Surfactant-based supramolecular dye assembly: A highly selective and economically viable platform for quantification of heparin antidote.

Herein, we have employed a supramolecular assembly of a cationic dye, LDS-698 and a common surfactant sodium dodecyl sulfate (SDS) as a turn-on fluorescent sensor for protamine (Pr) detection. Addition of cationic Pr to the solution of dye-surfactant complex brings negatively charged SDS molecules together through strong electrostatic interaction, assisting aggregation of SDS way before its critical micellar concentration (CMC). These aggregates encapsulate the dye molecules within their hydrophobic region, arresting non-radiative decay channels of the excited dye. Thus, the LDS-698•SDS assembly displays substantial enhancement in fluorescence intensity that follows a nice linear trend with Pr concentration, providing limit of detection (LOD) for Pr as low as 3.84(±0.11) nM in buffer, 124.4(±6.7) nM in 1% human serum and 28.3(±0.5) nM in 100% human urine. Furthermore, high selectivity, low background signal, large stokes shift, and emission in the biologically favorable deep-red region make the studied assembly a promising platform for Pr sensing. As of our knowledge it is the first ever Pr sensory platform, using a very common surfactant (SDS), which is economically affordable and very easily available in the market. This innovative approach can replace the expensive, exotic and specialized chemicals considered for the purpose and thus showcase its potential in practical applications.

Decellularized tissue exhibits large differences of extracellular matrix properties dependent on decellularization method: novel insights from a standardized characterization on skeletal muscle.

Decellularized matrices are an attractive choice of scaffold in regenerative medicine as they can provide the necessary extracellular matrix (ECM) components, signals and mechanical properties. Various detergent-based protocols have already been proposed for decellularization of skeletal muscle tissue. However, a proper comparison is difficult due to differences in species, muscle origin and sample sizes. Moreover, a thorough evaluation of the remaining acellular matrix is often lacking. We compared an in-house developed decellularization protocol to four previously published methods in a standardized manner. Porcine skeletal muscle samples with uniform thickness were subjected to in-depth histological, ultrastructural, biochemical and biomechanical analysis. In addition, 2D and three-dimensional cytocompatibility experiments were performed. We found that the decellularization methods had a differential effect on the properties of the resulting acellular matrices. Sodium deoxycholate combined with deoxyribonuclease I was not an effective method for decellularizing thick skeletal muscle tissue. Triton X-100 in combination with trypsin, on the other hand, removed nuclear material but not cytoplasmic proteins at low concentrations. Moreover, it led to significant alterations in the biomechanical properties. Finally, sodium dodecyl sulphate (SDS) seemed most promising, resulting in a drastic decrease in DNA content without major effects on the ECM composition and biomechanical properties. Moreover, cell attachment and metabolic activity were also found to be the highest on samples decellularized with SDS. Through a newly proposed standardized analysis, we provide a comprehensive understanding of the impact of different decellularizing agents on the structure and composition of skeletal muscle. Evaluation of nuclear content as well as ECM composition, biomechanical properties and cell growth are important parameters to assess. SDS comes forward as a detergent with the best balance between all measured parameters and holds the most promise for decellularization of skeletal muscle tissue.

Interaction between Sophorolipids and ß-glucan in Aqueous Solutions.

Skin disorders, including acne vulgaris, atopic dermatitis, and rosacea, are characterized by the presence of biofilms, which are communities of microorganisms. The mechanical stability of biofilms is attributed to one of their constituents-polysaccharides-which are secreted by microorganisms. Sophorolipids are biosurfactants with biofilm disruption and removal abilities and are expected to become alternatives for classical petrochemical-based surfactants in cosmetics. In this study, we investigated the influence of sophorolipids on ß-glucan such as dispersion status, interaction mechanism, and configuration change as a model polysaccharide of biofilm in aqueous solution. Dynamic light scattering measurements showed that sophorolipids interfere with the aggregation of ß- glucan in aqueous solutions. In contrast, sodium dodecyl sulfate (SDS), which is used as a typical surfactant reference, promotes the aggregation of ß-glucan. The interaction between sophorolipids and ß-glucan were investigated using surface tension measurements and isothermal titration calorimetry (ITC). Surface tension increased only near critical micelle concentration (CMC) region of sophorolipids in the presence of ß-glucan. This suggests that the interaction occurred in the solution rather than at the air-liquid interface. Moreover, the results of ITC indicate that hydrophobic interactions were involved in this interaction. In addition, the results of optical rotation measurements indicate that sophorolipids did not unfold the triple helical structure of ß-glucan. ß-glucan dispersion was expected to be caused steric hindrance and electrostatic repulsion when sophorolipids interacted with ß-glucan via hydrophobic interactions owing to the unique molecular structure of sophorolipids attributed by a bulky sugar moiety and a carboxyl functional group. These results demonstrated unique performances of sophorolipids on ß-glucan and provided more insights on the efficacy of sophorolipids as good anti-biofilms.

