sodium-dodecyl-sulfate and dodecyltrimethylammonium

The irritation potential of surfactants and body cleansing products was determined by evaluating the removal of dansyl chloride from the skin. Dilute solutions (2% active ingredient, w/v) of surfactants and soap extract fluorescence from the skin within 30 min. This is probably a physicochemical effect as it is too rapid to be due to a modification of epidermal cell turnover rate. Such an extraction of the fluorescent dye occurs without any clinical sign of irritation. However, it may represent an early phase of the skin irritation process, because it is related to the ranking of irritant products as determined by other assessment methods.

Topics: Betaine; Body Water; Dansyl Compounds; Dermatitis, Irritant; Detergents; Erythema; Fluorescence; Humans; Patch Tests; Polysorbates; Quaternary Ammonium Compounds; Reproducibility of Results; Skin; Skin Diseases; Soaps; Sodium Dodecyl Sulfate; Staining and Labeling; Surface-Active Agents

Although the induction of irritant dermatitis by surfactants has been extensively studied in recent years, our understanding of the repair phase of irritant dermatitis is limited.. We investigated qualitative and quantitative differences in surfactant-induced irritant skin reactions from short-term exposure to three structurally different surfactants.. Sodium lauryl sulfate (SLS), dodecyl trimethyl ammonium bromide (DTAB), and potassium soap were the model irritants. Surfactant solutions (0.5%) were applied for 24 hours to the volar aspect of the forearm of 11 volunteers. Irritant reactions were assessed until complete healing was indicated by visual assessment and by various aspects of skin function, that is, transepidermal water loss (TEWL), erythema (skin color reflectance), and stratum that is, transepidermal water loss (TEWL), erythema (skin color reflectance), and stratum corneum hydration (electrical capacitance).. SLS and DTAB induced similar degrees of erythema, whereas SLS induced significantly higher TEWL increase. Although both erythema and TEWL were highest 1 hour after exposure to surfactants, skin dryness was a symptom with delayed onset, justifying the long observation period in this study. Minimum hydration values were measured as late as 7 days after surfactant exposure. Dryness was significantly more pronounced in areas exposed to SLS than in areas exposed to DTAB. Complete repair of the irritant reaction induced by either SLS or DTAB was achieved 17 days after surfactant exposure. Stratum corneum hydration was the last feature to return to baseline values. Potassium soap did not significantly influence any skin function.. We emphasize the importance of extended periods needed before a patient with irritant contact dermatitis can be reexposed to irritant substances. The evaluation of the irritation potential of diverse surfactants depended significantly on the feature (erythema vs hydration and TEWL) measured.

Topics: Adult; Dermatitis, Irritant; Detergents; Double-Blind Method; Erythema; Galvanic Skin Response; Humans; Lipids; Middle Aged; Quaternary Ammonium Compounds; Skin; Skin Physiological Phenomena; Soaps; Sodium Dodecyl Sulfate; Surface-Active Agents; Time Factors; Water Loss, Insensible; Wound Healing

The interaction (adsorption process) of commercial ionic surfactants with non-functionalized and functionalized carbon nanotubes (CNTs) has been studied by potentiometric measurements based on the use of ion-selective electrodes. The goal of this work was to investigate the role of the CNTs' charge and structure in the CNT/surfactant interactions. Non-functionalized single- (SWCNT) and multi-walled carbon nanotubes (MWCNT), and amine functionalized SWCNT were used. The influence of the surfactant architecture on the CNT/surfactant interactions was also studied. Surfactants with different charge and hydrophobic tail length (sodium dodecyl sulfate (SDS), octyltrimethyl ammonium bromide (OTAB), dodecyltrimethyl ammonium bromide (DoTAB) and hexadecyltrimethyl ammonium bromide (CTAB)) were studied. According to the results, the adsorption process shows a cooperative character, with the hydrophobic interaction contribution playing a key role. This is made evident by the correlation between the free surfactant concentration (at a fixed [CNT]) and the critical micellar concentration,

Topics: Adsorption; Cetrimonium; Electrodes; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Ion-Selective Electrodes; Ions; Light; Micelles; Microscopy, Electron, Transmission; Nanotubes, Carbon; Physical Phenomena; Potentiometry; Pulmonary Surfactants; Quaternary Ammonium Compounds; Scattering, Radiation; Sodium Dodecyl Sulfate; Surface-Active Agents; Water Pollutants, Chemical

Foam separation can selectively remove a target substance from a solution via adsorption of the substance with the surfactant at the surface of the bubble. A cationic dye, methylene blue, and an anionic dye, Fast Green FCF, were prepared as substances to be removed via foam separation. Anionic (sodium dodecyl sulfate, SDS), cationic (dodecyltrimethylammonium chloride, DTAC), and amphoteric (3-(dodecyldimethylammonio)propane-1-sulfonate, SB-12) surfactants were used in the foam separation process. The effectiveness of the surfactants for removing the cationic methylene blue increased as follows: DTAC < SB-12 < SDS. On the other hand, the effectiveness of the surfactants for removing the anionic Fast Green FCF was in the opposite order. The dyes were effectively adsorbed by the foams via electrostatic interactions between the oppositely charged surfactant and the dye molecules. Since amphoteric surfactants have both anionic and cationic charges in a molecule, they could effectively remove both dyes in the foam separation process. Therefore, it was found that the amphoteric surfactant was highly versatile. Analysis of the kinetics of the removal rate showed that the aqueous solutions of monomers could remove the dyes more effectively than micellar solutions in foam separation.

Topics: Adsorption; Amino Acid Transport Systems, Basic; Anions; Coloring Agents; Lissamine Green Dyes; Methylene Blue; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Static Electricity; Surface-Active Agents

Foam separation promotes the removal of dissolved materials from solutions by adsorbing the molecules onto a surfactant. The zwitterion of rhodamine B was removed by using both anionic (sodium dodecyl sulfate: SDS) and cationic (dodecyltrimethylammonium chloride: DTAC) surfactants through foam separation. However, rhodamine B could not be removed from a strongly acidic DTAC solution (pH 2), because the molecular form changes from the zwitterion to cation. Moreover, the cationic dye of rhodamine 6G could not be removed from the DTAC solution. Therefore, these results demonstrate that the electrostatic interaction between a surfactant and target ion is an important factor in foam separation.

Topics: Adsorption; Cations; Hydrogen-Ion Concentration; Ions; Quaternary Ammonium Compounds; Rhodamines; Sodium Dodecyl Sulfate; Solutions; Static Electricity; Surface-Active Agents

Ion pair amphiphile (IPA), a molecular complex composed of a pair of cationic and anionic amphiphiles, is an inexpensive phospholipid substitute to fabricate vesicles with various pharmaceutical applications. Modulating the physicochemical and permeation properties of IPA vesicles are important for carrier designs. Here, we applied molecular dynamics simulations to examine the cholesterol effects on the structures, mechanics, and water permittivity of hexadecyltrimethylammonium-dodecylsulfate (HTMA-DS) and dodecyltrimethylammonium- hexadecylsulfate (DTMA-HS) IPA bilayers. Structural and mechanical analyses indicate that both IPA systems are in gel phase at 298 K. Adding cholesterol induces alkyl chain ordering around the rigid sterol ring and increases the cavity density within the hydrophilic region of both IPA bilayers. Furthermore, the enhanced alkyl chain ordering and the membrane deformation energy induced by cholesterol increase the permeation free energy penalty. In contrast, cholesterol has minor effects on the water local diffusivities within IPA membranes. Overall, the cholesterol reduces the water permittivity of rigid IPA membranes due to the synergistic effects of increased alkyl chain ordering and enhanced membrane mechanical modulus. The results provide molecular insights into the effects of molecular packing and mechanical deformations on the water permittivity of biomimetic IPA membranes, which is critical for designing IPA vesicular carriers.

