N-acetyl-D-Glucosamine
(Synonyms: N-乙酰-D-氨基葡萄糖; N-Acetyl-2-amino-2-deoxy-D-glucose) 目录号 : GC41283
Monosaccharide derivative of glucose
Cas No.:7512-17-6
Sample solution is provided at 25 µL, 10mM.
Quality Control & SDS
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- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
N-acetyl-D-Glucosamine (GlcNAc) is a monosaccharide derivative of glucose. It is released by the action of O-GlcNAcase, in mammalian systems from proteins that have been post-translationally modified with O-GlcNAc. Levels of O-GlcNAcylation proteins from Alzheimer’s disease brain extracts are decreased as compared to that in controls, suggesting that release of GlcNAc may contribute to pathogenesis. In E. coli, GlcNAc induces the expression of multidrug exporter genes, indicating that this sugar can alter gene expression. GlcNAc is also the monomeric unit of chitin, which is found in fungi and many invertebrates, including crustaceans, insects, and nematodes. For this reason, chemicals that inhibit the incorporation of GlcNAc into chitin are cytotoxic to these organisms.
| Cas No. | 7512-17-6 | SDF | |
| 别名 | N-乙酰-D-氨基葡萄糖; N-Acetyl-2-amino-2-deoxy-D-glucose | ||
| Canonical SMILES | O=CC(NC(=O)C)C(O)C(O)[C@H](O)CO | ||
| 分子式 | C8H15NO6 | 分子量 | 221.2 |
| 溶解度 | ≤10mg/ml in DMSO;0.25mg/ml in dimethyl formamide | 储存条件 | Store at -20°C, stored under nitrogen |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 4.5208 mL | 22.604 mL | 45.208 mL |
| 5 mM | 0.9042 mL | 4.5208 mL | 9.0416 mL |
| 10 mM | 0.4521 mL | 2.2604 mL | 4.5208 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Molecular dynamics analysis of N-acetyl-D-Glucosamine against specific SARS-CoV-2's pathogenicity factors
PLoS One 2021 May 27;16(5):e0252571.PMID:34043733DOI:10.1371/journal.pone.0252571.
The causative agent of the pandemic identified as SARS-CoV-2 leads to a severe respiratory illness similar to SARS and MERS with fever, cough, and shortness of breath symptoms and severe cases that can often be fatal. In our study, we report our findings based on molecular docking analysis which could be the new effective way for controlling the SARS-CoV-2 virus and additionally, another manipulative possibilities involving the mimicking of immune system as occurred during the bacterial cell recognition system. For this purpose, we performed molecular docking using computational biology techniques on several SARS-CoV-2 proteins that are responsible for its pathogenicity against N-acetyl-D-Glucosamine. A similar molecular dynamics analysis has been carried out on both SARS-CoV-2 and anti-Staphylococcus aureus neutralizing antibodies to establish the potential of N-acetyl-D-Glucosamine which likely induces the immune response against the virus. The results of molecular dynamic analysis have confirmed that SARS-CoV-2 spike receptor-binding domain (PDB: 6M0J), RNA-binding domain of nucleocapsid phosphoprotein (PDB: 6WKP), refusion SARS-CoV-2 S ectodomain trimer (PDB: 6X79), and main protease 3clpro at room temperature (PDB: 7JVZ) could bind with N-acetyl-D-Glucosamine that these proteins play an important role in SARS-CoV-2's infection and evade the immune system. Moreover, our molecular docking analysis has supported a strong protein-ligand interaction of N-acetyl-D-Glucosamine with these selected proteins. Furthermore, computational analysis against the D614G mutant of the virus has shown that N-acetyl-D-Glucosamine affinity and its binding potential were not affected by the mutations occurring in the virus' receptor binding domain. The analysis on the affinity of N-acetyl-D-Glucosamine towards human antibodies has shown that it could potentially bind to both SARS-CoV-2 proteins and antibodies based on our predictive modelling work. Our results confirmed that N-acetyl-D-Glucosamine holds the potential to inhibit several SARS-CoV-2 proteins as well as induce an immune response against the virus in the host.
Interactions of N-acetyl-D-glucosamine-conjugated silk fibroin with lectins, cytoskeletal proteins and cardiomyocytes
Colloids Surf B Biointerfaces 2021 Feb;198:111406.PMID:33250416DOI:10.1016/j.colsurfb.2020.111406.
