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A simple synthetic route has been devised for the production of coating agents that can give multivalent displays of saccharides on the surface of magnetite nanoparticles and phospholipid vesicles. A versatile and potentially high-throughput condensation reaction allowed the rapid synthesis of a variety of glycosylhydrazide conjugates with lipid, resorcinol or catechol termini, each in good yield and high anomeric purity. The hydrolytic stability of these adducts was assessed in D2O at different pD values using 1H-NMR spectroscopy, whilst quartz crystal microbalance with dissipation monitoring (QCM-D) confirmed that the saccharide functionality on bilayers and on nanoparticles was still available to lectins. These multivalent saccharide displays promoted nanoparticle interactions with cells, for example N-acetylglucosamine-coated nanoparticles interacted much more effectively with 3T3 fibroblasts than uncoated nanoparticles with these cells. Despite potential sensitivity to oxidation, catechol coatings on magnetite nanoparticles were found to be more stable and generate better nanoparticle interactions with fibroblasts than resorcinol coatings.

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The cells of the human monocytic leukemia cell line THP-1 differentiated into macrophages bound to human erythrocytes oxidized with adenosine 5′- diphosphate (ADP)-Fe3+ chelate (ADP/Fe3+) in the absence of serum. The binding was prevented when the cells were treated with ADP/Fe3+ in the presence of antioxidants, indicating that oxidation of the cells is responsible for the increased susceptibility to the THP-1 cell binding. Galactose, fucose, mannose and mannan partially inhibited the binding. Glycoproteins containing poly-N-acetyllactosaminyl saccharide chains such as band 3 glycoprotein isolated from human erythrocyte membrane and lactoferrin, and their oligosaccharides, strongly inhibited the binding. On the other hand, glycoproteins with non-poly-N-acetyllactosaminyl saccharide chains such as glycophorin A isolated from the erythrocyte membrane, fetuin and alpha1- acid glycoprotein, little or partially inhibited the binding. The inhibitory activity of band 3 oligosaccharides and lactoferrin oligosaccharides was little affected by treatment with endo-beta-galactosidase, which specifically cleaves poly-N-acetyllactosamine to shorter oligosaccharides. Removal of the nonreducing terminal region of the saccharide chains of band 3 on the erythrocyte surface by treatment of the cells with endo-beta-galactosidase resulted in a decrease in the susceptibility of the cells to the THP-1 cell binding. These results suggest that THP-1 cells which have been differentiated into macrophages bind the oxidized erythrocytes primarily through the recognition of poly-N-acetyllactosaminyl saccharide chains of band 3, and the site of the recognition exists in the nonreducing terminal region of the saccharide chains. Clustering of band 3 molecules is proposed as a possible alteration of oxidized erythrocyte membrane which promotes the interaction of the saccharide receptor on THP-1 cells with the saccharide chains of band 3 on erythrocytes.

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Lectins, also recognized as hemagglutinins, are multivalent proteins, and their desirable quality of fine sugar-binding specificity plays an important role in defense functions in invertebrates. In the present study, a galactose-specific lectin was detected, purified, and characterized from the hemolymph of the grub of rhinoceros beetle, Oryctes rhinoceros. The lectin was purified by affinity column chromatography with acid-treated Sepharose 6B as the matrix. The purified lectin was heat-labile, cation independent, and insensitive to EDTA. It revealed the presence of three distinct polypeptides with molecular weights of 90, 78, and 45 kDa. Thus, the native molecular weight of the purified lectin was calculated to be approximately 213 kDa, as revealed by a single band in native-PAGE. Studies on antibacterial activity and bacterial agglutination assays revealed that the purified lectin possess both these properties against two bacterial species, Bacillus subtilis and B. pumilus, isolated from the native larval habitat of O. rhinoceros.

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Ring-opening glycosylation of a chitobiose oxazoline was exclusively achieved by catalysis of a mutated chitinase that is only active for the glycosylation and not for chitinolysis.