Topics: Biomimetic Materials; Cholesterol; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Molecular Dynamics Simulation; Permeability; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents; Water

Prion proteins (PrP) from different species have the ability to tightly bind Cu

Topics: Amino Acid Sequence; Amyloid; Animals; Chickens; Copper; Humans; Membranes, Artificial; Micelles; Models, Molecular; Peptide Fragments; Prion Proteins; Protein Binding; Protein Conformation, alpha-Helical; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents; Thermodynamics

This report examines the energetics of aggregate formation between hydroxypropyl methylcellulose (HPMC) and model ionic surfactants including sodium dodecyl sulfate (SDS) at pharmaceutically relevant concentrations using the isothermal titration calorimetry (ITC) technique and a novel treatment of calorimetric data that accounts for the various species formed. The influence of molecular weight of HPMC, temperature and ionic strength of solution on the aggregate formation process was explored. The interaction between SDS and HPMC was determined to be an endothermic process and initiated at a critical aggregation concentration (CAC). The SDS-HPMC interactions were observed to be cooperative in nature and dependent on temperature and ionic strength of the solution. Molecular weight of HPMC significantly shifted the interaction parameters between HPMC and SDS such that at the highest molecular weight (HPMC K-100M;>240kDa), although the general shape of the titration curve (enthalpogram) was observed to remain similar, the critical concentration parameters (CAC, polymer saturation concentration (C

Topics: Calorimetry; Chemistry, Pharmaceutical; Hydrophobic and Hydrophilic Interactions; Hypromellose Derivatives; Micelles; Molecular Weight; Osmolar Concentration; Polymers; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents; Temperature; Thermodynamics

Ion pair amphiphile (IPA), a molecular complex composed of a pair of cationic and anionic surfactants, has been proposed as a novel phospholipid substitute. Controlling the physical stability of IPA vesicles is important for its application developments such as cosmetic and drug deliveries. To investigate the effects of IPA alkyl chain combinations and the cholesterol additive on the structural and mechanical properties of IPA vesicular bilayers, we conducted a series of molecular dynamics studies on the hexadecyltrimethylammonium-dodecylsulfate (HTMA-DS) and dodecyltrimethylammonium-hexadecylsulfate (DTMA-HS) IPA bilayers with cholesterol. We found that both IPA bilayers are in the gel phase at 298 K, consistent with experimental observations. Compared with the HTMA-DS system, the DTMA-HS bilayer has more disordered alkyl chains in the hydrophobic region. When adding cholesterol, it induces alkyl chain ordering around its rigid sterol ring. Yet, cholesterol increases the molecular areas for all species and disturbs the molecular packing near the hydrophilic region and the bilayer core. Cholesterol also promotes the alkyl chain mismatch between the IPA moieties, especially for the DTMA-HS bilayer. The combined effects lead to non-monotonically enhancement of the membrane mechanical moduli for both IPA-cholesterol systems. Furthermore, cholesterol can form H-bonds with the alkylsulfate and thus enhance the contribution of alkylsulfate to the overall mechanical moduli. Combined results provide valuable molecular insights into the roles of each IPA component and the cholesterol on modulating the IPA bilayer properties.

Topics: Cetrimonium; Cetrimonium Compounds; Cholesterol; Hydrogen Bonding; Lipid Bilayers; Mechanical Phenomena; Molecular Dynamics Simulation; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents

In order to elucidate an electroacoustic phenomenon of mixed micelles in an aqueous solution, we measured the colloid vibration current (CVI) in aqueous solutions of binary surfactant mixtures. Based on the thermodynamic treatment of critical micelle concentration (cmc) values determined by conductivity measurements, it was expected that dodecyltrimethylammonium bromide (DTAB) and dodecyltrimethylammonium chloride (DTAC) molecules would mix ideally in the micelle. However, the micelle composition as evaluated from the CVI measurement, based on the linear dependence of the CVI value on the micelle composition, differed from the aforementioned ideality. Considering these observations, we concluded that the CVI measurement was more sensitive to the counterion distribution near the micelle surface, whereas the thermodynamically determined micelle composition included the counterions more loosely bound in the diffuse double layer due to the electroneutrality condition included in its assumption. On the other hand, the phase diagram illustrating micelle formation in the lithium dodecyl sulfate (LiDS) - lithium perfluorooctane sulfonate (LiFOS) mixture system showed a heteroazeotropic point arising from the stronger interactions between homologous surfactants than between heterologous ones. Although the concentration dependence of CVI values was expected to drastically change at a heteroazeotropic point due to the enormous variation in the density of the micelle core, the results showed a monotonous change, which suggests that the density of the micelle core varies continuously. By taking the partial molar volume of fluorocarbon compounds in the hydrocarbon compounds into account, the density of the micelle core was affected by the size of the micelle as well as its constituents.

Topics: Alkanesulfonic Acids; Anions; Colloids; Electric Conductivity; Fluorocarbons; Hydrophobic and Hydrophilic Interactions; Micelles; Molecular Structure; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents; Thermodynamics; Ultrasonic Waves; Water

Recent research has reported many attractive benefits from short peptide amphiphiles. A practical route for them to enter the real world of applications is through formulation with conventional surfactants. This study reports the co-adsorption of the surfactant-like peptide, V6K, with conventional anionic and cationic surfactants at the solid/water interface. The time-dependant adsorption behaviour was examined using spectroscopic ellipsometry whilst adsorbed layer composition and structural distribution of the components were investigated by neutron reflection with the use of hydrogen/deuterium labelling of the surfactant molecules. Both binary (surfactant/peptide mixtures) and sequential (peptide followed by surfactant) adsorption have been studied. It was found that at the hydrophilic SiO2/water interface, the peptide was able to form a stable, flat, defected bilayer structure however both the structure and adsorbed amount were highly dependent on the initial peptide concentration. This consequently affected surfactant adsorption. In the presence of a pre-adsorbed peptide layer anionic sodium dodecyl sulfate (SDS) could readily co-adsorb at the interface; however, cationic dodecyl trimethyl ammonium bromide (C12TAB) could not co-adsorb due to the same charge character. However on a trimethoxy octyl silane (C8) coated hydrophobic surface, V6K formed a monolayer, and subsequent exposure to cationic and anionic surfactants both led to some co-adsorption at the interface. In binary surfactant/peptide mixtures, it was found that adsorption was dependent on the molar ratio of the surfactant and peptide. For SDS mixtures below molar unity and concentrations below CMC for C12TAB, V6K was able to dominate adsorption at the interface. Above molar unity, no adsorption was detected for SDS/V6K mixtures. In contrast, C12TAB gradually replaced the peptide and became dominant at the interface. These results thus elucidate the adsorption behaviour of V6K, which was found to dominate interfacial adsorption but its exact adsorbed amount and distribution were affected by interfacial hydrophobicity and interactions with conventional surfactants.

Topics: Adsorption; Kinetics; Peptides; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents; Water

Small-angle neutron scattering and dynamic light scattering studies have been carried out to examine the interaction of bovine serum albumin (BSA) protein with different surfactants under varying solution conditions. We show that the interaction of anionic BSA protein (pH7) with surfactant and the resultant structure are strongly modified by the charge head group of the surfactant, ionic strength of the solution, and mixed surfactants. The protein-surfactant interaction is maximum when two components are oppositely charged, followed by components being similarly charged through the site-specific binding, and no interaction in the case of a nonionic surfactant. This interaction of protein with ionic surfactants is characterized by the fractal structure representing a bead-necklace structure of micellelike clusters adsorbed along the unfolded protein chain. The interaction is enhanced with ionic strength only in the case of site-specific binding of an anionic surfactant with an anionic protein, whereas it is almost unchanged for other complexes of cationic and nonionic surfactants with anionic proteins. Interestingly, the interaction of BSA protein with ionic surfactants is significantly suppressed in the presence of nonionic surfactant. These results with mixed surfactants thus can be used to fold back the unfolded protein as well as to prevent surfactant-induced protein unfolding. For different solution conditions, the results are interpreted in terms of a change in fractal dimension, the overall size of the protein-surfactant complex, and the number of micelles attached to the protein. The interplay of electrostatic and hydrophobic interactions is found to govern the resultant structure of complexes.

Topics: Animals; Cattle; Dynamic Light Scattering; Fractals; Hydrophobic and Hydrophilic Interactions; Ions; Micelles; Models, Chemical; Neutron Diffraction; Polyethylene Glycols; Protein Folding; Quaternary Ammonium Compounds; Scattering, Small Angle; Serum Albumin, Bovine; Sodium Dodecyl Sulfate; Static Electricity; Surface-Active Agents

The central reason behind pathogenesis of various neurological disorders is usually attributed to the accumulation of aggregated proteins particularly in fibrillar morphology in vivo. One of the plausible remedial treatments for such disorders may be to identify molecules which are capable of either preventing formation of fibrils or disintegrating formed fibrils. The effect of cationic surfactants cetyl trimethylammonium bromide (CTAB), dodecyl trimethylammonium bromide (DTAB) and the anionic surfactant sodium dodecyl sulfate (SDS) in vitro toward mature HSA fibrils has been investigated. The process has been monitored using ThT fluorescence, FTIR, circular dichroism, fluorescence microscopy and HRTEM. It was observed that the micelles of cationic surfactants were able to effectively disrupt the HSA fibrils, among which CTAB was found to be the most potent.

