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Novel phosphinite-nitrogen chiral ligands synthesized from D-glucosamine furnish a high level of enantiomeric excess (up to 96% ee] in palladium-catalysed allylic alkylation.

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Reference:
Tetrahydropyran – Wikipedia,
Tetrahydropyran – an overview | ScienceDirect Topics

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Proteoglycan synthesis is dependent on N-acetyl glucosamine (GlcNAc) produced by the hexosamine biosynthetic pathway or obtained exogenously. Although used therapeutically to relieve symptoms of osteoarthritis, the actions of glucosamine and its analogs on cartilage are poorly understood. The purpose of this study was to determine the effects on chondrocytes of N-acylated-glucosamine analogs bearing alkyl chains of different lengths. Chondrocytes isolated from neonatal rat femoral condyles were cultured in the presence of glucosamine analogs. GlcNAc, N-proprionyl glucosamine (GlcNPro), or N-butyryl glucosamine (GlcNBu) did not alter cell number, lactate dehydrogenase release, or metabolic acid production, consistent with lack of cytotoxicity. Treatment of chondrocyte cultures with GlcNBu for 6 days significantly increased levels of type II collagen and aggrecan mRNA as determined by Northern blot analysis. In contrast, GlcNAc and GlcNPro had no significant effect. A significant increase in type II collagen mRNA was induced by GlcNBu within 3 days. GlcNBu did not alter stability of type II collagen mRNA, suggesting it acts on gene transcription. We have previously shown that tumor necrosis factor-alpha (TNFalpha) decreases levels of type II collagen mRNA. However, chondrocytes pretreated with GlcNBu maintained type II collagen mRNA at control levels in the presence of TNFalpha. These results establish that the N-butyrylated analog of glucosamine but not GlcNAc promotes matrix gene expression by chondrocytes. Thus, GlcNBu has the potential for use as a chondro-protective agent in osteoarthritis.

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Reference:
Tetrahydropyran – Wikipedia,
Tetrahydropyran – an overview | ScienceDirect Topics

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Reducing sugars may be directly converted into the corresponding para-nitrophenyl (pNP) glycosides using 2-chloro-1,3-dimethylimidazolinium chloride (DMC), para-nitrophenol, and a suitable base in aqueous solution. The reaction is stereoselective for sugars with either a hydroxyl or an acetamido group at position 2, yielding the 1,2-trans pNP glycosides. A judicious choice of base allows extension to di-and oligosaccharide substrates, including a complex N-glycan oligosaccharide isolated from natural sources, without the requirement of any protecting group manipulations

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Tetrahydropyran – Wikipedia,
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A series of novel 1,3-difunctionalized glycoconjugates were synthesized using a sequence of regioselective functionalization and stereoselective glycosidation of D-glucose and D-GlcNAc. Regioselective C-3 functionalization of sugar molecules was achieved by chemical functionalization of isopropylidene or oxazoline protected sugar derivatives.The structural diversity at the anomeric carbon was explored by stereoselective chemical glycosidation.The oxazoline protected D-GlcNAc derivative gave either pyranose or furanose derivatives on glycosidation depending on the amount of Lewis acid used.The diversely functionalized glycoconjugates with azide or alkyne groups are potentially useful for the synthesis of multifunctionalized complex glycoconjugates via click reactions.

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Reference:
Tetrahydropyran – Wikipedia,
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A catalyst don’t appear in the overall stoichiometry of the reaction it catalyzes, but it must appear in at least one of the elementary reactions in the mechanism for the catalyzed reaction. 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, Quality Control of: N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide

Legume lectins, despite high sequence homology, express diverse biological activities that vary in potency and efficacy. In studies reported here, the mannose-specific lectin from Cymbosema roseum (CRLI), which binds N-glycoproteins, shows both pro-inflammatory effects when administered by local injection and anti-inflammatory effects when by systemic injection. Protein sequencing was obtained by Tandem Mass Spectrometry and the crystal structure was solved by X-ray crystallography using a Synchrotron radiation source. Molecular replacement and refinement were performed using CCP4 and the carbohydrate binding properties were described by affinity assays and computational docking. Biological assays were performed in order to evaluate the lectin edematogenic activity. The crystal structure of CRLI was established to a 1.8 A resolution in order to determine a structural basis for these differing activities. The structure of CRLI is closely homologous to those of other legume lectins at the monomer level and assembles into tetramers as do many of its homologues. The CRLI carbohydrate binding site was predicted by docking with a specific inhibitory trisaccharide. CRLI possesses a hydrophobic pocket for the binding of alpha-aminobutyric acid and that pocket is occupied in this structure as are the binding sites for calcium and manganese cations characteristic of legume lectins. CRLI route-dependent effects for acute inflammation are related to its carbohydrate binding domain (due to inhibition caused by the presence of alpha-methyl-mannoside), and are based on comparative analysis with ConA crystal structure. This may be due to carbohydrate binding site design, which differs at Tyr12 and Glu205 position.

