79695-15-1

Usage

InChI:InChI=1/C7H15NO5/c1-12-7-6(11)5(10)4(9)3(2-8)13-7/h3-7,9-11H,2,8H2,1H3/t3?,4-,5?,6-,7u/m1/s1

Upstream product

• 6619-09-6 methyl 6-O-tosyl-α-D-glucopyranoside 
• 67-56-1 methanol 
• 104652-58-6 6-azido-6-deoxy-1,2-O-isopropylidene-β-L-idofuranose 
• 97-30-3 methyl-alpha-D-glucopyranoside 
• 866556-24-3 avrainvilloside 
• 23661-33-8 methyl 2,3,4-tri-O-acetyl-6-O-(p-tolylsulfonyl)-α-D-glucopyranoside 
• 66224-56-4 methyl 6-azido-6-deoxy-α-D-mannopyranoside 
• 617-04-9 (2R,3S,4S,5S,6S)-2-(hydroxymethyl)-6-methoxytetrahydro-2H-pyran-3,4,5-triol 
• 18439-60-6 methyl 2,3,4-tri-O-acetyl-6-O-p-toluenesulfonyl-α-D-mannopyranoside 
• 18439-61-7 methyl 2,3,4-tri-O-acetyl-6-azido-6-deoxy-α-D-mannopyranoside 
• 4990-80-1 Methyl-6-chlor-6-deoxy-α-D-mannopyranosid 
• 51103-66-3 methyl 6-O-(p-tolylsulfonyl)-α-D-mannopyranoside 
• 1332641-39-0 C₆₃H₆₇NO₉ 
• 104652-56-4 3-O-acetyl-1,2-O-isopropylidene-5-O-methylsulfonyl-6-O-(p-nitrobenzoyl)-D-glucofuranose 

Downstream Products

• 86462-45-5 methyl 6-(benzyloxycarbonyl)amino-6-deoxy-α-D-glucopyranoside 
• 1198571-24-2 methyl 6-(o-nitro)benzamidyl-6-deoxy-α-D-glucopyranoside 
• 1180509-83-4 1-amino-1-deoxy-N-(methyl 6-amino-6-deoxy-α-D-glucopyranosid-6-yl)-5,6-oxomethylidenenojirimycin 
• 628328-88-1 methyl 6-(4-bromomethyl-3-nitrobenzoylamino)-6-deoxy-α-D-glucopyranoside 
• 1338809-58-7 methyl 6-deoxy-6-((2S,6S)-6-methoxy-2-(hydroxymethyl)morpholin-4-yl)-α-D-glucopyranoside 
• 1198571-26-4 methyl 6-(o-nitro)benzamidyl-6-deoxy-α-D-mannopyranoside 
• 1446093-36-2 C₁₄H₂₁NO₅ 
• 1446093-37-3 C₁₄H₂₀N₂O₇ 
• 1446093-38-4 C₁₅H₂₀N₂O₅ 
• 1446093-39-5 C₁₄H₂₀ClNO₅ 
• 1446093-46-4 methyl 6-(phenylsulfonylamido)-6-deoxy-α-D-mannopyranoside 
• 58994-96-0 Ranimustine 
• 86462-44-4 methyl 6-benzyloxycarbonylamino-4-chloro-4,6-dideoxy-α-D-galactopyranoside 

Relevant academic research and scientific papers

Design, physico-chemical characterization andin vitrobiological activity of organogold(iii) glycoconjugates

To develop new metal-based glycoconjugates as potential anticancer agents, four organometallic gold(iii)-dithiocarbamato glycoconjugates of the type [AuIII(2-Bnpy)(SSC-Inp-GlcN)](PF6) (2-Bnpy: 2-benzylpyridine; Inp: isonipecotic moie

The strategic use of: Para-quinone methides to access synthetically challenging and chemoselective α,α-diarylmethyl N-glycosides from unprotected carbohydrate amines

Reported herein is a practical route to access synthetically challenging and chemoselective α,α-diarylmethyl N-glycosides via Sc(OTf)3-catalyzed 1,6-conjugate addition of amino sugars with para-quinone methides (p-QMs). The reactions proceed smoothly without a base and under mild reaction conditions with a broad substrate scope and moderate to good yields.

An innovative and efficient route to the synthesis of metal-based glycoconjugates: proof-of-concept and potential applications

With a view to developing more efficient strategies to the functionalization of metallodrugs with carbohydrates, we here report on an innovative and efficient synthetic route to generate gold(iii) glycoconjugates in high yields and purity. The method is based on the initial synthesis of the zinc(ii)-dithiocarbamato intermediate [ZnII(SSC-Inp-GlcN)2] (Inp = isonipecotic moiety; GlcN = amino-glucose) followed by the transfer of the glucoseisonipecoticdithiocarbamato ligand to the gold(iii) center via transmetallation reaction between the zinc(ii) intermediate and K[AuIIIBr4] in 1?:?2 stoichiometric ratio, yielding the corresponding glucose-functionalized gold(iii)-dithiocarbamato derivative [AuIIIBr2(SSC-Inp-GlcN)]. No protection/deprotection of the amino-glucose scaffold and no chromatographic purification were needed. The synthetic protocol was optimized for glucose precursors bearing the amino function at either the C2 or the C6 position, and works in the case of both α and β anomers. The application of the synthetic strategy was also successfully extended to other metal ions of biomedical interest, such as gold(i) and platinum(ii), to obtain [AuI(SSC-Inp-GlcN)(PPh3)] and [PtII(SSC-Inp-GlcN)2], respectively. All compounds were fully characterized by elemental analysis, mid- and far-IR, mono- and multidimensional NMR spectroscopy, and, where possible, X-ray crystallography. Results and potential applications are here discussed.