Ultrasound assisted electrodeposition of photocatalytic antibacterial MoS2-Zn coatings controlled by sodium dodecyl sulfate.

Photocatalytic MoS2 with visible light response is considered as a promising bactericidal material owing to its non-toxicity and high antibacterial efficiency. However, photocatalysts always exist as powder, so it is difficult to settle photocatalysts on the metal surface, which limits their application in aqueous environments. To solve this problem, ultrasound and sodium dodecyl sulfate (SDS) were introduced into the co-deposition process of MoS2 and zinc matrix, so that novel MoS2-Zn coatings were obtained. In this process, ultrasound and SDS strongly promoted the dispersion and adsorption of MoS2 on the co-depositing surfaces. Then MoS2 were proved to be composited into the Zn matrix with effective structures, and the addition of SDS effectively increased the loading content of MoS2 in the MoS2-Zn coatings. Besides, the antibacterial performance of the MoS2-Zn coatings was evaluated with three typical fouling bacteria E.coli, S.aureus and B.wiedmannii. The MoS2-Zn coating showed high and broad-spectrum antibacterial properties with over 98 % inhibition rate against these three bacteria. Furthermore, it is proved that the MoS2-Zn coatings generated superoxide (·O2-) and hydroxyl radicals (·OH) under visible light, which played the dominant and subordinate roles in the antibacterial process, respectively. The MoS2-Zn coatings also showed high antibacterial stability after four "light-dark" cycles. According to the results of the attached bacteria, the MoS2-Zn coatings were considered to effectively repel the living pelagic bacteria instead of killing the attached ones, which was highly environmentally friendly. The obtained MoS2-Zn coatings were considered promising in biofilm inhibiting and marine antifouling fields.

Effect of biologically active amino acids based deep eutectic solvents on sodium dodecyl sulfate: A comparative spectroscopic study.

Study the effects of three novel synthesized biologically deep eutectic solvents (DESs) on the micellar characteristics of anionic sodium dodecyl sulfate (SDS). The biologically active amino acids based three DESs synthesized have composed the 2:1 M of L-Aspartic acid (DES1), L-Tyrosine (DES2), L-Glutamine (DES3) and choline chloride, furthermore which characterized by FTIR. Surface tension, viscosity, UV-visible, fluorescence, and FTIR spectroscopy are a few of the techniques used to study the interactions of SDS within 5 and 10 wt% of three novel biological DESs in aqueous solutions. The presence and absence of 5 and 10 wt% of the three novel biological DESs in an aqueous solution is used to study the critical micelle concentration (CMC) and various interfacial characteristics including CMC, the efficiency of adsorption, the maximum surface excess concentration, the packing parameter, the minimum area per molecule, and the surface pressure at CMC, is assessed by the surface tension method. The calculated fluorescence data and those obtained using surface tension and UV-visible methods correspond well. The interactions that cause changes in the structure of the surfactant self-assemblies within aqueous DESs were investigated using FTIR technique. It is significant to highlight that the presence of unique biological DESs considerably facilitates the micellization process for SDS and the extent is more affinity for DES2 compared to DES1/DES3. The colloidal properties of DES and their combinations with water are anticipated to benefit from the current findings.

The investigation of the binding ability between sodium dodecyl sulfate and Cu (II) in urban stormwater runoff.