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A new method is described for sequencing linear oligosaccharides on gels using charged, fluorescent conjugates. The reducing ends of various mono-, di-, tri-, and tetra-saccharides were conjugated with monopotassium 7-amino-1,3-naphthalenedisulfonate (a fluorescent and negatively charged compound) by reductive amination using sodium cyanoborohydride. The sugar conjugates were purified by preparative gradient polyacrylamide gel electrophoresis followed by a newly developed technique involving their semi-dry transfer to positively charged nylon membranes and elution with sodium chloride. The structures of a monosaccharide- and trisaccharide-conjugate were established by f.a.b.-m.s. and 2D n.m.r. Seven linear oligosaccharide-fluorescent conjugates were treated sequentially with exoglycosidases and with endoglycosidases. Analysis of the products by gel electrophoresis provided sequence information. These methods may be useful for sequencing oligosaccharides that are chemically or enzymically (endoglycosidase) released from glycoproteins, glycolipids, and proteoglycans. A new method is described for sequencing linear oligosaccharides on gels using charged, fluorescent conjugates. The reducing ends of various mono-, di-, tri-, and tetra-saccharides were conjugated with monopotassium 7-amino-1,3-naphthalenedisulfonate (a fluorescent and negatively charged compound) by reductive amination using sodium cyanoborohydride. The sugar conjugates were purified by preparative gradient polyacrylamide gel electrophoresis followed by a newly developed technique involving their semi-dry transfer to positively charged nylon membranes and elution with sodium chloride. The structures of a monosaccharide- and trisaccharide-conjugate were established by f.a.b.-m.s. and 2D n.m.r. Seven linear oligosaccharide-fluorescent conjugates were treated sequentially with exoglycosidases and with endoglycosidases. Analysis of the products by gel electrophoresis provided sequence information. These methods may be useful for sequencing oligosaccharides that are chemically or enzymically (endoglycosidase) released from glycoproteins, glycolipids, and proteoglycans.

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Chemistry involves the study of all things chemical – chemical processes, chemical compositions and chemical manipulation – in order to better understand the way in which materials are structured, how they change and how they react in certain situations.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, name: N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide

D-Galactosyl disaccharides have been synthesized by utilizing the reversed hydrolysis activity of beta-D-galactosidases from E. coli and from A. oryzae, respectively.In order to shift the equilibrium towards the formation of disaccharide, solutions of monosaccharides were circulated through columns of immobilized beta-D-galactosidase and activated carbon in series.After 24 h, the disaccharides were eluted with aqueous 50 percent ethanol from the column of activated carbon and analyzed by h.p.l.c. and 13C-n.m.r. spectroscopy.In this way, beta-D-galactosyl-D-glucose, beta-D-galactosyl-2-acetamido-2-deoxy-D-glucose, and beta-D-galactosyl-D-fructose were produced in yields of 6.0, 16.0, and 11.3 percent, respectively, when the immobilized beta-D-galactosidase from E. coli was used.The possible mechanism of the synthesis of the disaccharides is discussed.

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A series of sugar derivatives (1-13) were synthesized and evaluated for antibacterial activity against Mycobacterium tuberculosis (MTB), especially multi-drug resistant (MDR) MTB, and the structure-activity relationships of these compounds were studied. The results showed that the compound OCT313 (2-acetamido-2deoxy-beta-d-glucopyranosyl N,N-dimethyldithiocarbamate) (4) exhibited significant in vitro bactericidal activity, and that the dithiocarbamate group at C-1 position of the glucopyranoside ring was requisite for the antibacterial activity.

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The reactant in an enzyme-catalyzed reaction is called a substrate. Enzyme inhibitors cause a decrease in the reaction rate of an enzyme-catalyzed reaction.I hope my blog about 14215-68-0 is helpful to your research., Formula: C8H15NO6

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Chitin treatment using different methods, including ball mill grinding, steam explosion, alkaline treatment, phosphoric acid, and ionic liquid (IL) dissolution/reprecipitation have been systematically investigated. The chitin structures were thoroughly investigated by using a series of analytical techniques, and the reactivity after each treatment was evaluated in dehydration and liquefaction reactions. The parallel studies enable direct comparisons of these methods and help to establish the structure-activity correlations. Ball mill grinding in dry mode was the most effective method, with the crystal size and the hydrogen-bond network being the two crucial factors in enhancing the reactivity. Remarkably, the yield of 3-acetamido-5-acetylfuran (3A5AF) from chitin dehydration increased to the highest amount (28.5%) after ball mill grinding (the previous record yield was 7.5% for untreated chitin).