Topics: Amyloid; Cetrimonium; Cetrimonium Compounds; Circular Dichroism; Humans; Micelles; Molecular Mimicry; Quaternary Ammonium Compounds; Serum Albumin; Sodium Dodecyl Sulfate; Solutions; Spectroscopy, Fourier Transform Infrared; Surface-Active Agents

Isoforms A (LGB-A) and B (LGB-B) of bovine lactoglobulin, the milk protein, differ in positions 64 (D↔G) and 118 (V↔A). Interactions of LGB-A and LGB-B with sodium dodecyl sulfate (SDS), dodecyltrimethylammonium chloride (DTAC) and lauric acid (LA), 12-carbon ligands possessing differently charged polar groups, were investigated using isothermal titration calorimetry and X-ray crystallography, to study the proton linkage phenomenon and to distinguish between effects related to different isoforms and different ligand properties. The determined values of ΔS and ΔH revealed that for all ligands, binding is entropically driven. The contribution from enthalpy change is lower and shows strong dependence on type of buffer that indicates proton release from the protein varying with protein isoform and ligand type and involvement of LA and Asp64 (in isoform A) in this process. The ligand affinities for both isoforms were arranged in the same order, DTAC < LA < SDS, and were systematically lower for variant B. The entropy change of the complexation process was always higher for isoform A, but these values were compensated by changes in enthalpy, resulting in almost identical ΔG for complexes of both isoforms. The determined crystal structures showed that substitution in positions 64 and 118 did not influence the overall structure of LGB complexes. The chemical character of the ligand polar group did not affect the position of its aliphatic chain in protein β-barrel, indicating a major role of hydrophobic interactions in ligand binding that prevailed even with the repulsion between positively charged DTAC and lysine residues located at binding site entrance.

Topics: Animals; Calorimetry; Carbon; Cattle; Crystallography, X-Ray; Lactoglobulins; Lauric Acids; Ligands; Protein Binding; Protein Isoforms; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Thermodynamics

The formation of a hybrid-nanocomposite using α-glucosyl stevia (Stevia-G) and surfactant was explored to improve the dissolution of flurbiprofen (FP). As reported previously, the dissolution amount of FP was enhanced in the presence of Stevia-G, induced by the formation of an FP and Stevia-G-associated nanostructure. When a small amount of sodium dodecyl sulfate (SDS) was present with Stevia-G, the amount of dissolved FP was extremely enhanced. This dissolution-enhancement effect was also observed with the cationic surfactant of dodecyl trimethyl ammonium bromide, but not with the non-ionic surfactant of n-octyl-β-D-maltopyranoside. To investigate the dissolution-enhancement effect of Stevia-G/SDS mixture, the pyrene I(1)/I(3) ratio was plotted versus the Stevia-G concentration. The pyrene I(1)/I(3) ratio of Stevia-G/SDS mixture had a sigmoidal curve at lower Stevia-G concentrations compared to the Stevia-G solution alone. These results indicate that the Stevia-G/SDS mixture provides a hydrophobic core around pyrene molecules at lower Stevia-G concentrations, leading to nanocomposite formation between Stevia-G and SDS. The nanocomposite of Stevia-G/SDS showed no cytotoxicity to Caco-2 cells at a mixture of 0.1% SDS and 1% Stevia-G solution, whereas 0.1% SDS solution showed high toxicity. These results suggest that the nanocomposite formation of Stevia-G/SDS may be useful way to enhance the dissolution of poorly water-soluble drugs without special treatment.

Topics: Caco-2 Cells; Flurbiprofen; Humans; Hydrophobic and Hydrophilic Interactions; Maltose; Micelles; Nanocomposites; Pyrenes; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Solubility; Stevia; Surface-Active Agents; Thermodynamics; Water

The chain-length compatibility of mixed anionic-cationic surfactants was investigated for the extraction of organophosphorus pesticides (OPPs). Cationic surfactants with different chain lengths (n = 12 and 16) were mixed with sodium dodecyl sulfate (SDS; n = 12) for the mixed anionic-cationic surfactants-based extraction. Six OPPs were studied including azinphos-methyl, parathion-methyl, fenitrothion, diazinon, chlorpyrifos, and prothiophos. Reversed-phase high-performance liquid chromatography was used for the determination of the studied OPPs. The extraction was performed using mixtures of SDS and cationic surfactants including dodecyltrimethyl ammonium bromide or dodecyltrimethylammonium bromide (DTAB; n = 12) and cetyltrimethyl ammonium bromide or cetyltrimethyl ammonium bromide (CTAB; n = 16). The parameters affecting the extraction efficiencies of two extraction systems were studied and discussed. The optimum condition for SDS-DTAB was 15 mmol L(-1) SDS and 1 mmol L(-1) DTAB in the presence of 15% (w/v) sodium chloride (NaCl). Meanwhile, the condition for SDS-CTAB was 10 mmol L(-1) SDS and 1.0 mmol L(-1) CTAB with 10% (w/v) NaCl. Under the optimum conditions, the extraction efficiency of SDS-DTAB (66-85%) was slightly higher than that of SDS-CTAB (61-82%). In addition, the SDS-DTAB system also gave greater enrichment factor than SDS-CTAB for all the studied OPPs. This result may be due to the compatibility of chain length between SDS and DTAB. The extraction using SDS-DTAB was successfully applied to determine OPPs in fruit samples (i.e., pomelo, apple, and pineapple). No contamination by the studied OPPs in samples was observed. Good accuracy with recoveries ranging from 77 to 105% was obtained. Low limits of detection were in the range of 0.003-0.01 mg kg(-1) which are below the MRLs established by EU-MRLs for the OPPs residues in fruit samples.

Topics: Cetrimonium; Cetrimonium Compounds; Chemical Fractionation; Chromatography, Reverse-Phase; Food Contamination; Fruit; Organophosphorus Compounds; Pesticides; Quaternary Ammonium Compounds; Sensitivity and Specificity; Sodium Dodecyl Sulfate; Surface-Active Agents

Two positively charged basic amino acids, arginine and lysine, are mostly exposed to protein surface, and play important roles in protein stability by forming electrostatic interactions. In particular, the guanidinium group of arginine allows interactions in three possible directions, which enables arginine to form a larger number of electrostatic interactions compared to lysine. The higher pKa of the basic residue in arginine may also generate more stable ionic interactions than lysine. This paper reports an investigation whether the advantageous properties of arginine over lysine can be utilized to enhance protein stability. A variant of green fluorescent protein (GFP) was created by mutating the maximum possible number of lysine residues on the surface to arginines while retaining the activity. When the stability of the variant was examined under a range of denaturing conditions, the variant was relatively more stable compared to control GFP in the presence of chemical denaturants such as urea, alkaline pH and ionic detergents, but the thermal stability of the protein was not changed. The modeled structure of the variant indicated putative new salt bridges and hydrogen bond interactions that help improve the rigidity of the protein against different chemical denaturants. Structural analyses of the electrostatic interactions also confirmed that the geometric properties of the guanidinium group in arginine had such effects. On the other hand, the altered electrostatic interactions induced by the mutagenesis of surface lysines to arginines adversely affected protein folding, which decreased the productivity of the functional form of the variant. These results suggest that the surface lysine mutagenesis to arginines can be considered one of the parameters in protein stability engineering.

Topics: Amino Acid Motifs; Amino Acid Substitution; Arginine; Detergents; Green Fluorescent Proteins; Half-Life; Hydrogen Bonding; Hydrogen-Ion Concentration; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Protein Denaturation; Protein Stability; Protein Structure, Tertiary; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Surface Properties; Urea

The surface tension lowering abilities of insoluble steroids, progesterone and testosterone, were examined at the dodecane/water interface in the presence and absence of surfactants, sodium dodecyl sulfate, dodecyltrimethylammonium bromide, and dodecyl maltoside. In the absence of these surfactants, the steroids significantly lowered the interfacial tension while exhibiting no activity at the air/water and air/dodecane surfaces. Further, in mixtures of surfactants and steroids, significant enhancement of interfacial tension lowering was observed. At a sufficiently high concentration of surfactant, no further lowering of tension was observed in the presence of the steroids. The synergistic effects on interfacial tension of steroids and surfactants were characterized by the free energy of transfer to the interface of each solute based on a two-dimensional solution equation of state. Assuming no significant interaction between the steroids and the surfactants in the interface, predictions of interfacial tensions were made based on the calculated free energies of transfer and interfacial area occupied. Good agreement was found between the predicted values and experimental values for interfacial tension. The results of these studies show that progesterone and testosterone, molecules not normally thought of as surface active, exhibit significant interfacial activity and can successfully compete with surfactants for the dodecane/water interface.

Topics: Adsorption; Air; Alkanes; Glucosides; Hydrophobic and Hydrophilic Interactions; Kinetics; Pharmaceutical Solutions; Progesterone; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Solutions; Surface Tension; Surface-Active Agents; Testosterone; Thermodynamics; Water

We investigated the effect of two commonly studied surfactants, sodium dodecyl sulfate (SDS) and dodecyl trimethylammonium bromide (C(12)TAB), on skin barrier properties. Using skin conductivity, FT-IR of stratum corneum samples, and penetration of radiolabelled SDS, we determined that addition of C(12)TAB lowers the ability of SDS to perturb skin's barrier properties. Ultrafiltration experiments revealed that addition of C(12)TAB serves to decrease the concentration of monomers and sub-micellar aggregates. None of the measured skin properties including enhancement of skin conductivity, perturbation of lipid structure and skin concentration of SDS correlated with the total SDS concentration in the donor compartment (i.e., the total SDS concentration). However, all these parameters correlated well against the concentration of monomers and sub-micellar aggregates. These findings provide the evidence of the importance of monomer and sub-micellar components in altering skin barrier properties.

