2-Chloro-1,4-naphthoquinone
(Synonyms: 2-氯-1,4-萘醌) 目录号 : GC681602-Chloro-1,4-naphthoquinone 是一种活性中间体。2-Chloro-1,4-naphthoquinone 可用于多种生化研究。
Cas No.:1010-60-2
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
2-Chloro-1,4-naphthoquinone is an reactive intermediate. 2-Chloro-1,4-naphthoquinone can be used for the research of various biochemical studies[1].
[1]. Dr Anton Wagner, et al. Process for the preparation of 2-chloronaphthoquinone- (1, 4). Patent. DE1182648B.
| Cas No. | 1010-60-2 | SDF | Download SDF |
| 别名 | 2-氯-1,4-萘醌 | ||
| 分子式 | C10H5ClO2 | 分子量 | 192.6 |
| 溶解度 | 储存条件 | Store at -20°C | |
| 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 | 5.1921 mL | 25.9605 mL | 51.9211 mL |
| 5 mM | 1.0384 mL | 5.1921 mL | 10.3842 mL |
| 10 mM | 0.5192 mL | 2.5961 mL | 5.1921 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。
2-Chloro-1,4-naphthoquinone derivative of quercetin as an inhibitor of aldose reductase and anti-inflammatory agent
J Enzyme Inhib Med Chem 2015 Feb;30(1):107-13.PMID:24666303DOI:10.3109/14756366.2014.892935.
The ability of flavonoids to affect multiple key pathways of glucose toxicity, as well as to attenuate inflammation has been well documented. In this study, the inhibition of rat lens aldose reductase by 3,7-di-hydroxy-2-[4-(2-chloro-1,4-naphthoquinone-3-yloxy)-3-hydroxy-phenyl]-5-hydroxy-chromen-4-one (compound 1), was studied in greater detail in comparison with the parent quercetin (compound 2). The inhibition activity of 1, characterized by IC50 in low micromolar range, surpassed that of 2. Selectivity in relation to the closely related rat kidney aldehyde reductase was evaluated. At organ level in isolated rat lenses incubated in the presence of high glucose, compound 1 significantly inhibited accumulation of sorbitol in a concentration-dependent manner, which indicated that 1 was readily taken up by the eye lens cells and interfered with cytosolic aldose reductase. In addition, compound 1 provided macroscopic protection of colonic mucosa in experimental colitis in rats. At pharmacologically active concentrations, compound 1 and one of its potential metabolite 2-chloro-3-hydroxy-[1,4]-naphthoquinone (compound 3) did not affect osmotic fragility of red blood cells.
Anti-acute myeloid leukemia activity of 2-chloro-3-alkyl-1,4-naphthoquinone derivatives through inducing mtDNA damage and GSH depletion
Bioorg Med Chem 2018 Aug 7;26(14):4191-4200.PMID:30007564DOI:10.1016/j.bmc.2018.07.010.
2-Chloro-3-alkyl-1,4-naphthoquinone derivatives were synthesized and tested as the anti-acute myeloid leukaemia agents. The compound 9b (2-chloro-3-ethyl-5,6,7-trimethoxy-1,4-naphthoquinone) was the most potent toward HL-60 leukaemia cells. In mechanistic study for 9b, the protein levels of mtDNA-specific DNA polymerase γ (poly-γ) and mtDNA transcription factor A (mt-TFA) were decreased after the 24 h treatment, showing the occurrence of mtDNA damage. And 9b triggered cell cycle arrest at S phase accompanied by a secondary block in G2/M phase which had a direct link to the process of mtDNA damage. The dissipations of mitochondrial membrane potential and ATP also proceeded. On the other hand, 9b promoted the generation of ROS and resulted in the oxidation of intracellular GSH to GSSG. This process was coupled to the formation of adduct between 9b and GSH, detected by the UV-Vis spectrum and HRMS analysis. Depletion of GSH by buthionine sulfoximine enhanced ROS level and produced higher cytotoxicity, suggesting GSH was involved in the anti-leukemic mechanism of 9b. Together, our results provide new insights on the molecular mechanism of the derivatives of 2-Chloro-1,4-naphthoquinone and 9b might be useful for the further development into an anti-leukemia agent.
CHNQ, a novel 2-Chloro-1,4-naphthoquinone derivative of quercetin, induces oxidative stress and autophagy both in vitro and in vivo
Arch Biochem Biophys 2016 Apr 15;596:84-98.PMID:26946942DOI:10.1016/j.abb.2016.03.004.
