beta-Gal-(1-->3)-alpha-GalNAc-OC6H4NO2-p and beta-Gal-(1-->3)-alpha-GlcNAc-OC6H4NO2-p in high respective yields of 75.9 and 79.3% based on the acceptors added. However, replacement of beta-D-Gal-OC6H4NO2-p by beta-D-GalNAc-OC6H4NO2-p did change the direction of galactosylation. The enzyme formed regioselectively beta-Gal-(1-->6)-beta-Gal-OC6H4NO2-p with (beta-Gal-1-->(6-beta-Gal-1-->)n6-beta-Gal-OC6H4NO2-p, n = 1-4). No beta-(1-->3)-linked product was detected during the reaction. Use of the two readily available beta-D-galactosidases facilitates the preparation of (1-->3)- and (1-->6)-linked disaccharide glycosides of beta-D-Gal-GalNAc and beta-D-Gal-GlcNAc.

Animals↗

PubMed1997

Influence of extracellular K+ concentration on the time-course of Na+/K+-ATPase inhibition by cardiac glycosides with fast and low binding kinetics.

The magnitude of the K+ antagonism of cardiac glycoside binding to Na+/K+-ATPase prepared from porcine heart, was estimated from the enzyme activities determined in the presence of different concentrations of K+ ([K+]), ouabain, and alpha-methyl-digitoxigenin-glucoside, the latter showing a 30 fold greater dissociation rate than ouabain. An increase of [K+] (3-20 mmol/l) prolonged the half-lives of Na+/K+-ATPase inhibition and caused a rightward shift of the cardiac glycoside's dose-response curves by the same factor, almost maximal (4 fold) at 14 mmol/l K+. These data could be verified from the cardiac glycoside-elevated intravesicular Na+ concentrations of rat brain vesicles. These concentrations declined rapidly in brain vesicles treated with alpha-methyl-digitoxigenin-glucoside but not with ouabain after K+ was increased from 3.5 to 14 mM. The results suggest that the magnitude of the K+ antagonism under physiological conditions is only limited by the lifespan of the cardiac glycoside-binding E2P enzyme conformation reduced by K+.

Animals↗

PubMed1981

High-performance liquid chromatography of cardiac glycosides.

Highly efficient, short columns have been prepared for the separation of mixtures of cardiac glycosides at relatively small pressure drops. The selectivities of silica adsorbents with different chemically modified surface layers for cardiac glycosides were determined. The influence of the structure of cardiac glycoside molecules on their retention characteristics in liquid chromatography was investigated. The relative number of hydrophobic and hydrophilic groups in the glycoside molecules as well as the configurations are very important for the separation.

Animals↗

PubMed1976

Rapid and sensitive high-resolution procedure for digitalis glycoside analysis by derivatization liquid chromatography.

The separation and quantitative determination of digitalis glycosides by high performance liquid chromatography following derivatization with 4-nitrobenzoylchloride (4-NBC1) is described. The compounds of primary interest were the digitalis glycosides and aglycones of the pharmaceutically important A, B and C series, The derivatization step results in higher extinction values at a more favourable wavelength (260 nm), which permits the use of low-cost ultraviolet detectors. Detection limits are below 20 ng/ml for all of the glycosides tested. The chromatographic properties are also improved by reducing the polarity without a decrease in selectivity. The use of low-polarity and low-viscosity solvent systems on silica gel adsorbents permits rapid isocratic separations of complex mixtures as they usually occur in pharmaceutical products and extracts. The quantitative potential of this method was demonstrated by analyzing ampoule solutions containing desacetyl lanatoside C as the active compound. The active substance, by-products and degradation products were determined down to 0.1% of the total glycoside concentration in one ampoule.

Chromatography, High Pressure Liquid↗

PubMed1982

Correlation between the retention of cardiac glycosides in reversed-phase high-performance liquid chromatography with a diphenylsilyl stationary phase, the structure of their molecules and their biological activity.

The separation of mixtures of cardiac glycosides by reversed-phase high-performance liquid chromatography on silica gel with chemically grafted diphenylsilyl groups using water-ethanol as the eluent was carried out. It is shown that the configuration and conformation of the glycoside molecules, and the hydrophilic properties of their aglycones and glycones, influence the separation. The hydrophilic properties of the aglycones are more important than those of the glycones. The glycosides with more hydrophilic aglycones have higher biological activity. This is probably related to the easier transport of these glycosides to the receptor.