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Hypochlorous acid and its acid-base counterpart, hypochlorite ions, produced under inflammatory conditions, may produce chloramides of glycosaminoglycans, these being significant components of the extracellular matrix (ECM). This may occur through the binding of myeloperoxidase directly to the glycosaminoglycans. The N-Cl group in the chloramides is a potential selective target for both reducing and oxidizing radicals, leading possibly to more efficient and damaging fragmentation of these biopolymers relative to the parent glycosaminoglycans. In this study, the fast reaction techniques of pulse radiolysis and nanosecond laser flash photolysis have been used to generate both oxidizing and reducing radicals to react with the chloramides of hyaluronan (HACl) and heparin (HepCl). The strong reducing formate radicals and hydrated electrons were found to react rapidly with both HACl and HepCl with rate constants of 1-1.7 x 108 and 0.7-1.2 x 108 M-1 s-1 for formate radicals and 2.2 x 109 and 7.2 x 10 8 M-1 s-1 for hydrated electrons, respectively. The spectral characteristics of the products of these reactions were identical and were consistent with initial attack at the N-Cl groups, followed by elimination of chloride ions to produce nitrogen-centered radicals, which rearrange subsequently and rapidly to produce C-2 radicals on the glucosamine moiety, supporting an earlier EPR study by M.D. Rees et al. (J. Am. Chem. Soc. 125: 13719-13733; 2003). The oxidizing hydroxyl radicals also reacted rapidly with HACl and HepCl with rate constants of 2.2 x 108 and 1.6 x 108 M-1 s-1, with no evidence from these data for any degree of selective attack on the N-Cl group relative to the N-H groups and other sites of attack. The carbonate anion radicals were much slower with HACl and HepCl than hydroxyl radicals (1.0 x 105 and 8.0 x 10 4 M-1 s-1, respectively) but significantly faster than with the parent molecules (3.5 x 104 and 5.0 x 10 4 M-1 s-1, respectively). These findings suggest that these potential in vivo radicals may react in a site-specific manner with the N-Cl group in the glycosaminoglycan chloramides of the ECM, possibly to produce more efficient fragmentation. This is the first study therefore to conclusively demonstrate that reducing radicals react rapidly with glycosaminoglycan chloramides in a site-specific attack at the N-Cl group, probably to produce a 100% efficient biopolymer fragmentation process. Although less reactive, carbonate radicals, which may be produced in vivo via reactions of peroxynitrite with serum levels of carbon dioxide, also appear to react in a highly site-specific manner at the N-Cl group. It is not yet known if such site-specific attacks by this important in vivo species lead to a more efficient fragmentation of the biopolymers than would be expected for attack by the stronger oxidizing species, the hydroxyl radical. It is clear, however, that the N-Cl group formed under inflammatory conditions in the extracellular matrix does present a more likely target for both reactive oxygen species and reducing species than the N-H groups in the parent glycosaminoglycans.

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Ionic liquids (ILs) have emerged as an alternative to conventional organic media due to their high thermal and chemical stability, negligible vapour pressure, non-flammability and easy recycling. In this context, this work assesses the catalytic activity of a beta-galactosidase from Bacillus circulans ATCC 31382 (beta-Gal-3-NTag) in the synthesis of beta-(1?3)-galactosides using different ILs. A noticeably increase in activity, retaining total regioselectivity was found in the synthetic behaviour of B. circulans beta-galactosidase in ILs as co-solvents and using a 1:5 molar ratio of donor (pNP-beta-Gal):acceptor (GlcNAc or GalNac). Yields up to 97% of beta-(1?3) with different ILs were found. These reactions take place without noticeable hydrolytic activity and with total regioselectivity, representing a considerable improvement over the use of aqueous buffer or conventional organic solvents. Furthermore, reaction scaling up and IL recovery and recycling are feasible without losing catalytic action. Molecular modelling studies performed predict a three-dimensional interaction at the active centre between the acceptor and the water-IL mixture, which could explain the results obtained.

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