We have reported that cytoskeletal proteins such as desmin and vimentin are expressed on the surface of muscle, mesenchymal and cancer cells, and possess N-acetyl-β-D-glucosamine (β-GlcNAc) residue-binding properties. As cell-recognizable β-GlcNAc residue-bearing biopolymer, we prepared glycoconjugates (SF-GlcNAc) composed of silk fibroin (SF) and monosaccharide N-acetyl-D-Glucosamine (GlcNAc) by chemical modification using cyanuric chloride. The covalent immobilization of GlcNAc into SF was assessed by 1H-NMR measurements. The 1H-NMR spectrum of SF-GlcNAc conjugates showed new peaks attributed to the methyl protons of the N-acetyl group in GlcNAc, and the integration of these peaks revealed that the GlcNAc content in the conjugates was 9 wt%. The existence of β-GlcNAc residues in SF-GlcNAc was examined by the criteria using lectins such as wheat germ agglutinin (WGA). Addition of WGA to SF-GlcNAc solution caused an increase in the turbidity of the solution due to lectin-mediated aggregation. Solid-phase lectin binding assay based on the biotin-avidin interaction showed that biotinylated succinylated WGA bound more strongly onto SF-GlcNAc conjugate-coated wells compared to SF-coated well. Following the establishment of the existence of β-GlcNAc residues in SF-GlcNAc, the interaction of SF-GlcNAc with desmin was examined by enzyme-linked immunosorbent assay using anti-desmin antibody. The stronger binding of desmin was observed for SF-GlcNAc conjugate-coated wells compared to SF-coated wells. The use of SF-GlcNAc conjugates as a substrate for culturing desmin-expressing human cardiac myocytes demonstrated an increase in the numbers of attached cells and proliferating cells on the conjugate-coated wells compared to SF-coated wells. These results suggest that the immobilization of monosaccharide GlcNAc is a useful method for the versatile functionalization of SF as an application in tissue engineering.
Efficient production of D-glucosamine by diacetylchitobiose deacetylase catalyzed deacetylation of N-acetyl-D-Glucosamine
Biotechnol Lett 2022 Mar;44(3):473-483.PMID:35072843DOI:10.1007/s10529-022-03225-2.
Objective: D-Glucosamine (GlcN) is an important amino sugar with various applications in medicine, food & beverages, nutritional supplements, and dairy products. This study aimed to produce GlcN from N-acetyl-D-Glucosamine (GlcNAc) with an efficient deacetylase, and apply different strategies to enhance GlcN production. Results: We screened a series of deacetylases that involved in the deacetylation of GlcNAc to form GlcN. A diacetylchitobiose deacetylase (TKDac) from Thermococcus kodakarensis exhibited high-efficient deacetylation activity for GlcNAc, yet mostly in the form of inclusion bodies. The soluble expression of TKDac was improved by a co-expressing molecular chaperone (groEL) and TKDac, and insertion of rare codon ATA encoding isoleucine. As such, the recombinant strain TKEL4 was constructed to express TKDac, and 48 g/L GlcN was achieved by TKDac-catalyzed deacetylation. To overcome the inhibition of byproduct (acetate), immobilized TKDac was carried out to produce GlcN from GlcNAc. The immobilized TKDac was conveniently re-used for several batches (above 8) with a 90% conversion rate. Conclusions: TKDac from T. kodakarensis was found to be an efficient deacetylase to produce GlcN. Co-expression of molecular chaperone and target protein, and insertion of rare codons were effective to improve the soluble expression of TKDac. The immobilized TKDac represents a promising method for future GlcN production.
The effect of D-(+)-glucosamine, N-acetyl-D-Glucosamine and tetraethylene glycol on the stability of oxytocin in aqueous solution
Pharmazie 2021 Oct 1;76(10):480-483.PMID:34620274DOI:10.1691/ph.2021.1081.
The aim of the present study was to identify the effect of D-(+)-glucosamine, N-acetyl-D-Glucosamine, tetraethyleneglycol, and the mixture of these additives on the stability of oxytocin in phosphate and acetate buffer solutions, at pH 4.5. Our findings demonstrate that tetraethyleneglycol has a destabilizing effect on oxytocin in both phosphate buffer and acetate buffer. D-(+)-Glucosamine hydrochloride had small to negligible effect at low concentrations, yielding a slight improvement lower concentrations of the additive in the presence of the buffers used, but at higher concentrations it increased the rate of degradation. N-acetyl-D-Glucosamine showed a possibly slight improvement to the stability of oxytocin. It is hypothesized that the different effect of N-acetyl-D-Glucosamine compared to D-(+)-glucosamine is a consequence of the free amine group in D-(+)-glucosamine promoting a faster degradation, while the amino group is acetylated in N-acetyl-D-Glucosamine and therefore no longer reactive in the same way. While it remains unclear why tetraethyleneglycol has a destabilizing effect on oxytocin, the D-(+)-glucosamine results aid in deepening our understanding of the degradation mechanism of oxytocin.
Structural dynamics and vibrational feature of N-acetyl-D-Glucosamine in aqueous solution
Spectrochim Acta A Mol Biomol Spectrosc 2021 Oct 5;259:119918.PMID:33991814DOI:10.1016/j.saa.2021.119918.
Molecular dynamics simulations and DFT calculations were performed for the demonstration of the structural dynamics and vibrational feature of N-acetyl-D-Glucosamine (NAG) in solution phase. The interactions between NAG and solvent molecules were evaluated through spatial distribution function and radial distribution function, and the preferred conformations of NAG in aqueous solution were revealed by cluster analysis. Results from normal mode analysis show that the solvent induced structural fluctuation of NAG could be reflected in the vibrational feature of specific chromophores, thus we can evaluate the molecular structure with the help of its vibrational signature based on the built correlation between molecular structure and vibrational frequencies of specific groups.