Animals↗

PubMed1988

Identification of partially methylated methyl glycosides by gas chromatography-mass spectrometry of trimethylsilyl derivatives. Application to mycobacterial glycolipid antigen analysis.

Partially methylated glycosides play an important role in the stereospecificity of glycolipid antigen-antibody binding reactions. A method for the structural determination of partially methylated methyl glycosides is described. The proposed method, which is an alternative to that using alditol acetates, consists in the analysis of trimethylsilyl glycoside derivatives by gas chromatography-mass spectrometry in the electron impact (EI) mode. Seven partially methylated methyl rhamnopyranosides were synthesized, then purified by high-performance liquid chromatography. After trimethylsilylation, their EI mass spectra showed characteristic fragmentation patterns allowing the determination of the position and the number of methoxy groups in the sugar ring. This method was successfully applied to the structural elucidation of partially methylated sugars contained by a quantitatively minor phenolic glycolipid antigen isolated from Mycobacterium kansasii. Moreover, the carbons involved in the glycosidic linkages of the glycolipid tetrasaccharide moiety were also identified by this method after permethylation, methanolysis and trimethylsilylation.

Antigens, Bacterial↗

PubMed1999

Purification of cytosolic beta-glucosidase from pig liver and its reactivity towards flavonoid glycosides.

Flavonoid glycosides are common dietary components which may have health-promoting activities. The metabolism of these compounds is thought to influence their bioactivity and uptake from the small intestine. It has been suggested that the enzyme cytosolic beta-glucosidase could deglycosylate certain flavonoid glycosides. To test this hypothesis, the enzyme was purified to homogeneity from pig liver for the first time. It was found to have a molecular weight (55 kDa) and specific activity (with p-nitrophenol glucoside) consistent with other mammalian cytosolic beta-glucosidases. The pure enzyme was indeed found to deglycosylate various flavonoid glycosides. Genistein 7-glucoside, daidzein 7-glucoside, apigenin 7-glucoside and naringenin 7-glucoside all acted as substrates, but we were unable to detect activity with naringenin 7-rhamnoglucoside. Quercetin 4'-glucoside was a substrate, but neither quercetin 3, 4'-diglucoside, quercetin 3-glucoside nor quercetin 3-rhamnoglucoside were deglycosylated. Estimates of K(m) ranged from 25 to 90 microM while those for V(max) were about 10% of that found with the standard artificial substrate p-nitrophenol glucoside. The non-substrate quercetin 3-glucoside was found to partially inhibit deglycosylation of quercetin 4'-glucoside, but it had no effect upon activity with p-nitrophenol glucoside. This study confirms that mammalian cytosolic beta-glucosidase can deglycosylate some, but not all, common dietary flavonoid glycosides. This enzyme may, therefore, be important in the metabolism of these compounds.

Animals↗

PubMed1999

Degradation of cyanogenic glycosides by Lactobacillus plantarum strains from spontaneous cassava fermentation and other microorganisms.

Strains of Lactobacillus plantarum, Leuconostoc mesenteroides, Candida tropicalis and Penicillium sclerotiorum were screened for 19 enzymatic activities using the commercial kit API zym (Bio Mérieux). This activity was compared to the ability of degrading the toxic cyanogenic glycosides amygdalin, linamarin, and linseed cyanogens (a mixture of linustatin and neolinustatin). Good correlation between the beta-glucosidase activity found in the API zym screening and the ability to degrade the cyanogenic glycosides was found for the first three species mentioned. P. sclerotiorum strains exhibited very high activity in the API zym test (substrate: 6-Br-2-naphthyl-beta-D-glucopyranoside), but proved unable to degrade any of the cyanogenic substrates. Among the seven strains of L. plantarum tested, a great variation was seen in the beta-glucosidase activity as well as in the ability to degrade the cyanogens. This was also the case for the strains of C. tropicalis. However, all the glucosidase positive strains of these species were also able to degrade all of the cyanogens tested and at approximately the same rate. A co-culture of the most active strain of L. plantarum and C. tropicalis seemed to degrade linamarin faster than the mono cultures. L. plantarum LPI (originally isolated from fermented cassava) was investigated in further detail. The hydrolytic activity of this strain was intracellular or cell bound, and beta-bis-glycosides such as amygdalin were hydrolysed by a two-stage sequential mechanism as follows: (1) amygdalin to prunasin and (2) prunasin to cyanohydrin. Finally, inoculation of extracted linseed meal (containing linustatin and neolinustatin) with L. plantarum LPI resulted in hydrolysis of the glycosides.