Quercetin (Qc) shows strong antitumor effects but has limited clinical application due to poor water solubility and bioavailability. In a screening of novel semi-synthetic derivatives of Qc, 3,7-dihydroxy-2-[4-(2-chloro-1,4-naphthoquinone-3-yloxy)-3-hydroxyphenyl]-5-hydroxychromen-4-one (CHNQ) could ameliorate acetic acid induced acute colitis in vivo more efficiently than Qc. Since inflammation contributes to colorectal cancer (CRC), we have hypothesized that CHNQ may have anti-cancer effects. Using CRC cell lines HCT-116 and HT-29, we report that CHNQ was three-fold more cytotoxic than Qc along with a robust induction of apoptosis. As expected from naphthoquinones such as CHNQ, a strong induction of oxidative stress was observed. This was accompanied by reactive oxygen species (ROS) induced autophagy marked by a dramatic increase in the lipidation of LC3, decreased activation of Akt/PKB, acidic vesicle accumulation and puncta formation in HCT-116 cells treated with CHNQ. Interestingly, an incomplete autophagy was observed in HT-29 cells where CHNQ treatment led to LC3 lipidation, but not the formation of acidic vacuoles. CHNQ-induced cytotoxicity, ROS formation and autophagy were also detected in vivo in Saccharomyces cerevisiae strain RDKY3615 (WinstonS288C background). Overall, we propose that CHNQ can induce cancer cell death through the induction of oxidative stress, and may be examined further as a potential chemotherapeutic drug.
Degradation of 1,4-naphthoquinones by Pseudomonas putida
Biol Chem Hoppe Seyler 1988 Sep;369(9):1031-43.PMID:3228489DOI:10.1515/bchm3.1988.369.2.1031.
Pseudomonas putida J1 and J2, enriched from soil with juglone, are capable of a total degradation of 1,4-naphthoquinone, 2-hydroxy-1,4-naphthoquinone, and 2-Chloro-1,4-naphthoquinone. Naphthazerin and plumbagin are only converted into the hydroxyderivatives 2-hydroxynaphthazerin and 3-hydroxyplumbagin, respectively, whereas 2-amino-1,4-naphthoquinone is not attacked at all. The degradation of 1,4-naphthoquinone begins with a hydroxylation of the quinoid ring, yielding 2-hydroxy-1,4-naphthoquinone (lawsone). Lawsone is reduced to 1,2,4-trihydroxynaphthalene with consumption of NADH. The fission product of the quinol could not be detected by direct means because of its instability. However, the presence of 2-chromonecarboxylic acid, a secondary product of lawsone degradation, leads to the conclusion, that the cleavage of the quinol takes place in the meta-position. The resulting ring fission product is converted into salicylic acid by removal of the side chain, presumably as pyruvate. Further degradation of salicyclic acid leads to the formation of catechol, which is then cleaved in the ortho-position and then metabolized via the 3-oxoadipate pathway. The initial steps in the degradation of 2-Chloro-1,4-naphthoquinone, namely, the hydroxylation of the quinone to 2-chloro-3-hydroxy-1,4-naphthoquinone, followed by the elimination of the chlorine substituent lead to lawsone, which is further degraded through the pathway described. The degradation steps could be verified by the accumulation products of mutant strains blocked in different steps of lawsone metabolism. Generation of mutants was carried out by chemical and by transposon mutagenesis. The regulation of the first steps of the pathway catalysed by juglone hydroxylase and lawsone reductase, was investigated by induction experiments.
Studies in rats on in vitro inhibition and in vivo activity of vitamin-K-dependent carboxylation
Haemostasis 1986;16(5):321-36.PMID:3781349DOI:10.1159/000215305.
Vitamin-K-dependent procoagulant activity was studied in vitro by characterizing vitamin-K-dependent carboxylation and in vivo by assessing prothrombin complex activity (PCA). The kinetics of endogenous substrate carboxylation were apparently first order. Inhibition of vitamin-K-dependent carboxylation versus antagonist concentration was determined for 2,3,5,6-tetrachloropyridin-4-ol (TCP), phenindione, 2,6-dichloroindophenol sodium (2,6-DIP), 2-Chloro-1,4-naphthoquinone (chloro-K3), 2-chloro-3-phytyl-1,4-naphthoquinone (chloro-K1) and warfarin. These compounds represent different chemical classes of anticoagulants that exert their effects via vitamin K antagonism. The percent inhibition versus concentration plots exhibited a sigmoidal shape and were described by the logistic function. The following concentrations were associated with 50% inhibition of vitamin-K-dependent carboxylation: TCP = 1.23 +/- 0.238 microM (mean +/- SD), phenindione = 19.0 +/- 11.2 microM, 2,6-DIP = 116 +/- 39.2 microM, chloro-K3 = 146 +/- 62.1 microM, chloro-K1 = 285 +/- 89.3 microM and warfarin = 6.63 +/- 2.82 mM. The slope parameters of the percent inhibition versus concentration plots for chloro-K1 and phenindione were different from those for the other antagonists, suggesting a mechanism of action consistent with other data in the literature, i.e. competitive antagonism of the vitamin-K-dependent carboxylase. The relationships between in vitro parameters of vitamin-K-dependent carboxylation of precursor proteins and in vivo indices of rate of production of vitamin-K-dependent coagulation factors were studied in control animals and animals pretreated with compounds perturbing hepatic function. The in vivo rate of synthesis of prothrombin complex activity and the circulating levels of PCA were correlated with the in vitro first-order rate constant of vitamin-K-dependent carboxylation, but not with the amount of precursor proteins present. The results of these studies suggest that the rate of vitamin-K-dependent carboxylation is intimately involved in the regulation of levels and activity of vitamin-K-dependent coagulation factors.