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Chitin is one of the most abundant and cheaply available biopolymers in Nature. Chitin has become a valuable starting material for many biotechnological products through manipulation of its N-acetyl functionality, which can be cleaved under mild conditions using the enzyme family of de-N-acetylases. However, the chemoselective enzymatic re-acylation of glucosamine derivatives, which can introduce new stable functionalities into chitin derivatives, is much less explored. Herein we describe an acylase (CmCDA from Cyclobacterium marinum) that catalyzes the N-acylation of glycosamine with a range of carboxylic acids under physiological reaction conditions. This biocatalyst closes an important gap in allowing the conversion of chitin into complex glycosides, such as C5-modified sialosides, through the use of highly selective enzyme cascades.

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Reference:
Tetrahydropyran – Wikipedia,
Tetrahydropyran – an overview | ScienceDirect Topics

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Glycosaminoglycans (GAGs) are important polysaccharides with various biological functions, but their structures in solution are affected in a complex manner by their component residues. We successfully measured the vacuum-ultraviolet circular dichroism (VUVCD) spectra of six GAGs (chondroitin, chondroitin sulfates, hyaluronic acid, and heparin) and their component sugars (N-acetylaminosugars and uronic acid) from 240 to 160nm by a synchrotron-radiation VUVCD spectrophotometer in aqueous solutions at 25 C. These comprehensive VUVCD spectra revealed the characteristic contribution of the constituent functional groups (sulfate, carboxyl, hydroxyl, hydroxymethyl, acetamido, etc.) and intersaccharide linkages to the higher energy transition of oxygen lone-pair electrons, giving basic information for understanding the detailed structures of GAGs in solution and for their theoretical assignment.

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Cell density cultivation of recombinant Escherichia coli strains harboring the nodC gene (encoding chitooligosaccharide synthase) from Azorhizobium caulinodans has been previously described as a practical method for the preparation of gram-scale quantities of penta-N-acetyl-chitopentaose. We have now extended this method to the production of allylated derivative of penta-N-acetyl-chitopentaose by using allyl 2-acetamido-2-deoxy-beta-d- glucopyranoside (2) as the initial acceptor for the synthesis of target pentaoside in vivo.

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Reference:
Tetrahydropyran – Wikipedia,
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The development of sialidase inhibitors is an area of continuing interest due to their potential use as therapeutic agents to combat viral and bacterial infections. Herein, we report our studies involving the sialidase from the pathogen Vibrio cholerae, through the modelling, synthesis and biological evaluation of mimetics of 5-acetamido-2,6-anhydro-3,5-dideoxy-d-glycero-d- galacto-non-2-enonic acid (Neu5Ac2en, 1), a naturally occurring sialidase inhibitor. These mimetics are O- and S-glycosides of N-acetyl-d-glucosaminuronic acid in which the aglycone portion effectively replaces the C-6 glycerol side chain of Neu5Ac2en (1). The choice of aglycones was aided by use of the X-ray crystal structure of V. cholerae sialidase complexed with Neu5Ac2en (1). All Neu5Ac2en mimetics tested were found to inhibit V. cholerae sialidase as determined using a standard fluorometric assay.

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Porphyromonas gingivalis (P.g.)-induced TNF-alpha can be affected by muramyl dipeptide (MDP) in a biphasic concentration-dependent manner. We found that in P.g.-exposed macrophages, treatment with 10 mug/mL of MDP (MDP-low) up-regulated TNF-alpha by 29%, while 100 mug/mL or higher (MDP-high) significantly decreased it (16% to 38%). MDP-high was found to affect the ubiquitin-editing enzyme A20 and activator protein 1 (AP1). An AP1 binding site was found in the promoter region of A20. A20 promoter activity was up-regulated after transfection of AP1 cDNA in cells. Four analogues of MDP (3-6) were prepared through a convergent strategy involving the synthesis of two unique carbohydrate fragments, 7a and 7b, using the peptide coupling reagents, EDCI and HOAt. Analogue 4 improved MDP function and P.g.-induced activities. We propose a new signaling pathway for TNF-alpha induction activated after exposing macrophages to both P.g. and MDP-high or analogue 4.

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Reference£º
Tetrahydropyran – Wikipedia,
Tetrahydropyran – an overview | ScienceDirect Topics