16-Doxylstearic Acid
(Synonyms: 16-DOXYL-硬脂酸) 目录号 : GC41944
A hydrophobic spin label
Cas No.:53034-38-1
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
| Cas No. | 53034-38-1 | SDF | |
| 别名 | 16-DOXYL-硬脂酸 | ||
| Canonical SMILES | [O]N1C(C)(C)COC1(CC)CCCCCCCCCCCCCCC(O)=O | ||
| 分子式 | C22H42NO4 | 分子量 | 384.6 |
| 溶解度 | DMF: 30 mg/ml,DMSO: 10 mg/ml,Ethanol: 20 mg/ml | 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 | 2.6001 mL | 13.0005 mL | 26.001 mL |
| 5 mM | 0.52 mL | 2.6001 mL | 5.2002 mL |
| 10 mM | 0.26 mL | 1.3001 mL | 2.6001 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。
Location of spectroscopic probes in self-aggregating assemblies. I. The case for 5-doxylstearic acid methyl ester serving as a benchmark spectroscopic probe to study micelles
J Phys Chem B 2006 May 25;110(20):9791-9.PMID:16706430DOI:10.1021/jp060515y.
A strategy to locate spectroscopic probes in micelles is presented which involves establishing a "benchmark" probe, i.e., one whose position is well-known and against which other probe positions may be established. Theoretically calculated values of the fraction of the micelle polar shell occupied by water, H(shell), are compared with experimental values measured with the spin probe 5-doxylstearic acid methyl ester (5DSE) for a series of sodium n-alkyl sulfate micelles as functions of both the aggregation numbers and the alkyl chain length. The theoretical values involve one adjustable parameter that may be taken to be the volume in the polar shell inaccessible to water, V(dry). Under the hypothesis that the thickness of the polar shell (5 Angstroms) remains constant as either the aggregation number or the chain length is varied, we find excellent agreement between the theoretical predictions and the experimental results, using the same value of V(dry) for chain lengths 8-12 and for aggregation numbers varying from approximately 38 to 130. We argue that these are compelling reasons that 5DSE follows the zero-order model (ZOM) of probe location. The ZOM applies to any probe that rapidly diffuses within the confines of the micelle polar shell and nowhere else. Thus, 5DSE can serve as a benchmark in the sodium alkyl sulfate micelles. As a further check, results are also presented for ammonium dodecyl sulfate micelles, where 5DSE is also found to follow the ZOM, i.e, no further adjustable parameters are needed to pass from the sodium alkyl sulfate micelles to ammonium dodecyl sulfate micelles. In contrast, results are also presented for a similar spin probe 16-Doxylstearic Acid methyl ester (16DSE) that is found not to adhere to the ZOM in any of the micelles. A simple first-order correction to the ZOM in which 16DSE is displaced slightly from the polar shell is shown to account for the results well. The necessary displacements, which range from about 0.7 Angstroms outside the polar shell to 1.3 Angstroms inside, are not correlated with either chain lengths or aggregation numbers; however, they correlate rather well with H(shell). Calibrations of 6-, 7-, 10-, and 12DSE spin probes are presented in the Appendix, making them available to measure microviscosities and effective water concentrations.
Beta-blockers and benzodiazepines location in SDS and bile salt micellar systems. An ESR study
J Pharm Biomed Anal 2007 Sep 21;45(1):62-69.PMID:17606356DOI:10.1016/j.jpba.2007.05.023.
The work here described aimed to find out the location of the different species of two families of pharmaceutical substances, namely two beta-blockers (atenolol and nadolol) and two benzodiazepines (midazolam and nitrazepam) in synthetic (sodium dodecyl sulphate, SDS) and natural (bile salts-sodium cholate and sodium deoxycholate) micellar aggregate solutions. Electronic spin resonance spectroscopy studies were carried out, at 25 degrees C and at an ionic strength of 0.10 M in NaCl, using 5-, 12- and 16-Doxylstearic Acid probes (AS). The immobilization degree of solubilized stearic acid spin probes was found to vary with the position of the nitroxide group in the sequence 5-doxylstearic acid>12-doxylstearic acid>16-Doxylstearic Acid for SDS and 12-doxylstearic acid>5-doxylstearic acid>16-Doxylstearic Acid for both bile salts investigated. Therefore, from the rotational correlational time values obtained, it can be inferred that the structure of bile salt micelles is markedly different from that of SDS micelles and the results suggest that the bile salt micelles studied have similar structure independently of differences in the molecular structure of the respective bile salts. Drug location studies were performed at pH 4.0 (SDS solutions) or 7.0 (bile salt solutions) and 10.8 in order to study the effect of the drug ionisation on its relative position on micelles. The results have shown that drug location is controlled by the (i) drug hydrophilicity and acid/base properties, with the more soluble compound in water (atenolol) exhibiting smaller variation of rotational correlational time (in SDS and bile salts solutions), and with both beta-blockers exhibiting smaller deviations in the protonated forms and (ii) the bile salt monomers, with the dihydroxylic bile salt (deoxycholate) producing larger differences. The work described herein allow us to conclude that the (protonated) beta-blockers are probably located on the surface of the detergent micelles, and linked to them by means of essentially electrostatic forces, while the (neutral) benzodiazepines are probably located deeper in the interior of the micelles.
Effects of Proteus mirabilis lipopolysaccharides with different O-polysaccharide structures on the plasma membrane of human erythrocytes
Z Naturforsch C J Biosci 2008 May-Jun;63(5-6):460-8.PMID:18669036DOI:10.1515/znc-2008-5-624.
