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The synthesis and biological activity of oleylN-acetyl-alpha- and beta-d-glucosaminides (1 and 2, respectively) and their thioglycosyl analogues (3 and 4, respectively) are reported. The compounds exhibited antimitotic activity on rat glioma (C6) and human lung carcinoma (A549) cell cultures in the micromolar range. Analysis of cell extracts using ultra performance liquid chromatography-mass spectrometry showed that the synthetic glycosides produce alterations in glycosphingolipid metabolism, with variable effect on the level of glucosylceramide depending on the configuration of the antimitotic used. In vivo experiments in nude mice bearing an implanted C6 glioma showed that the alpha-thioglycoside 3 reduced tumor volume, while the O-glycosyl derivative was inactive, highlighting the importance of using enzyme resistant glycosides.

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The present invention relates to a method for preparing a sialic acid derivative, wherein the method is characterized in that a process of using N-acetyl-D-glucosamine to prepare CMP-M-acetylneuraminic acid and a process of combining sialic acid with galactose or a galactose derivative to prepare a sialic acid (neuraminic acid) derivative are performed together in one reactor. According to the present invention, a high-priced cytidine 5′-monophosphoric acid (CMP) can be recycled in a reaction container, thereby reducing the amount of cytidine 5′-monophosphoric acid (CMP) introduced into the reaction, producing a sialic acid derivative using low-priced N-acetyl-D-glucosamine and pyruvic acid as substrates, and producing the sialic acid derivative at higher efficiency.

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An efficient heterologous expression system for overproduction of the enzyme alpha-1,6-Fucosyltransferase (alpha-1,6-FucT) from Rhizobium sp. has been developed. The gene codifying for the alpha-1,6-FucT was amplified by PCR using specific primers. After purification, the gene was cloned in the plasmid pKK223-3. The resulting plasmid, pKK1,6FucT, was transformed into the E. coli strain XL1-Blue MRF?. The protein was expressed both as inclusion bodies and in soluble form. Changing the induction time a five-fold increase of enzyme expressed in soluble form was obtained. In this way five units of enzyme alpha-1,6-FucT can be obtained per liter of culture. A crude preparation of the recombinant enzyme was used for the synthesis of the branched trisaccharide alpha-D-GlcNAc-(1 ? 4)-[alpha-L-Fuc-(1 ? 6)]-D-GlcNAc (3), from chitobiose (2) and GDP-Fucose (1). After purification, the trisaccharide 3 was obtained in a 84% overall yield. In order to elucidate the structural requirements for the acceptors, the specificity of the enzyme was studied towards mono-, di- and trisaccharides, which are structurally related to chitobiose. The enzyme uses, among others, the disaccharide N-acetyl lactosamine as a good substrate; the monosaccharide GlcNAc is a weak acceptor. Finally, several racemic polyhydroxylated indolizidines have been tested as potential inhibitors of the enzyme. Indolizidine 21 was the best inhibitor with an IC50 of 4.5 × 10-5M. Interestingly, this compound turned out to be the best mimic for the structural features of the fucose moiety in the presumed transition state. WILEY-VCH Verlag GmbH, 2001.

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Trypanosoma cruzi, the agent of Chagas disease, expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The enzyme is shed to the medium and may affect the immune system of the host. We have previously described that lactose derivatives effectively inhibited the transfer of sialic acid to N-acetyllactosamine. Lactitol also prevented the apoptosis caused by the TcTS, although it is rapidly eliminated from the circulatory system. In this paper we report covalent conjugation of polyethylene glycol (PEG) with lactose, lactobionolactone and benzyl beta-D-galactopyranosyl-(1?6)-2-amino-2- deoxy-alpha-D-glucopyranoside (1) with the hope to improve the bioavailability, though retaining their inhibitory properties. Different conjugation methods have been used and the behavior of the PEGylated products in the TcTS reaction was studied.