The simultaneous presence of heavy metals and surfactants in runoff induces complexation and ecological harm during migration. However, interactions between these pollutants are often overlooked in past studies. Thus, investigating heavy metal-surfactant complexes in runoff is imperative. In this work, Cu (II) and sodium dodecyl sulfate (SDS) were selected to investigate the interaction between heavy metals and surfactants due to the higher detected frequency in runoff. Through 1H NMR and FTIR observation of hydrogen atom nuclear displacement and functional group displacement of SDS, the change of SDS and Cu (II) complexation was obtained, and then the complexation form of Cu (II) and SDS was verified. The results showed that solution pH values and ionic strength had significant effects on the complexation of Cu (II). When the pH values increase from 3.0 to 6.0, the complexation efficiency of SDS with Cu (II) increased by 12.12% at low concentration of SDS, which may be attributed to the excessive protonation in the aqueous solution at acidic condition. The increase of ionic strength would inhibit the complexation reaction efficiency by 19.57% and finally reached the platform with concentration of NaNO3 was 0.10 mmol/L, which was mainly due to the competitive relationship between Na (I) and Cu (II). As a general filtering material in stormwater treatment measures, natural zeolite could affect the interaction between SDS and Cu (II) greatly. After the addition of SDS, the content of free Cu (II) in the zeolite-SDS-Cu (II) three-phase mixed system was significantly reduced, indicating that SDS had a positive effect on the removal of Cu (II) from runoff. This study is of great significance for investigating the migration and transformation mechanism of SDS and Cu (II) in the future and studying the control technology of storm runoff pollution.

Drug-ionic surfactant interactions: density, sound speed, spectroscopic, and electrochemical studies.

The failure of antibiotics against infectious diseases has become a global health issue due to the incessant use of antibiotics in the community and a lack of entry of new antibacterial drugs onto the market. The limited knowledge of biophysical interactions of existing antibiotics with bio-membranes is one of the major hurdles to design and develop more effective antibiotics. Surfactant systems are the simplest biological membrane models that not only mimic the cell membrane functions but are also used to investigate the biophysical interactions between pharmaceutical drugs and bio-membranes at the molecular level. In this work, volumetric and acoustic studies were used to investigate the molecular interactions of moxifloxacin (MXF), a potential antibacterial drug, with ionic surfactants (dodecyl-tri-methyl-ammonium bromide (DTAB), a cationic surfactant and sodium dodecyl sulfate (SDS), an anionic surfactant) under physiological conditions (phosphate buffer, pH 7.4) at T = 298.15-313.15 K at an interval of 5 K. Various volumetric and acoustic parameters were computed from the density and sound speed data and interpreted in terms of MXF-ionic surfactant interaction using electrostriction effect and co-sphere overlap model. Absorption spectroscopy and cyclic voltammetry were further used to determine the binding, partitioning, and related free energies of MXF with ionic micelles.

Non-Steroidal Anti-Inflammatory Drugs Loaded to Micelles for the Modulation of Their Water Solubility.

The low water solubility of aspirin (ASPH) is well known, creating research challenges regarding both its composition and its delivery. Therefore, the development of new aspirin-based formulations that are water soluble is a research, technological, and financial issue. With the aim to improve the water solubility of ASPH, the micelle of formula SLS@ASPH (SLS = Sodium Lauryl Sulfate) was formed. The Critical Micelle Concentration (CMC) of SLS in the presence of ASPH was determined by ultrasonic velocity, complementary, and transient birefringence measurements. The SLS@ASPH was characterized by the melting point (m.p.), attenuated total reflection spectroscopy (FT-IR-ATR), and X-ray fluorescence spectroscopy (XRF) in a solid state and in a solution by ultraviolet-visible (UV-Vis) and 1H NMR spectroscopies. The SLS/ASPH molar ratio was determined to be 5/1 in SLS@ASPH. The inhibitory activity of SLS@ASPH towards lipoxygenase (LOX), an enzyme that takes part in the inflammation mechanism, was studied. The inhibitory activity of SLS@ASPH against LOX is 3.5-fold stronger than that of free SLS. The in vitro toxicity of the SLS@ASPH was tested on immortalized human keratinocyte (HaCaT) cells.

Development and qualification of clinical grade decellularized and cryopreserved human esophagi.

Tissue engineering is a promising alternative to current full thickness circumferential esophageal replacement methods. The aim of our study was to develop a clinical grade Decellularized Human Esophagus (DHE) for future clinical applications. After decontamination, human esophagi from deceased donors were placed in a bioreactor and decellularized with sodium dodecyl sulfate (SDS) and ethylendiaminetetraacetic acid (EDTA) for 3 days. The esophagi were then rinsed in sterile water and SDS was eliminated by filtration on an activated charcoal cartridge for 3 days. DNA was removed by a 3-hour incubation with DNase. A cryopreservation protocol was evaluated at the end of the process to create a DHE cryobank. The decellularization was efficient as no cells and nuclei were observed in the DHE. Sterility of the esophagi was obtained at the end of the process. The general structure of the DHE was preserved according to immunohistochemical and scanning electron microscopy images. SDS was efficiently removed, confirmed by a colorimetric dosage, lack of cytotoxicity on Balb/3T3 cells and mesenchymal stromal cell long term culture. Furthermore, DHE did not induce lymphocyte proliferation in-vitro. The cryopreservation protocol was safe and did not affect the tissue, preserving the biomechanical properties of the DHE. Our decellularization protocol allowed to develop the first clinical grade human decellularized and cryopreserved esophagus.

