LDAO
(Synonyms: 月桂基二甲基氧化胺) 目录号 : GC44046
A zwitterionic detergent
Cas No.:1643-20-5
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
LDAO is a zwitterionic detergent that can be used to solubilize membrane proteins. It has a critical micelle concentration (CMC) of 1-2 mM. LDAO has been used to solubilize and extract colicin A from the plasma membrane and for inactivation of enveloped viruses. It has also been used in combination with 1-decanoyl-rac-glycerol (10MAG) to encapsulate proteins and nucleic acids dissolved in low viscosity fluids.
| Cas No. | 1643-20-5 | SDF | |
| 别名 | 月桂基二甲基氧化胺 | ||
| Canonical SMILES | CCCCCCCCCCCC[N+](C)([O-])C | ||
| 分子式 | C14H31NO | 分子量 | 229.4 |
| 溶解度 | DMF: 0.3 mg/ml,DMSO: 0.1 mg/ml,Ethanol: 15 mg/ml,PBS (pH 7.2): 0.1 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 | 4.3592 mL | 21.796 mL | 43.592 mL |
| 5 mM | 0.8718 mL | 4.3592 mL | 8.7184 mL |
| 10 mM | 0.4359 mL | 2.1796 mL | 4.3592 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。
Addition of Lauryldimethylamine N-Oxide (LDAO) to a Copper-Free Click Chemistry Reaction Improves the Conjugation Efficiency of a Cell-Free Generated CRM197 Variant to Clinically Important Streptococcus pneumoniae Serotypes
ACS Omega 2022 Sep 20;7(39):34921-34928.PMID:36211053DOI:10.1021/acsomega.2c03481.
Strain-promoted azide-alkyne cycloaddition (SPAAC) reactions like click chemistry have the potential to be highly scalable, robust, and cost-effective methods for generating small- and large-molecule conjugates for a variety of applications. However, despite method improvements, the rates of copper-based click chemistry reactions continue to be much faster than the rates of copper-free click chemistry reactions, which makes broader deployment of click chemistry challenging from a safety and compatibility standpoint. In this study, we used a zwitterionic detergent, namely, lauryldimethylamine N-oxide (LDAO), in a copper-free click chemistry reaction to investigate its impact on the generation of conjugate vaccines (CVs). For this, we utilized an Xpress cell-free protein synthesis (CFPS) platform to generate a proprietary variant of CRM197 (eCRM) containing non-native amino acids (nnAA) with azide-containing side chains as a carrier protein for conjugation to several clinically relevant dibenzocyclooctyne (DBCO)-derivatized S. pneumoniae serotypes (types 3, 5, 18C, and 19A). For conjugation, we performed copper-free click chemistry in the presence and absence of LDAO. Our results show that the addition of LDAO significantly enhanced the reaction kinetics to generate larger conjugates, which were similarly immunogenic and equally stable to conjugates generated without LDAO. Most importantly, the addition of LDAO substantially improved the efficiency of the conjugation process. Thus, our results for the first time show that the addition of a zwitterionic surfactant to a copper-free click chemistry reaction can significantly accelerate the reaction kinetics along with improving the efficiency of the conjugation process.
Derivation of original RESP atomic partial charges for MD simulations of the LDAO surfactant with AMBER: applications to a model of micelle and a fragment of the lipid kinase PI4KA
J Biomol Struct Dyn 2017 Jan;35(1):159-181.PMID:26998712DOI:10.1080/07391102.2015.1135822.
In this paper, we describe the derivation and the validation of original RESP atomic partial charges for the N, N-dimethyl-dodecylamine oxide (LDAO) surfactant. These charges, designed to be fully compatible with all the AMBER force fields, are at first tested against molecular dynamics simulations of pure LDAO micelles and with a fragment of the lipid kinase PIK4A (DI) modeled with the QUARK molecular modeling server. To model the micelle, we used two distinct AMBER force fields (i.e. Amber99SB and Lipid14) and a variety of starting conditions. We find that the micelle structural properties (such as the shape, size, the LDAO headgroup hydration, and alkyl chain conformation) slightly depend on the force field but not on the starting conditions and more importantly are in good agreement with experiments and previous simulations. We also show that the Lipid14 force field should be used instead of the Amber99SB one to better reproduce the C(sp3)C(sp3)C(sp3)C(sp3) conformation in the surfactant alkyl chain. Concerning the simulations with LDAO-DI protein, we carried out different runs at two NaCl concentrations (i.e. 0 and 300 mM) to mimic, in the latter case, the experimental conditions. We notice a small dependence of the simulation results with the LDAO parameters and the salt concentration. However, we find that in the simulations, three out of four tryptophans of the DI protein are not accessible to water in agreement with our fluorescence spectroscopy experiments reported in the paper.