Topics: Animals; Biomedical Engineering; Electric Conductivity; In Vitro Techniques; Permeability; Quaternary Ammonium Compounds; Skin; Sodium Dodecyl Sulfate; Spectroscopy, Fourier Transform Infrared; Surface-Active Agents; Swine

The aggregation behavior of catanionics formed by the mixture of cationic geminis derived from dodecyltrimethylammonium chloride (DTAC) and anionic sodium dodecylsulfate (SDS) was studied by means of phase studies and comprehensive small-angle neutron scattering (SANS) experiments at 25 °C and 50 mM overall concentration. The results are compared to those for the previously studied SDS + DTAC system. Various gemini spacers of different natures and geometries were used, but all of them had similar lengths: an ethoxy bridge, a double bond, and an aromatic ring binding the two DTACs in three different substitutions (ortho, meta, and para). SANS and SAXS data analysis indicates that the spacer has no large effect on the spheroidal micelles of pure surfactants formed at low concentration in water; however, specific effects appear with the addition of electrolytes. Microstructures formed in the catanionic mixtures are rather strongly dependent on the nature of the spacer. The most important finding is that for the hydrophilic, flexible ethoxy bridge, monodisperse vesicles with a fixed anionic/cationic charge ratio (depending only on the surfactant in excess) are formed. Furthermore, the composition of these vesicles shows that strongly charged aggregates are formed. This study therefore provides new opportunities for developing tailor-made gemini surfactants that allow for the fine tuning of catanionic structures.

Topics: Anions; Calcitriol; Cations; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents

The dynamic dilatational surface elasticity of mixed solutions of globular proteins (β-lactoglobulin (BLG) and bovine serum albumin (BSA)) with cationic (dodecyltrimethylammonium bromide (DTAB)) and anionic (sodium dodecyl sulfate (SDS)) surfactants was measured as a function of the surfactant concentration and surface age. If the cationic surfactant concentration exceeds a certain critical value, the kinetic dependencies of the dynamic surface elasticity of BLG/DTAB and BSA/DTAB solutions become nonmonotonous and resemble those of mixed solutions of proteins with guanidine hydrochloride. This result indicates not only the destruction of the protein tertiary structure in the surface layer of mixed solution but also a strong perturbation of the secondary structure. The corresponding kinetic dependencies for protein solutions with added anionic surfactants are always monotonous, thereby revealing a different mechanism of the adsorption layer formation. One can assume that the secondary structure is destroyed to a lesser extent in the latter case and hinders the formation of loops and tails at the interface. The increase of the solution's ionic strength by the addition of sodium chloride results in stronger changes of the protein conformations in the surface layer and the appearance of a local maximum in the kinetic dependencies of the dynamic surface elasticity in a relatively narrow range of SDS concentration.

Topics: Adsorption; Air; Animals; Cattle; Elasticity; Lactoglobulins; Osmolar Concentration; Protein Structure, Secondary; Quaternary Ammonium Compounds; Rheology; Serum Albumin, Bovine; Sodium Chloride; Sodium Dodecyl Sulfate; Surface Properties; Surface-Active Agents; Water

Femtosecond fluorescence upconversion experiments were performed on the naturally occurring medicinal pigment, curcumin, in anionic, cationic, and neutral micelles. In our studies, the micelles are composed of sodium dodecyl sulfate (SDS), dodecyl trimethyl ammonium bromide (DTAB), and triton X-100 (TX-100). We demonstrate that the excited-state kinetics of curcumin in micelles have a fast (3-8 ps) and slow (50-80 ps) component. While deuteration of curcumin has a negligible effect on the fast component, the slow component exhibits a pronounced isotope effect of approximately 1.6, indicating that micelle-captured curcumin undergoes excited-state intramolecular hydrogen atom transfer. Studies of solvation dynamics of curcumin in a 10 ps time window reveal a fast component (< or = 300 fs) followed by a 8, 6, and 3 ps component in the solvation correlation function for the TX-100, DTAB, and SDS micelles, respectively.

Topics: Curcumin; Hydrogen; Micelles; Octoxynol; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Surface-Active Agents; Time Factors

In this work, we studied the effect of compressed CO2 on the stability of vesicles formed in a dodecyltrimethylammonium bromide (DTAB)/sodium dodecyl sulfate (SDS) mixed surfactant system by combination of phase behavior and turbidity study, and UV-vis and fluorescence techniques. It was discovered that compressed CO2 could enhance the stability of vesicles significantly. This new and effective method to stabilize vesicles has some unique advantages over conventional methods. For example, the size and stability of the vesicles can be easily controlled by CO2 pressure; the method is greener because CO2 is a green reagent and it can be released completely after depressurization, which simplifies postseparation processes in applications. The main reason for CO2 to stabilize the vesicles is that CO2 molecules can insert into the hydrophobic bilayer region to enhance the rigidity of the vesicle film and reduce the size of the vesicles, which is different from that of conventional cosolvents (e.g., alcohols) used to stabilize vesicles. On the basis of this discovery, we developed a method to prepare hollow silica spheres using tetraethoxysilane as the precursor and CO2-stabilized vesicles as the template, in which CO2 acts as both the stabilizer of the vesicular template and the catalyst for the hydrolysis reaction of the precursor, and other cosolvents and catalysts are not required. Besides, the size of the silica hollow spheres prepared can be controlled by the pressure of CO2.

Topics: Carbon Dioxide; Nephelometry and Turbidimetry; Quaternary Ammonium Compounds; Silicon Dioxide; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

Proton nuclear magnetic resonance relaxation times were measured for the protons of micelles formed by the detergents sodium dodecyl sulfate, dodecyltrimethyl ammonium bromide, and polyethylene glycol sorbitan monolaureate in the presence of ferriprotoporphyrin IX and the antimalarial drugs chloroquine, 7-chloro-4-quinolyl 4-N,N-diethylaminobutyl sulfide, and primaquine. Diffusion coefficients were extracted from pulsed gradient NMR experiments to evaluate the degree of association of these drugs with the detergent micelles. Results indicate that at low or neutral pH when the quinolyl N is protonated, chloroquine does not associate with neutral or cationic detergent micelles. For this reason, chloroquine's interaction with heme perturbs the partitioning of heme between the aqueous medium and detergent micelles.

Topics: Antimalarials; Detergents; Heme; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Micelles; Molecular Structure; Primaquine; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate

This paper reports that the acetylation of lysine epsilon-NH3(+) groups of alpha-amylase--one of the most important hydrolytic enzymes used in industry--produces highly negatively charged variants that are enzymatically active, thermostable, and more resistant than the wild-type enzyme to irreversible inactivation on exposure to denaturing conditions (e.g., 1 h at 90 degrees C in solutions containing 100-mM sodium dodecyl sulfate). Acetylation also protected the enzyme against irreversible inactivation by the neutral surfactant TRITON X-100 (polyethylene glycol p-(1,1,3,3-tetramethylbutyl)phenyl ether), but not by the cationic surfactant, dodecyltrimethylammonium bromide (DTAB). The increased resistance of acetylated alpha-amylase toward inactivation is attributed to the increased net negative charge of alpha-amylase that resulted from the acetylation of lysine ammonium groups (lysine epsilon-NH3(+) --> epsilon-NHCOCH3). Increases in the net negative charge of proteins can decrease the rate of unfolding by anionic surfactants, and can also decrease the rate of protein aggregation. The acetylation of lysine represents a simple, inexpensive method for stabilizing bacterial alpha-amylase against irreversible inactivation in the presence of the anionic and neutral surfactants that are commonly used in industrial applications.

Topics: Acetylation; alpha-Amylases; Bacillus; Bacterial Proteins; Calorimetry, Differential Scanning; Circular Dichroism; Electrophoresis, Capillary; Enzyme Stability; Lysine; Octoxynol; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Spectrometry, Mass, Electrospray Ionization

Effects of sodium dodecyl sulfate, dodecyltrimethylammonium bromide, sodium chloride, sodium sulfate, methanol and ethanol, on the structure and activity of adenosine deaminase (ADA) were investigated by UV-Vis, circular dichroism spectrophotometry and molecular dynamics (MDs) studies. Relative activity, experimental and computational helix content, total accessible surface area (ASA) and exposed charged surface area (ECSA) were obtained. The relative activity of ADA in the absence and the presence of denaturants were compared with structural results. It was shown that an increase in the surface area and a decrease in the amount of helicity are associated with a decrease in the activity of ADA.

Topics: Adenosine Deaminase; Circular Dichroism; Ethanol; Kinetics; Methanol; Quantitative Structure-Activity Relationship; Quaternary Ammonium Compounds; Sodium Chloride; Sodium Dodecyl Sulfate; Solvents; Spectrophotometry, Ultraviolet; Sulfates; Surface-Active Agents

In this research, the effects of micellar systems on alkaline hydrolysis reactions of acetylsalicylic acid (ASA) and triflusal (TFL) were found to be dependant upon the surfactant charge within the micelle. In cationic micelles, there is a catalytic effect at low concentrations of surfactant. However, this reaction is inhibited at higher surfactant concentrations. In anionic micelles, a catalytic effect occurs, while in zwitterionic and non-ionic micelles there is an inhibitory effect. Such reactions are attributable to changes in reactants on the micellar surface, or to the fact that both reactants are found in different microenvironments. The pseudophase (PS) and ion-exchange (PPIE) models were found to be consistent with the experimental result. Furthermore, the association constants for both drugs could be determined together with micellar rate constants in heterogeneous media.