The effects of O33 and O49 P. mirabilis lipopolysaccharides (LPSs) on human erythrocyte membrane properties were examined. Physical parameters of the plasma membrane, such as membrane lipid fluidity, physical state of membrane proteins, and osmotic fragility, were determined. The fluidity of the lipids was estimated using three spin-labeled stearic acids of doxyl derivatives: 5-doxylstearic acid, 12-doxylstearic acid, and 16-Doxylstearic Acid. All the applied labels locate to different depths of the lipid layer and provide information on the ordering of phospholipid fatty acyl chain mobility. LPSs O49 increased the membrane lipid fluidity in the polar region of the lipid bilayer as indicated by spin-labeled 5-doxylstearic acid. An increase in fluidity was also observed in the deeper region using 12-doxylstearic acid only for O33 LPSs. The highest concentration of O33 LPSs (1 mg/ml) increased the motion of membrane proteins detected by the spin-label residue of iodoacetamide. These results showed different actions of O33 and O49 LPSs on the plasma membrane due to the different chemical structures of O-polysaccharides. P. mirabilis O33 and O49 LPSs did not induce changes in the membrane cytoskeleton, osmotic fragility and lipid peroxidation of erythrocytes. On the other hand a rise in the content of carbonyl compounds was observed for the highest concentrations of O33 LPS. This result indicated protein oxidation in the erythrocyte membrane. Lipid A, the hydrophobic part of LPS, did not change the membrane lipid fluidity and osmotic fragility of erythrocytes. Smooth and rough forms of P. mirabilis LPSs were tested for their abilities for complement-mediated immunohemolysis of erythrocytes. Only one out of seven LPSs used was a potent agent of complement-mediated hemolysis. It was rough, Ra-type of P. mirabilis R110 LPS. The O-polysaccharide-dependent scheme of reaction is presented.
Modulation of Na+-Ca2+ exchange and Ca2+ permeability in cardiac sarcolemmal vesicles by doxylstearic acids
Biochim Biophys Acta 1987 Feb 12;897(1):152-8.PMID:3099842DOI:10.1016/0005-2736(87)90323-3.
We examine the effects of 5-, 12- and 16-doxylstearic acids on the Na+-Ca2+ exchange and passive Ca2+ permeability of cardiac sarcolemmal vesicles. Stearic acid is a weak stimulator of Na+-Ca2+ exchange. A doxyl moiety potentiates stimulation with the order of increasing potency being 5-, 12- and then 16-Doxylstearic Acid. Stearic acid has little effect on vesicle Ca2+ permeability but again the doxylstearates are more effective. The sequence of potency is reversed, however, from that for increasing Na+-Ca2+ exchange. 5-Doxylstearic acid most markedly exchanges passive Ca2+ flux followed by the 12-, and then 16-doxylstearic acids. Methyl esters of the doxylstearates have no effect on either Na+-Ca2+ exchange or Ca2+ permeability. We model the results as follows. For a fatty acid to stimulate Na+-Ca2+ exchange activity, an anionic charge is required to interact with the exchanger protein at the membrane surface. Stimulation is potentiated by a perturbation (such as provided by a doxyl group) within the lipid bilayer. The perturbation is most effective at a location towards the center of the bilayer. To increase passive Ca2+ permeability an anionic charge is again essential. Disorder within the bilayer is also important, but now the most important site is near the membrane surface. Results of experiments with linolenic and gamma-linolenic acid and previous studies with other fatty acids also support this model.
Erythrocytes properties in varicose veins patients
Microvasc Res 2017 May;111:72-79.PMID:28012884DOI:10.1016/j.mvr.2016.12.005.
Varicose veins (VV) are enlarged veins of the subcutaneous tissue, usually caused by faulty or damaged venous valves leading to impaired blood flow. Blood stasis, excessive clotting disorder and alterations in the vein walls are symptoms of Virchow's triad which may affect the morphotic elements of blood, including erythrocytes. The aim of this study was to investigate alterations in the properties of the erythrocytes taken from varicose veins in comparison to those from antecubital vein of patients with chronic venous disease. The investigation was conducted on whole erythrocytes using spin labeling method in EPR spectroscopy and flow cytometry. The internal viscosity of cells was determined by Tempamine. The conformation state of internal proteins, mainly hemoglobin and membrane proteins was determined by maleimide spin label (MSL, 4-maleimido-2,2,6,6-tetramethylpiperidine-1-oxyl). The plasma membrane fluidity was measured using two spin labeled fatty acids (5- and 16-Doxylstearic Acid), while conformational state of membrane protein was measured using two covalently bound spin labels MSL and ISL [4-(2-iodoacetamido)-2,2,6,6-tetramethylpiperidine-1-oxyl]. The osmotic fragility and the shape and size of the erythrocytes were also determined. A decrease in internal viscosity of the erythrocytes from varicose vein was observed. A significant decrease in lipid membrane fluidity indicated by 5-DS, which is located at the polar region of lipid layer was found in the erythrocytes from varicose vein in comparison to normal vein. A significant decrease in the motion of MSL and ISL attached to erythrocyte membrane proteins from varicose vein was found. Changes in the plasma membrane of the erythrocytes from varicose vein were also confirmed by measuring osmotic fragility. These cells were more sensitive to hemolysis than red blood cells from the peripheral blood vein. Meanwhile, no significant differences in size and shape were observed between the erythrocytes taken from varicose veins and those from peripheral veins. In conclusion, the erythrocytes from varicose veins exhibited decreased intracellular viscosity and decreased plasma membrane fluidity. At the same time, conformational changes of membrane proteins and higher osmotic fragility of these cells were found in comparison to the erythrocytes obtained from peripheral veins in the same patients with chronic venous disease. Our findings strongly suggest that presented abnormalities in the erythrocyte plasma membrane may have significant pathophysiological implications, including shortened cell survival and alterations in the hemorheology of the varicose vein blood.