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The transformation of simple hydrocarbons into more complex and valuable products has revolutionised modern synthetic chemistry. This type of reactivity has quickly become one of the cornerstones of modern catalysis . 14215-68-0, Name is N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide, molecular formula is C8H15NO6. In a Article,once mentioned of 14215-68-0, Related Products of 14215-68-0

The monosaccharide N-acetyl-d-glucosamine (GlcNAc) is an abundant building block in naturally occurring oligosaccharides, but its incorporation by chemical glycosylation is challenging since direct reactions are low yielding. This issue, generally agreed upon to be caused by an intermediate 1,2-oxazoline, is often bypassed by introducing extra synthetic steps to avoid the presence of the NHAc functional group during glycosylation. The present paper describes new fundamental mechanistic insights into the inherent challenges of performing direct glycosylation with GlcNAc. These results show that controlling the balance of oxazoline formation and glycosylation is key to achieving acceptable chemical yields. By applying this line of reasoning to direct glycosylation with a traditional thioglycoside donor of GlcNAc, which otherwise affords poor glycosylation yields, one may obtain useful glycosylation results.

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Disaccharide and trisaccharide mimics containing the amino(methoxy) interglycosidic linkage were obtained by chemoselective condensation of unprotected aldoses in an aqueous environment both in solution and in solid phase.

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The present invention provides methods for preventing, treating, managing and/or ameliorating a condition associated with inflammation (e.g., an inflammatory disorder) or a symptom thereof, the methods comprising administering to a subject in need thereof an effective amount of a theaflavin composition and an effective amount of one or more therapies other than such a theaflavin composition. In particular, the present invention provides methods for preventing, treating, managing and/or ameliorating a condition associated with inflammation (e.g., an inflammatory disorder) or a symptom thereof, the methods comprising administering to a subject in need thereof an effective amount of a theaflavin composition, an effective amount of a glucosamine composition, and optionally one or more other therapies.

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One of the major reasons for studying chemical kinetics is to use measurements of the macroscopic properties of a system, such as the rate of change in the concentration of reactants or products with time. 14215-68-0, Name is N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide, molecular formula is C8H15NO6. In a Article,once mentioned of 14215-68-0, Recommanded Product: N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide

Sugar dihydroozaxole monomers with two free hydroxyl groups undergo acid-catalyzed polymerization to hyperbranched aminopolysaccharides [Eq. (a)]. Their molecular weights were determined by the light-scattering method to be between 2.3 x 105 and 7.6 x 105. The degree of branching determined by 1H NMR spectroscopy after reaction with [iPr2Si(Cl)]2O is close to the ideal value. Ts = MeC6H4SO2, CSA = 10-camphorsulfonic acid.

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The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described. This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades. It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).

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Background: Lectins are highly important biomolecules to study several biological processes. A novel alpha-D-glucose/mannose specific lectin was isolated from the seeds of litchi fruits (Litchi chinensis) and its various biophysical and biochemical properties were studied. Methods: Purification was done by successive Sephadex G 100 and Con A-Sepharose 4B affinity chromatography. SDS-PAGE, Surface Plasmon Resonance (SPR), steady state absorbance, fluorescence, time-correlated single-photon counting, circular dichroism and antibiofilm activity by measuring total protein estimation and azocasein degradation assay have been performed. Results: The purified lectin is a homodimer of molecular mass ~ 54 kDa. The amount of lectin required for hemagglutination of normal human O erythrocytes was 6.72 mug/ml. Among the saccharides tested, Man-alpha-(1,6)-Man was found to be the most potent inhibitor (0.01 mM) determined by hemagglutination inhibition assay. Steady state and time resolved fluorescence measurements revealed that litchi lectin formed ground state complex with maltose (Ka=4.9 (±0.2)×104 M-1), which indicated static quenching (Stern-Volmer (SV) constant Ksv=4.6 (±0.2)×104 M-1). CD measurements demonstrated that litchi lectin showed no overall conformational change during the binding process with maltose. The lectin showed antibiofilm activity against Pseudomonus aeruginosa. Conclusions: A novel homodimeric lectin has been purified from the seeds of litchi fruits (Litchi chinensis) having specificity for alpha- d-glucose/mannose. The thermodynamics and conformational aspects of its interaction with maltose have been studied in detail. The antibiofilm activity of this lectin towards Pseudomonus aeruginosa has been explored. General significance: The newly identified litchi lectin is highly specific for alpha- d-glucose/mannose with an important antibiofilm activity towards Pseudomonus aeruginosa.

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