Topics: Algorithms; Alkalies; Aspirin; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Platelet Aggregation Inhibitors; Polyethylene Glycols; Quaternary Ammonium Compounds; Salicylates; Salicylic Acid; Sodium Dodecyl Sulfate; Sodium Hydroxide; Spectrophotometry, Ultraviolet; Static Electricity; Surface-Active Agents; Water

Novispirin G-10 is an 18-residue designed cationic peptide derived from the N-terminal part of an antimicrobial peptide from sheep. This derivative is more specific for bacteria than the parent peptide. We have analyzed Novispirin's interactions with various amphipathic molecules and find that a remarkably wide variety of conditions induce alpha-helical structure. Optimal structure induction by lipids occurs when the vesicles contain 40-80% anionic lipid, while pure anionic lipid vesicles induce aggregation. SDS also forms aggregates with Novispirin at submicellar concentrations but induces alpha-helical structures above the cmc. Both types of aggregates contain significant amounts of beta-sheet structure, highlighting the peptide's structural versatility. The cationic detergent LTAC has a relatively strong affinity for the cationic peptide despite the peptide's net positive charge of +7 at physiological pH and total lack of negatively charged side chains. Zwitterionic and nonionic detergents induce alpha-helical structures at several hundred millimolar detergent. We have solved the peptide structure in SDS and LTAB by NMR and find subtle differences compared to the structure in TFE, which we ascribe to the interaction with an amphiphilic environment. Novispirin is largely buried in the SDS-micelle, whereas it does not enter the LTAC-micelle but merely forms a dynamic equilibrium between surface-bound and nonbound Novispirin. Thus, electrostatic repulsion can be overruled by relatively high-detergent concentrations or by deprotonating a single critical side chain, despite the fact that Novispirin's ability to bind to amphiphiles and form alpha-helical structure is sensitive to the electrostatics of the amphiphilic environment. This emphasizes the versatility of cationic antimicrobial peptides' interactions with amphiphiles.

Topics: Antimicrobial Cationic Peptides; Circular Dichroism; Detergents; Deuterium Exchange Measurement; Glucosides; Lipids; Lipopolysaccharides; Liposomes; Micelles; Nuclear Magnetic Resonance, Biomolecular; Polyethylene Glycols; Protein Binding; Protein Structure, Tertiary; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Static Electricity; Trifluoroethanol

The synthesis of gold nanoparticles has been carried out in aqueous phase in the presence of both ionic surfactants (i.e., sodium dodecylsulfate (SDS) and dodecyltrimethylammonium bromide (DTAB)) and poly(amidoamine) dendrimers (PAMAM). It has been observed that the fluoroderivative of 2G PAMAM (2D) acts as reducing agent in reducing Au(lll) to Au(0) leading to the formation of fine gold nanoparticles. This process has been further evaluated in the presence of fixed amounts of both SDS and DTAB in their respective pre and post micellar concentration regions. The presence of SDS leads to the appearance of clear ordered morphologies such as triangular, hexagonal, spherical, and rod shaped, while the presence of DTAB does not show this effect. The formation of nanoparticles in triangular morphologies is more significant in the premicellar concentration range of SDS whereas hexagonal morphologies in the post micellar concentration range. On the contrary, increase in the DTAB concentration from pre to post micellar range only reduces the size of gold nanoparticles without the appearance of any ordered morphology. The formation of ordered gold nanoparticles in the presence of SDS has been further attributed to the significant SDS-dendrimer interactions and an appropriate mechanism has been proposed to justify the results.

Topics: Complex Mixtures; Crystallization; Dendrimers; Gold; Molecular Conformation; Nanostructures; Particle Size; Polyamines; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate

Mixed micelles of the phospholipid 1,2-diheptanoyl-sn-glycero-3-phosphocholine (DHPC) with sodium dodecyl sulfate (SDS) or dodecyltrimethylammonium bromide (DTAB) in aqueous solutions and the effects of interactions between the components were studied by fluorescence and NMR measurements. The regular solution theory (RST) was applied to analyze the experimental critical micelle concentration values determined from the fluorescence spectra of pyrene in the mixed micelles. Negative values for the interaction parameter (beta12) were obtained for both DHPC + SDS and DHPC + DTAB mixtures, with the value being more negative in the former case. The negative beta12 values for the two systems imply that the interaction between the phospholipid and the two ionic surfactants is attractive in nature, being more intense in the case of DHPC + SDS. The interaction parameter, beta12, varies with composition of the mixtures indicating changes in packing. The proton NMR shifts are quite different for the two systems and also vary with composition. An interpretation of these experimentally determined chemical shifts in terms of the degree of compactness attributed to electrostatic and steric interactions in the mixed micelle supports the conclusions derived from the fluorescence cmc experiments.

Topics: Micelles; Phosphatidylcholines; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents

Solvation dynamics of the fluorescence probe, coumarin 102, in anionic surfactant, sodium alkyl sulfate (C(n)H(2n+1)SO(4)Na; n = 8, 10, 12, and 14), and cationic surfactant, alkyltrimethylammonium bromide (C(n)H(2n+1)N(CH(3))(3)Br; n = 10, 12, 14, and 16), micelle solutions have been investigated by a picosecond streak camera system. The solvation dynamics in the time range of 10(-10)-10(-8) s is characterized by a biexponential function. The faster solvation time constants are about 110-160 ps for both anionic and cationic micelle solutions, and the slower solvation time constants for sodium alkyl sulfate and alkyltrimethylammonium bromide micelle solutions are about 1.2-2.6 ns and 450-740 ps, respectively. Both the faster and the slower solvation times become slower with longer alkyl chain surfactant micelles. The alkyl-chain-length dependence of the solvation dynamics in both sodium alkyl sulfate and alkyltrimethylammonium bromide micelles can be attributed to the variation of the micellar surface density of the polar headgroup by the change of the alkyl chain length. The slower solvation time constants of sodium alkyl sulfate micelle solutions are about 3.5 times slower than those of alkyltrimethylammonium bromide micelle solutions for the same alkyl-chain-length surfactants. The interaction energies of the geometry optimized mimic clusters (H(2)O-C(2)H(5)SO(4)(-) and H(2)O-C(2)H(5)N(CH(3))(3)(+)) have been estimated by the density functional theory calculations to understand the interaction strengths between water and alkyl sulfate and alkyltrimethylammonium headgroups. The difference of the slower solvation time constants between sodium alkyl sulfate and alkyltrimethylammonium bromide micelle solutions arises likely from their different specific interactions.

Topics: Anions; Cations; Micelles; Models, Chemical; Monosaccharides; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Surface Properties; Surface-Active Agents; Water

Mixed micelles of l,2-diheptanoyl-sn-grycero-3-phosphocholine (DHPC) with ionic detergents were prepared to develop well characterized substrates for the study of lipolytic enzymes. The aggregates that formed on mixing DHPC with the anionic surfactant sodium dodecyl sulfate (SDS) and with the positively charged dodecyl trimethylammonium bromide (DTAB) were investigated using time-resolved fluorescence quenching (TRFQ) to determine the aggregation numbers and bimolecular collision rates, and electron spin resonance (ESR) to measure the hydration index and microviscosity of the micelles at the micelle-water interface. Mixed micelles between the phospholipid and each of the detergents formed in all compositions, yielding interfaces with varying charge, hydration, and microviscosity. Both series of micelles were found to be globular up to 0.7 mole fraction of DHPC, while the aggregation numbers varied within the same concentration range of the components less than 15%. Addition of the zwitterionic phospholipid component increased the degree of counterion dissociation as measured by the quenching of the fluorescence of pyrene by the bromide ions bound to DHPC/DTAB micelles, showing that at 0.6 mole fraction of DHPC 80% of the bromide ions are dissociated from the micelles. The interface water concentration decreased significantly on addition of DHPC to each detergent. For combined phospholipid and detergent concentration of 50 mM the interface water concentration decreased, as measured by ESR of the spin-probes, from 38.5 M/L of interface volume in SDS alone to 9 M/L when the phospholipid was present at 0.7 mole fraction. Similar addition of DHPC to DTAB decreased the interfacial water concentration from 27 M/L to 11 M/L. Determination of the physicochemical parameters of the phospholipid containing mixed micelles here presented are likely to provide important insight into the design of assay systems for kinetic studies of phospholipid metabolizing enzymes.