Amygdalin↗

PubMed1996

Hexose keto-C-glycoside conjugates: design, synthesis, cytotoxicity, and evaluation of their affinity for the glucose transporter Glut-1.

The design, synthesis, cytotoxicity, and biological evaluation of carbohydrate/C-glycoside conjugates are described. The design concept is predicted on the idea that physiological barriers like the blood brain barrier could be crossed selectively by using glucose or glucose derivative/drug conjugates. The study demonstrates that, (1) carbohydrates and C-glycosides can be bonded at nonanomeric positions by the reaction of carbohydrate triflates with C-glycoside alkoxydes in the presence of DMPU; (2) there is a structure-activity relationship between the cytotoxicity of the conjugate and the nature of the carbohydrate residue; and (3) peracetylated hexose keto-C-glycoside conjugates are the most cytotoxic keto-C-glycosides.

Erythrocytes↗

PubMed1999

Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase.

BACKGROUND: The enzymatic hydrolysis of glycosides involves the formation and subsequent breakdown of a covalent glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states. The covalent intermediate may be trapped on-enzyme using 2-fluoro-substituted glycosides, which provide details of the intermediate conformation and noncovalent interactions between enzyme and oligosaccharide. Xylanases are important in industrial applications - in the pulp and paper industry, pretreating wood with xylanases decreases the amount of chlorine-containing chemicals used. Xylanases are structurally similar to cellulases but differ in their specificity for xylose-based, versus glucose-based, substrates. RESULTS: The structure of the family 11 xylanase, Xyl11, from Bacillus agaradhaerens has been solved using X-ray crystallography in both native and xylobiosyl-enzyme intermediate forms at 1.78 A and 2.0 A resolution, respectively. The covalent glycosyl-enzyme intermediate has been trapped using a 2-fluoro-2-deoxy substrate with a good leaving group. Unlike covalent intermediate structures for glycoside hydrolases from other families, the covalent glycosyl-enzyme intermediate in family 11 adopts an unusual 2,5B conformation. CONCLUSIONS: The 2,5B conformation found for the alpha-linked xylobiosyl-enzyme intermediate of Xyl11, unlike the 4C1 chair conformation observed for other systems, is consistent with the stereochemical constraints required of the oxocarbenium-ion-like transition state. Comparison of the Xyl11 covalent glycosyl-enzyme intermediate with the equivalent structure for the related family 12 endoglucanase, CelB, from Streptomyces lividans reveals the likely determinants for substrate specificity in this clan of glycoside hydrolases.

Bacillus↗

PubMed2006

Stereoisomeric separation of flavanones and flavanone-7-O-glycosides by capillary electrophoresis and determination of interconversion barriers.

The stereoisomeric separation of several flavanones and flavanone-7-O-glycosides has been achieved with capillary electrophoresis by adding native cyclodextrins or cyclodextrin derivatives to the background electrolyte. As an alternative method, micellar electrokinetic chromatography with sodium cholate as a chiral surfactant has been used for the epimeric separation of two flavanone-7-O-glycosides. The effect of buffer systems containing mixtures of cyclodextrin with either sodium dodecyl sulfate or sodium cholate upon the chiral recognition of flavanones and flavanone-7-O-glycosides as well as the variation of the background electrolyte (concentration of buffer and surfactant, pH value, organic modifier), and its influence on the resolution factor Rs was investigated. Temperature- and pH-dependent enantiomerization or epimerization barriers of several flavanones (naringenin, homoeriodictyol) and flavanone-7-O-glycosides (naringin, neohesperidin, prunin, narirutin) in basic media (pH values of 9-11) have been observed. Interconversion profiles featuring characteristic plateau formation of the elution pattern were observed at high pH and evaluated with the simulation software ChromWin to determine rate constants k(T) and Eyring activation parameters, DeltaG#(T), DeltaH#, and DeltaS#.

Cyclodextrins↗

PubMed1987

Transition-state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator.