Effect of amphiphilic surfactant LDAO on the solubilization of DOPC vesicles and on the activity of Ca(2+)-ATPase reconstituted in DOPC vesicles
Gen Physiol Biophys 2007 Dec;26(4):290-7.PMID:18281747doi
Solubilization of large unilamellar 1,2-dioleoylphosphatidylcholine (DOPC) vesicles by N-dodecyl-N,N-dimethylamine-N-oxide (LDAO) was studied using turbidimetry. From turbidity data, the LDAO partition coefficient between the aqueous phase and DOPC bilayers was obtained. Using this partition coefficient, the LDAO:DOPC molar ratio in the bilayer was calculated and effects of LDAO on the bilayer stability, bilayer thickness and on the phosphohydrolase activity of sarcoplasmic reticulum Ca(2+) transporting ATPase (SERCA) reconstituted into DOPC were compared at the same LDAO:DOPC molar ratios in the bilayer. The sequence "bilayers in vesicles - bilayer fragments (flat mixed micelles) - tubular mixed micelles - globular mixed micelles" was suggested for the solubilization mechanism of DOPC vesicles from the combined turbidimetric and small-angle neutron scattering (SANS) results. The effective molecular packing parameter delta = 0.5, corresponding to the mixed bilayer - mixed tubular micelle transition, was calculated from fragmental DOPC and LDAO volumes at the molar ratio LDAO:DOPC = 2.00 in bilayers, in the middle of transition region observed earlier experimentally by small-angle neutron scattering (SANS). The bilayer thickness decrease induced by LDAO in DOPC observed by SANS did not result in the SERCA phosphohydrolase activity decrease and this indicates that some other factors compensated this bilayer effect of LDAO. The ATPase activity decrease at higher LDAO concentrations was caused by the bilayer deformation. This deformation resulted in the formation of non-bilayer aggregates in LDAO+DOPC system.
[Influence of LDAO on the conformation and release of bacteriochlorophyll of peripheral light-harvesting complex (LH2) from Rhodobacter azotoformans]
Guang Pu Xue Yu Guang Pu Fen Xi 2010 Oct;30(10):2807-11.PMID:21137426doi
The aim of this study is to reveal the interaction relationships between lauryl dimethylamine N-oxide (LDAO) and peripheral light-harvesting complex (LH2) as well as the influence of LDAO on structure and function of LH2. In the present work, the effects of LDAO on the conformation and release processes of bacteriochlorophyll (BChl) of LH2 when incubated under different temperature and pH in the presence and absence of LDAO were investigated by spectroscopy. The results indicated that (1) the presence of LDAO resulted in alterations in the conformation, alpha-helix content, and spectra of Tyr and B850 band of LH2 at room temperature and pH 8.0. Moreover, energy transfer efficiency of LH2 was enhanced markedly in the presence of LDAO. (2) At 60 degrees C, both the B800 and B850 band of LH2 were released and transited into free BChl at pH 8.0. However, the release rates of bacteriochlorophylls of B800 and B850 band from LH2 were slowed down and the release processes were changed when incubated in the presence of LDAO. Hence, the stability of LH2 was improved in the presence of LDAO. (3) The accelerated release processes of bacteriochlorophylls of B800 and B850 band of LH2 were induced to transform into bacteriopheophytin (BPhe) and free BChl by LDAO in strong acid and strong alkalic solution at room temperature. However, the kinetic patterns of the B800 and B850 band were remarkably different. The release and self-assemble processes of B850 in LH2 were observed in strong acid solution without LDAO. Therefore, the different release behaviors of B800 and B850 of LH2 are induced by LDAO under different extreme environmental conditions.
Regulation of CD40 reconstitution into a liposome using different ratios of solubilized LDAO to lipids
Colloids Surf B Biointerfaces 2008 Mar 15;62(1):51-7.PMID:17981441DOI:10.1016/j.colsurfb.2007.09.021.
The integral membrane protein CD40 was found on the surface of B lymphocytes that interact with CD40L on T cells during the immune response. The hydrophobic transmembrane domains of membrane proteins can be stabilized in detergent or in lipid bilayers such as liposomes. Membrane proteins can be incorporated into the liposome in a similar fashion to the way they are handled in vivo. In this study, a large amount of full-sequence CD40 was produced using a bacterial system that contained a Mistic construct. The CD40 was then reconstituted into liposomes by detergent-mediated reconstitution. All stages in the process of liposome disruption with various detergent ratios were easily observed by monitoring the optical density. The structure of the liposome and the reconstitution of CD40 were confirmed by cryo-TEM. The results of the present study show that the detergent ratio had an effect on the structure of the liposome and the amount of CD40 that was reconstituted into the liposome.