Topics: Complex Mixtures; Detergents; Micelles; Phase Transition; Phospholipid Ethers; Phospholipids; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Viscosity; Water

We investigate the competition between the associations of oppositely charged protein-surfactant complexes and oppositely charged surfactant complexes. In all systems examined, the most favorable complexation is the one between the two oppositely charged surfactant ions, despite the strong binding known, for example, dodecyl sulfate, DS-, to lysozyme. Thus, the phase behavior of the catanionic system is dominating the features observed also in the presence of protein. The phase behavior of the dilute protein-free dodecyltrimethylammonium chloride-sodium dodecyl sulfate-water system is presented and used as a basis for the discussion on the different solubilization mechanisms. Our results show that the mechanism for resolubilization of a protein-surfactant salt is fundamentally different when it is caused by addition of a second surfactant than when it is accomplished by an excess of the first surfactant. The competition between lysozyme and cationic amphiphiles as hosts for the anionic surfactants was studied experimentally and analyzed quantitatively. Aggregates with C12 cationic surfactants are clearly preferred by the anionic surfactants, while for C10 and particularly C8 a clear excess of cationic surfactant has to be added to completely dissolve the complex salt lysozyme-anionic surfactant.

Topics: Cations; Muramidase; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Solubility; Spectrophotometry, Ultraviolet; Surface Tension; Surface-Active Agents; Water

In beta(2)-microglobulin-related (Abeta2M) amyloidosis, partial unfolding of beta(2)-microglobulin (beta2-m) is believed to be prerequisite to its assembly into Abeta2M amyloid fibrils in vivo. Although low pH or 2,2,2-trifluoroethanol at a low concentration has been reported to induce partial unfolding of beta2-m and subsequent amyloid fibril formation in vitro, factors that induce them under near physiological conditions have not been determined. Using fluorescence spectroscopy with thioflavin T, circular dichroism spectroscopy, and electron microscopy, we here show that at low concentrations, sodium dodecyl sulfate (SDS) converts natively folded beta2-m monomers into partially folded, alpha-helix-containing conformers. Surprisingly, this results in the extension of Abeta2M amyloid fibrils at neutral pH, which could be explained basically by a first-order kinetic model. At low concentrations, SDS also stabilized the fibrils at neutral pH. These SDS effects were concentration-dependent and maximal at approximately 0.5 mM, around the critical micelle concentration of SDS (0.67 mM). As the concentration of SDS was increased above 1 mM, the alpha-helix content of beta2-m rose to approximately 10%, while the beta-sheet content decreased to approximately 20%, a change paralleled by a complete cessation of fibril extension and the destabilization of the fibrils. Detergents of other classes had no significant effect on the extension of fibrils. These findings are consistent with the hypothesis that in vivo, specific factors (e.g., phospholipids) that affect the conformation and stability of beta2-m and amyloid fibrils will have significant effects on the kinetics of Abeta2M fibril formation.

Topics: Amyloid; beta 2-Microglobulin; Circular Dichroism; Detergents; Dose-Response Relationship, Drug; Humans; Hydrogen-Ion Concentration; Micelles; Octoxynol; Polymers; Protein Conformation; Protein Folding; Quaternary Ammonium Compounds; Recombinant Proteins; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Surface-Active Agents

The micellar liquid chromatographic (MLC) separations of polycyclic aromatic hydrocarbons (PAHs) were optimized for three micellar systems, cetyltrimethylammonium chloride (CTAC), dodecyltrimethylammonium chloride (DTAC), and sodium dodecylsulfate (SDS), with 1-pentanol as the only organic additive. A difference in the separation was observed between CTAC and SDS/DTAC. Under each optimized separation conditions, CTAC-modified mobile phase provides the least desirable separation, which is attributed to its longer carbon tail (C16 vs. C12). In addition to 1-pentanol, the main organic additive, a second organic additive (3% 1-propanol) in the micelle-modified mobile phase was found to enhance the resolution of PAH chromatographic peaks. However, the extent of the enhancement varies for the different micellar systems, with the greatest resolution improvement seen for CTAC, and little effect for shorter-tail SDS and DTAC. This study shows the potential use of second organic additive (1-propanol), to the main nonpolar additive (1-pentanol), in facilitating the MLC separation of larger nonpolar compounds.

Topics: Carbon; Cetrimonium; Cetrimonium Compounds; Chlorides; Chromatography; Chromatography, High Pressure Liquid; Chromatography, Liquid; Detergents; Hydrocarbons; Micelles; Pentanols; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Time Factors

Interactions in aqueous solutions of different generations of poly(amidoamine) (PAMAM) dendrimers containing amine, hydroxyl, or delta-glucolactone functional groups at the periphery with the anionic surfactant sodium dodecyl sulfate (SDS) were investigated. We used a SDS-specific electrode (EMF) for SDS monomer concentration monitoring, isothermal titration calorimetry (ITC) for binding information, and small angle neutron scattering (SANS) for structural studies. ITC experiments monitoring the interaction of the dendrimers with cationic dodecyltrimethylammonium bromide (DTAB) and nonionic hexaethylene glycol mono-n-dodecyl ether (C12EO6) showed no significant binding effects. In contrast, SDS binds to all of the above dendrimers. EMF and ITC data demonstrated a regular trend for both the onset of binding and binding saturation as the generation in each family of dendrimers increased. In addition, generation G6 exhibited a noncooperative binding process at very low SDS concentrations. Furthermore, the onset of cooperative binding in the EMF experiments started at lower concentrations as the weight % (w/v), the size, and the numbers of the internal or surface groups increased. On the other hand, the binding capacity of the dendrimers showed only a small dependence on the above parameters. At SDS concentrations approaching the binding limit and also at selective concentrations within the binding range, SANS measurements indicated that in all cases the bound surfactant is in the micellar form. From the electromotive force (EMF) measurements, ITC data, and SANS data, the stoichiometry of the supramolecular complexes was determined.

Topics: Calorimetry; Dendrimers; Electrodes; Ethers; Glycols; Molecular Structure; Neutron Diffraction; Polyamines; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface Properties; Surface-Active Agents; Titrimetry

We tested the effects of membrane phospholipids on the function of high-conductance, Ca(2+)-activated K(+) channels from the basolateral cell membrane of rabbit distal colon epithelium by reconstituting these channels into planar bilayers consisting of different 1:1 mixtures of phosphatidylethanolamine (PE), phosphatidylcholine (PC), phosphatidylserine (PS), and phosphatidylinositol (PI). At low ambient K(+) concentrations single-channel conductance is higher in PE/PS and PE/PI bilayers than in PE/PC bilayers. At high K(+) concentrations this difference in channel conductance is abolished. Introducing the negatively charged SDS into PE/PC bilayers increases channel conductance, whereas the positively charged dodecyltrimethylammonium has the opposite effect. All these findings are consistent with modulation of channel current by the charge of the lipid membrane surrounding the channel. But the K(+) that permeates the channel senses only a small fraction of the full membrane surface potential of the charged phospholipid bilayers, equivalent to separation of the conduction pathway from the charged phospholipid head groups by 20 A. This distance appears to insulate the channel entrance from the bilayer surface potential, suggesting large dimensions of the channel-forming protein. In addition, in PE/PC and PE/PI bilayers, but not in PE/PS bilayers, the open-state probability of the channel decreases with time ("channel rundown"), indicating that phospholipid properties other than surface charge are required to maintain channel fluctuations.

Topics: Animals; Calcium; Colon; Electric Conductivity; Electrochemistry; Intestinal Mucosa; Lipid Bilayers; Membrane Lipids; Phospholipids; Potassium; Potassium Channels; Quaternary Ammonium Compounds; Rabbits; Sodium Dodecyl Sulfate

We have studied the interaction of the polycationic peptide antibiotic polymyxin B (PMB) with asymmetric planar bilayer membranes via electrical measurements. The bilayers were of different compositions, including those of the lipid matrices of the outer membranes of various species of Gram-negative bacteria. One leaflet, representing the bacterial inner leaflet, consisted of a phospholipid mixture (PL; phosphatidylethanolamine, -glycerol, and diphosphatidylglycerol in a molar ratio of 81:17:2). The other (outer) leaflet consisted either of lipopolysaccharide (LPS) from deep rough mutants of PMB-sensitive (Escherichia coli F515) or -resistant strains (Proteus mirabilis R45), glycosphingolipid (GSL-1) from Sphingomonas paucimobilis IAM 12576, or phospholipids (phosphatidylglycerol, diphytanoyl-phosphatidylcholine). In all membrane systems, the addition of PMB to the outer leaflet led to the induction of current fluctuations due to transient membrane lesions. The minimal PMB concentration required for the induction of the lesions and their size correlated with the charge of the lipid molecules. In the membrane system resembling the lipid matrix of a PMB-sensitive strain (F515 LPS/PL), the diameters of the lesions were large enough (d = 2.4 nm +/- 8%) to allow PMB molecules to permeate (self-promoted transport), but in all other systems they were too small. A comparison of these phenomena with membrane effects induced by detergents (dodecyltriphenylphosphonium bromide, dodecyltrimethylammonium bromide, sodiumdodecylsulfate) revealed a detergent-like mechanism of the PMB-membrane interaction.