The mechanism of acid and enzymatic hydrolysis of the N-glycosidic bond of AMP has been investigated by fitting experimentally observed kinetic isotope effects [Parkin, D. W., & Schramm, V. L. (1987) Biochemistry (preceding paper in this issue)] to calculated kinetic isotope effects for proposed transition-state structures. The sensitivity of the transition-state calculations was tested by "arying the transition-state structure and comparing changes in the calculated kinetic isotope effects with the experimental values of the isotope effect measurements. The kinetic isotope effects for the acid-catalyzed hydrolysis of AMP are best explained by a transition state with considerable oxycarbonium character in the ribose ring, significant bonding remaining to the departing adenine ring, participation of a water nucleophile, and protonation of the adenine ring. A transition-state structure without preassociation of the water nucleophile cannot be eliminated by the data. Enzymatic hydrolysis of the N-glycosidic bond of AMP by AMP nucleosidase from Azotobacter vinelandii was analyzed in the absence and presence of MgATP, the allosteric activator that increases Vmax approximately 200-fold. The transition states for enzyme-catalyzed hydrolysis that best explain the kinetic isotope effects involve early SN1 transition states with significant bond order in the glycosidic bond and protonation of the adenine base. The enzyme enforces participation of an enzyme-bound water molecule, which has weak bonding to C1' in the transition state. Activation of AMP nucleosidase by MgATP causes the bond order of the glycosidic bond in the transition state to increase significantly. Hyperconjugation in the ribosyl group is altered by enzymatic stabilization of the oxycarbonium ion. This change is consistent with the interaction of an amino acid on the enzyme. Together, these changes stabilize a carboxonium-like transition-state complex that occurs earlier in the reaction pathway than in the absence of allosteric activator. In addition to the allosteric changes that alter transition-state structure, the presence of other inductive effects that are unobserved by kinetic isotope measurements is also likely to increase the catalytic rate.

Adenosine Monophosphate↗

PubMed2005

Interactions between cardiac glycosides and sodium/potassium-ATPase: three-dimensional structure-activity relationship models for ligand binding to the E2-Pi form of the enzyme versus activity inhibition.

Sodium/potassium-ATPase (Na/K-ATPase) is a transmembrane enzyme that utilizes energy gained from ATP hydrolysis to transport sodium and potassium ions across cell membranes in opposite directions against their chemical and electrical gradients. Its transport activity is effectively inhibited by cardiac glycosides, which bind to the extracellular side of the enzyme and are of significant therapeutic value in the treatment of congestive heart failure. To determine the extent to which high-affinity binding of cardiac glycosides correlates with their potency in inhibiting pump activity, we determined experimentally both the binding affinities and inhibitory potencies of a series of 37 cardiac glycosides using radioligand binding and ATPase activity assays. The observed variations in key structural elements of these compounds correlating with binding and inhibition were analyzed by comparative molecular similarity index analysis (CoMSIA), which allowed a molecular level characterization and comparison of drug-Na/K-ATPase interactions that are important for ligand binding and activity inhibition. In agreement with our earlier comparative molecular field analysis studies [Farr, C. D., et al. (2002) Biochemistry 41, 1137-1148], the CoMSIA models predicted favorable inhibitor interactions primarily at the alpha-sugar and lactone ring moieties of the cardiac glycosides. Unfavorable interactions were located about the gamma-sugar group and at several positions about the steroid ring system. Whereas for most compounds a correlation between binding affinity and inhibitory potency was found, some notable exceptions were identified. Substitution of the five-membered lactone of cardenolides with the six-membered lactone of bufadienolides caused binding affinity to decline but inhibitory potency to increase. Furthermore, while the removal of ouabain's rhamnose moiety had little effect on inhibitory potency, it caused a dramatic decline in ligand binding affinity.

Algorithms↗

PubMed2002

Variation in the flavonol glycoside composition of almond seedcoats as determined by maldi-tof mass spectrometry.

Seedcoats of 16 almond varieties were screened for flavonol glycosides by using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Flavonol glycosides were extracted by a simple methanolic extraction followed by a quick cleanup procedure with a Sep-Pak C(18) cartridge. Each of the 16 seedcoat samples exhibited a unique composition. Four flavonol glycosides, isorhamnetin rutinoside, isorhamnetin glucoside, kaempferol rutinoside, and kaempferol glucoside, were detected and quantified with use of rutin as an internal standard. Individual peak ratios were very consistent across triplicate analyses of all samples; the average standard deviation was 9%. In all almond varieties, isorhamnetin rutinoside was the most abundant flavonol glycoside, and the total content ranged from 75 to 250 microg/g.

Flavonoids↗