A new way to do an old reaction: highly efficient reduction of organic azides by sodium iodide in the presence of acidic ion exchange resin

Organic azides are readily reduced to the corresponding amines by treatment with sodium iodide in the presence of acidic ion exchange resin. The process, optimal when performed at 40 °C and 200 mbar pressure on a rotatory evaporator, is extremely efficient, clean, and tolerant of a variety of functional groups.

Cinnamide Derivatives of d-Mannose as Inhibitors of the Bacterial Virulence Factor LecB from Pseudomonas aeruginosa

Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen with high antibiotic resistance. Its lectin LecB was identified as a virulence factor and is relevant in bacterial adhesion and biofilm formation. Inhibition of LecB with carbohydrate-based ligands results in a decrease in toxicity and biofilm formation. We recently discovered two classes of potent drug-like glycomimetic inhibitors, that is, sulfonamides and cinnamides of d-mannose. Here, we describe the chemical synthesis and biochemical evaluation of more than 20 derivatives with increased potency compared to the unsubstituted cinnamide. The structure–activity relationship (SAR) obtained and the extended biophysical characterization allowed the experimental determination of the binding mode of these cinnamides with LecB. The established surface binding mode now allows future rational structure-based drug design. Importantly, all glycomimetics tested showed extended receptor residence times with half-lives in the 5–20 min range, a prerequisite for therapeutic application. Thus, the glycomimetics described here provide an excellent basis for future development of anti-infectives against this multidrug-resistant pathogen.

Cinnamide Derivatives of d-Mannose as Inhibitors of the Bacterial Virulence Factor LecB from Pseudomonas aeruginosa

Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen with high antibiotic resistance. Its lectin LecB was identified as a virulence factor and is relevant in bacterial adhesion and biofilm formation. Inhibition of LecB with carbohydrate-based ligands results in a decrease in toxicity and biofilm formation. We recently discovered two classes of potent drug-like glycomimetic inhibitors, that is, sulfonamides and cinnamides of d-mannose. Here, we describe the chemical synthesis and biochemical evaluation of more than 20 derivatives with increased potency compared to the unsubstituted cinnamide. The structure–activity relationship (SAR) obtained and the extended biophysical characterization allowed the experimental determination of the binding mode of these cinnamides with LecB. The established surface binding mode now allows future rational structure-based drug design. Importantly, all glycomimetics tested showed extended receptor residence times with half-lives in the 5–20 min range, a prerequisite for therapeutic application. Thus, the glycomimetics described here provide an excellent basis for future development of anti-infectives against this multidrug-resistant pathogen.

Glycomimetics as pseudomonas Aeruginosa lectin inhibitors

The present invention relates to fucose- and mannose-derived glycomimetics and their general use in prophylaxis or treatment of Pseudomonas aeruginosa infections including respiratory tract infections, urinary tract infections, nosocomial infections and chronic wound infections in a patient encompassing a patient suffering already from cystic fibrosis. Said glycomimetics are inhibitors of Pseudomonas aeruginosa lectin LecB.

GLYCOMIMETICS AS PSEUDOMONAS AERUGINOSA LECTIN INHIBITORS

The present invention relates to fucose- and mannose-derived glycomimetics and their general use in prophylaxis or treatment of Pseudomonas aeruginosa infections including respiratory tract infections, urinary tract infections, nosocomial infections and chronic wound infections in a patient encompassing a patient suffering already from cystic fibrosis. Said glycomimetics are inhibitors of Pseudomonas aeruginosa lectin LecB.

Discovery of two classes of potent glycomimetic inhibitors of pseudomonas aeruginosa LecB with distinct binding modes

The treatment of infections due to the opportunistic pathogen Pseudomonas aeruginosa is often difficult, as a consequence of bacterial biofilm formation. Such a protective environment shields the bacterium from host defense and antibiotic treatment and secures its survival. One crucial factor for maintenance of the biofilm architecture is the carbohydrate-binding lectin LecB. Here, we report the identification of potent mannose-based LecB inhibitors from a screening of four series of mannosides in a novel competitive binding assay for LecB. Cinnamide and sulfonamide derivatives are inhibitors of bacterial adhesion with up to a 20-fold increase in affinity to LecB compared to the natural ligand methyl mannoside. Because many lectins of the host require terminal saccharides (e.g., fucosides), such capped structures as reported here may offer a beneficial selectivity profile for the pathogenic lectin. Both classes of compounds show distinct binding modes at the protein, offering the advantage of a simultaneous development of two new lead structures as anti-pseudomonadal drugs with an anti-virulence mode of action.

Synthesis and glycosidase inhibitory profiles of functionalised morpholines and oxazepanes

In this work libraries of morpholines and oxazepanes have been prepared via the reductive amination reaction between dialdehydes, derived from carbohydrates, and a range of amines. In this way, functionalised morpholines and oxazepanes have been prepared