Topics: Anti-Bacterial Agents; Detergents; Lipid Bilayers; Organophosphorus Compounds; Polymyxin B; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate

The study includes partitioning of proteins in aqueous two-phase systems consisting of the polymer dextran and the non-ionic surfactant C12E5 (pentaethylene glycol mono-n-dodecyl ether). In this system a micelle-enriched phase is in equilibrium with a polymer-enriched phase. Charges can be introduced into the micelles by the addition of charged surfactants. The charge of the mixed micelles is easily varied in sign and magnitude independently of pH, by the addition of different amounts of negatively charged surfactant, sodium dodecyl sulphate (SDS), or positively charged surfactant dodecyl trimethyl ammonium chloride (DoTAC). A series of water-soluble model proteins (BSA, beta-lactoglobulin, myoglobin, cytochrome c and lysozyme), with different net charges at pH 7.1, have been partitioned in non-charged systems and in systems with charged mixed micelles or charged polymer (dextran sulphate). It is shown that partition coefficients for charged proteins in dextran-C12E5 systems can be strongly affected by addition of charged surfactants (SDS, DoTAC) or polymer (dextran sulphate) and that the effects are directly correlated to protein net charge.

Topics: Buffers; Cytochrome c Group; Dextran Sulfate; Ethers; Hydrogen-Ion Concentration; Isoelectric Point; Lactoglobulins; Micelles; Muramidase; Myoglobin; Polyethylene Glycols; Polymers; Proteins; Quaternary Ammonium Compounds; Serum Albumin, Bovine; Sodium Chloride; Sodium Dodecyl Sulfate; Surface Properties; Surface-Active Agents; Water

The fluorescence behavior of two tryptophans (Trp-134, Trp-213) in bovine serum albumin (BSA) and a single tryptophan (Trp-214) in human serum albumin (HSA) was examined. The maximum emission wavelength (lambda max) was 340.0 nm for both proteins. In a solution of sodium dodecyl sulfate (SDS), the lambda max of BSA abruptly shifted to 332 nm at 1 mM SDS and then reversed to 334 nm at 3 mM SDS. The lambda max of HSA gradually shifted to 330 nm below 3 mM SDS, although it returned to 338 nm at 10 mM SDS. In contrast to this, in a solution of dodecltrimethylammonium bromide, the lambda max positions of BSA and HSA gradually shifted to 334.0 and 331.5 nm, respectively. Differences in the fluorescence behavior of the proteins are attributed to the fact that Trp-134 exists only in BSA, with the assumption that Trp-213 of BSA behaves the same as Trp-214 of HSA. The Trp-134 behavior appears to relate to the disruption of the helical structure in the SDS solution.

Topics: Animals; Cattle; Circular Dichroism; Humans; Protein Conformation; Protein Structure, Secondary; Quaternary Ammonium Compounds; Serum Albumin; Serum Albumin, Bovine; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Surface-Active Agents; Time Factors; Tryptophan; Ultraviolet Rays

Although surfactant-induced acute irritant dermatitis has been extensively studied, our understanding about the induction and repair of the clinically more relevant chronic form is limited.. Our purpose was to investigate qualitative and quantitative differences in surfactant-induced irritant skin reactions from cumulative exposure to structurally unrelated surfactants and to compare the maximal irritant responses from this model with corresponding reactions noted in a previously reported acute irritation model.. Sodium lauryl sulfate (SLS), dodecyl trimethyl ammonium bromide (DTAB), and potassium soap were the model irritants. Surfactant solutions (7.5%) were applied for 20 minutes daily (for 8 consecutive days excluding the weekend) to the volar aspect of the forearm of 11 volunteers. Irritant reactions were repeatedly assessed until complete healing was indicated by visual assessment and by measurements of transepidermal water loss (TEWL), erythema (skin color reflectance), and stratum corneum hydration (electrical capacitance). Maximum irritant responses were compared with corresponding reactions from an acute irritation model.. TEWL was increased by SLS and DTAB to the same extent, but erythema was significantly higher in DTAB-treated skin. Skin dryness, as demonstrated by decreased capacitance values and increased scores for scaling and fissuring, was significantly more pronounced than in an acute irritation model for SLS and DTAB, although no difference was detected between the two surfactants. Potassium soap led to a slight increase in TEWL, whereas the remaining features were not significantly changed.. This chronic irritation model appears to represent the clinical situation of irritant contact dermatitis with pronounced skin dryness more closely than the acute irritation model. The present study confirms that an extended time is needed for complete healing of irritant skin reactions. We also demonstrated that the evaluation of the irritation potential of diverse surfactants depended significantly on the feature evaluated (erythema vs electrical capacitance and TEWL), on the mode of application (acute vs cumulative), and, in the cumulative model, on the point of observation.

Topics: Adult; Dermatitis, Irritant; Double-Blind Method; Electric Conductivity; Erythema; Evaluation Studies as Topic; Humans; Irritants; Lipids; Middle Aged; Models, Biological; Quaternary Ammonium Compounds; Skin; Soaps; Sodium Dodecyl Sulfate; Surface-Active Agents; Time Factors; Water Loss, Insensible; Wound Healing

Excessive calcium influx is important in the irreversible injury of cardiac myocytes and other cell types. The mechanism is unknown, but possibilities include L-type channels, Na(+)-Ca2+ exchange, sarcolemmal (SL) defects, and calcium leak channels. In this study, metabolic inhibition was used to induce ATP depletion and augmented calcium influx in cultured cardiac myocytes. Inhibition of the L-type calcium channel and Na(+)-Ca2+ exchanger had no significant effect on the calcium leak. There was no significant lactate dehydrogenase release, indicating that the leak did not occur through major SL defects. No alterations in the asymmetric distribution of SL phospholipids were demonstrated. Phospholipid rearrangements were therefore not responsible. The leak was unaffected by 0.5 mM cadmium and 1 microM nifedipine but was augmented by 50 microM nifedipine, characteristics in common with calcium leak channels. Insertion of the cationic amphiphiles dodecyltrimethylammonium bromide or polymyxin B sulfate into the SL had a profound inhibitory effect on the calcium leak. The anionic amphiphile sodium dodecyl sulfate had the opposite effect, and the neutral amphiphile lauryl acetate had no effect. These results suggest that an alteration in the SL surface charge affects calcium leak. It is proposed that the augmented calcium influx occurs via calcium leak channels and that these can be modulated by charged amphiphiles.

Topics: Adenosine Triphosphate; Animals; Animals, Newborn; Calcium; Calcium Channels; Cell Membrane; Cells, Cultured; Myocardium; Polymyxin B; Quaternary Ammonium Compounds; Rats; Sodium Dodecyl Sulfate

Modulation of voltage-dependent sodium and potassium currents by charged amphiphiles was investigated in cardiac ventricular myocytes using the patch-clamp technique. Negatively charged sodium dodecylsulfate (SDS) increased amplitude of INa, whereas positively charged dodecyltrimethylammonium (DDTMA) decreased INa. Furthermore, SDS shifted the steady-state activation and inactivation of INa in the negative direction, whereas DDTMA shifted the curves in the opposite direction. These shifts provided an explanation for the changes in current amplitude. Activation and inactivation kinetics of INa were accelerated by SDS but slowed by DDTMA. These changes in both steady-state gating and kinetics of INa are consistent with a decrease of the intramembrane field by SDS and an increase of the field by DDTMA due to an alteration of surface potential after their insertion into the outer monolayer of the sarcolemma. The effect of SDS on the steady-state inactivation of INa was concentration dependent and partially reversed by screening surface charges with increased extracellular [Ca2+]. These amphiphiles also altered the activation of the delayed rectifier K+ current (IK,del), producing a shift in the negative direction by SDS but in the positive direction by DDTMA. These results suggest that the insertion of charged amphiphiles into the cell membrane alters the behavior of voltage-dependent INa and IK,del by changing the surface charge density, and consequently the surface potential and implies, although indirectly, that the lipid surface charges are important to the voltage-dependent gating of these channels.

Topics: Animals; Calcium; Cell Membrane; Electrophysiology; Guinea Pigs; Heart Ventricles; In Vitro Techniques; Ion Channel Gating; Kinetics; Membrane Potentials; Myocardium; Nifedipine; Potassium Channels; Quaternary Ammonium Compounds; Rabbits; Sodium Channels; Sodium Dodecyl Sulfate; Tetraethylammonium Compounds; Thermodynamics

The effects of ouabain on muscle tension and the intracellular Ca2+ level ([Ca2+]i) were examined in guinea-pig aorta loaded with fura-2. Ouabain caused a gradual and sustained increase in both [Ca2+]i and muscle tension. There was a positive correlation between these two parameters. In Ca(2+)-free solution, ouabain did not affect either [Ca2+]i or muscle tension, suggesting that the ouabain-induced increase in [Ca2+]i was not due to Ca2+ release from storage sites. The ouabain-induced increase in [Ca2+]i and muscle tension was inhibited by Ni2+, which inhibits the Na+/Ca2+ exchanger, but not by verapamil. Furthermore, anionic and cationic amphiphiles were used as modulators of the Na+/Ca2+ exchanger. Sodium dodecyl sulfate accelerated the responses to ouabain, whereas dodecyltrimethylammonium bromide inhibited them. These results suggest that in the guinea-pig aorta, ouabain induces contraction by increasing the Ca2+ influx through the Na+/Ca2+ exchanger on the plasma membrane, but not through verapamil-sensitive Ca2+ channels.

Topics: Animals; Aorta; Calcium; Carrier Proteins; Cell Membrane; Electric Stimulation; Guinea Pigs; In Vitro Techniques; Male; Muscle Contraction; Muscle, Smooth, Vascular; Nickel; Ouabain; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Sodium-Calcium Exchanger; Verapamil

Exposure of isolated adult rabbit myocytes to the negatively charged amphiphile dodecylsulfate (DDS; 10 microM) increased the contraction amplitude to 185% of control. The positively charged amphiphile dodecyltrimethylammonium (DDTMA; 10 microM) decreased the amplitude to 58%. DDS increased Ca2+ uptake by the same cells, but this uptake was partially prevented by nifedipine. DDTMA had no effect on Ca2+ uptake. Ca2+ binding to isolated sarcolemma of neonatal heart cells was increased by 10 microM DDS and, at higher concentrations, reduced by DDTMA. Single-cell voltage-clamp studies, using isolated rabbit myocytes, showed that DDS enhanced L-type Ca2+ currents (ICa,L), whereas DDTMA depressed ICa,L. DDS shifted current-voltage (I-V) and isochronal inactivation curves of ICa,L in the negative direction, whereas DDTMA shifted them in positive direction. Furthermore, DDS depressed T-type Ca2+ currents (ICa,T), and DDTMA enhanced ICa,T. The inotropic effects of the amphiphiles are therefore mediated to a significant degree by ICa,L. The shifts in the I-V and inactivation curves of ICa,L and the effect on ICa,T can be explained by changes in the actual membrane potential (Em), induced by the insertion of the amphiphiles in the outer monolayer of the sarcolemma. However, the changes in the Em do not explain the effect on the maximal current, indicating effects on the channel per se, possibly by an alteration of the lipid environment.

Topics: Action Potentials; Adenosine Triphosphatases; Animals; Ca(2+) Mg(2+)-ATPase; Calcium; Calcium-Transporting ATPases; Carrier Proteins; Cation Transport Proteins; Cells, Cultured; Electrophysiology; Myocardial Contraction; Myocardium; Potassium; Quaternary Ammonium Compounds; Sarcolemma; Sodium Dodecyl Sulfate; Sodium-Calcium Exchanger

A laboratory-scale cyclone column reactor was tested to determine how its oxygen transfer characteristics were affected by surfactants in the liquid medium. The volumetric oxygen transfer coefficient was greatly decreased by small quantities of the synthetic surfactants dodecyltrimethylammonium bromide and sodium dodecylsulfate, and the biosurfactant surfactin produced by Bacillus subtilis (ATCC 21332). Since the gas holdup fraction was generally increased due to foaming, the effectiveness of the surfactants was probably due to an increase in the interfacial film resistance. B. subtilis was grown in the cyclone column to 0.6 g dm-3 with a significant level of surfactin produced while maintaining at least 75% oxygen saturation in the broth. Process optimization and scale-up of surfactin production will have to consider oxygen transfer as a key parameter.

Topics: Bacillus subtilis; Bacterial Proteins; Cell Division; Industrial Microbiology; Lipopeptides; Oxygen; Peptides, Cyclic; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Surface-Active Agents

The value of electrokinetic capillary chromatography for separating structurally similar model peptides and tryptic digests is demonstrated. The behavior of model peptides in buffer systems containing dodecyltrimethylammonium bromide, hexadecyltrimethylammonium bromide, sodium dodecyl sulfate and two cyclodextrins as additives is described. These additives, under different analytical circumstances, exhibit certain beneficial effects for peptides with similar net charges but different hydrophobicities. Separations of underivatized peptides, utilizing UV detection, are presented. In addition, separation of fluorescent products of peptides derivatized with o-phthalaldehyde, fluorescamine, and a new reagent, 3-(4-carboxybenzoyl)-2-quinolinecarboxaldehyde, are demonstrated and discussed. Beneficial spectroscopic detection effects with cyclodextrin are also noted.

Topics: Chromatography; Cyclodextrins; Fluorescamine; Fluorometry; Micelles; o-Phthalaldehyde; Peptides; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Ultraviolet Rays

Incubation of isolated bovine cornea with the surfactants lauryl trimethylammonium bromide (LTAB), sodium lauryl sulphate (NaLS) or Tween 20 in contact only with the epithelium side (outside) of the cornea produced dose-related development of opacity. The order of efficacy was LTAB greater than NaLS greater than Tween 20. After incubation and opacity reading the epithelium was surgically removed and the opacity of the remaining de-epithelialized cornea (stroma and endothelium) measured. The results indicate that the surfactants caused opacity predominantly by affecting the epithelium which itself became opaque.

Topics: Animals; Cattle; Corneal Opacity; Epithelium; In Vitro Techniques; Polysorbates; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate

We have used charged amphiphiles as phospholipid analogues to modulate the interaction of Ca2+ with myocardial sarcolemma. The amphiphiles were dodecyl sulfate, dodecyltrimethylamine, and lauryl acetate; these are anionic, cationic, and neutral molecules, respectively. The hydrophobic alkyl chain is identical in each case; only the hydrophilic head group is varied. The anionic dodecyl sulfate (50-100 microM) augmented the Ca2+ binding and Na+-Ca2+ exchange activity of sarcolemmal vesicles by approximately 80% and increases the contractility of rabbit papillary muscle. Both developed force and its derivative were increased by approximately 100% with no increase in rest tension. Cationic dodecyltrimethylamine (20-100 microM) produced nearly opposite effects. Neutral lauryl acetate (100 microM) had little apparent effect on any measurement. The charged amphiphiles should be useful tools for further elucidation of excitation-contraction coupling processes in a variety of contractile tissues.

Topics: Acetates; Animals; Calcium; Cations; Dogs; Fatty Alcohols; Ion Exchange; Myocardial Contraction; Myocardium; Papillary Muscles; Quaternary Ammonium Compounds; Rabbits; Sarcolemma; Sodium; Sodium Dodecyl Sulfate

The effect of cationic, anionic and nonionic detergents on the EPR spectrum of spin-labeled somatostatin has been studied. At detergent concentrations well above the critical micelle concentration, nonionic detergents do not alter the EPR spectrum. Sodium dodecyl sulfate markedly alters both the line height ratio and the hyperfine splitting constant, whilst dodecyltrimethylammonium bromide alters only slightly the hyperfine splitting constant and line height ratio. The somatostatin-sodium dodecyl sulfate complex appeared monodisperse by sedimentation equilibrium with about 17 g bound detergent per g peptide. Circular dichroic and difference spectra of the dodecyl sulfate-somatostatin complex show that the tryptophanyl residue is buried in a nonpolar environment and that the secondary and tertiary structure of the peptide is markedly altered. Sedimentation equilibrium studies suggest that two types of dodecyltrimethylammonium-somatostatin complex exist. One type resembles the dodecyl sulfate-peptide complex, whilst the other appears to include several peptide units with only about one gram bound detergent per gram peptide.

Topics: Amino Acids; Chemical Phenomena; Chemistry; Circular Dichroism; Detergents; Electron Spin Resonance Spectroscopy; Micelles; Models, Biological; Polyethylene Glycols; Protein Conformation; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Somatostatin; Spectrophotometry, Ultraviolet; Ultracentrifugation

The effect of detergents on the stability of enteric viruses was found to be highly dependent on pH. This was demonstrated primarily with two ionic detergents, sodium dodecyl sulfate (an anionic detergent) and dodecyltrimethylammonium chloride (a cationic detergent). Both detergents were shown to be potent virucidal agents for reovirus, but the effects of sodium dodecyl sulfate were minimal near neutrality and much more pronounced at low than at high pH values. Dodecyltrimethylammonium chloride was extremely virucidal at high pH's but had little observable effect on reovirus stability at low pH values. In contrast, both detergents protected enteroviruses against heat at neutral and alkaline pH's. However, as was found with reovirus, sodium dodecyl sulfate was extremely virucidal at pH values below 5, even when the virus samples were incubated in ice. At different pH's the effects of detergents on the stabilities of coliphages T4, f1, and Q beta were qualitatively similar to those found with reovirus. Differences in viral stability in these experiments appeared to be due to the effects of pH on the ionic states of the viral capsid proteins.

Topics: Coliphages; Detergents; Enterovirus B, Human; Hot Temperature; Hydrogen-Ion Concentration; Poliovirus; Quaternary Ammonium Compounds; Reoviridae; Sodium Dodecyl Sulfate