Solvent-Induced Lag Phase during the Formation of Lysozyme Amyloid Fibrils Triggered by Sodium Dodecyl Sulfate: Biophysical Experimental and In Silico Study of Solvent Effects.

Amyloid aggregates arise from either the partial or complete loss of the native protein structure or the inability of proteins to attain their native conformation. These aggregates have been linked to several diseases, including Alzheimer's, Parkinson's, and lysozyme amyloidosis. A comprehensive dataset was recently reported, demonstrating the critical role of the protein's surrounding environment in amyloid formation. In this study, we investigated the formation of lysozyme amyloid fibrils induced by sodium dodecyl sulfate (SDS) and the effect of solvents in the medium. Experimental data obtained through fluorescence spectroscopy revealed a notable lag phase in amyloid formation when acetone solution was present. This finding suggested that the presence of acetone in the reaction medium created an unfavorable microenvironment for amyloid fibril formation and impeded the organization of the denatured protein into the fibril form. The in silico data provided insights into the molecular mechanism of the interaction between acetone molecules and the lysozyme protofibril, once acetone presented the best experimental results. It was observed that the lysozyme protofibril became highly unstable in the presence of acetone, leading to the complete loss of its ß-sheet conformation and resulting in an open structure. Furthermore, the solvation layer of the protofibril in acetone solution was significantly reduced compared to that in other solvents, resulting in fewer hydrogen bonds. Consequently, the presence of acetone facilitated the exposure of the hydrophobic portion of the protofibril, precluding the amyloid fibril formation. In summary, our study underscores the pivotal role the surrounding environment plays in influencing amyloid formation.

Bovine liver catalase turns into three conformational states after exposure to an anionic surfactant.

The mechanism by which anionic surfactants promote amyloid fibril is not well understood. Here, we investigated how sodium dodecyl sulfate (SDS), a negatively charged surfactant, affects the fibrillation of the partially unfolded random-coiled bovine liver catalase (BLC) at a pH of 2.0. We used several methods, including turbidity, RLS kinetics, intrinsic fluorescence, ThT fluorescence, far-UV CD, and TEM imaging, to evaluate the conformational changes of BLC in vitro in response to SDS treatment. BLC is a multimeric protein and well folded at physiological pH but forms a random coil structure at pH 2.0. Intrinsic fluorescence and far-UV CD data showed that below 0.1 mM SDS, random coiled BLC turned into a native-like structure. BLC incubated with an SDS concentration ranging from 0.1 to 2.0 mM led to the formation of aggregates. The ThT fluorescence intensity was enhanced in the aggregated BLC samples (0.1-2.0 mM SDS), and cross beta-sheeted structure was detected by the far UV CD measurements. BLC adopts a complete alpha-helical structure upon interacting with SDS at a more than 2.0 mM concentration at pH 2.0. Understanding the mechanism of surfactant- or lipid-induced fibrillation is important for therapeutic purposes.

Size separation of sodium dodecyl sulfate-proteins by capillary electrophoresis in dilute and ultra-dilute dextran solutions.

SDS capillary gel electrophoresis is a widely used in the biopharma and the biomedical fields for rapid size separation of proteins. However, very limited information is available on the use of dilute and ultra-dilute sieving matrices for SDS-protein analysis. Here, background electrolytes (BGEs) containing 1%-0% dextran were used in borate-based BGE to separate a protein sizing ladder (PSL) ≤225 kDa and the intact and subunit forms of a therapeutic monoclonal antibody (mAb). The separation performance for the PSL and mAb components differed significantly with decreasing dextran concentration. Ferguson and reptation plots were used to elucidate the separation mechanism. Highly diluted dextran solutions resulted in linear Ferguson plots for both solute types (cf. Ogston theory) in spite of this model assumes a rigid pore structure, thus cannot describe the separation mechanism in ultra-dilute polymer solutions with no reticulations. The saddle differences between the resolution of the PSL and the intact/subunit mAb forms in ultra-dilute dextran-borate matrices suggested the importance of shape selectivity, manifested by the adequate separation of the SDS covered intact as well as light and heavy chain subunits of the therapeutic mAb even at zero dextran concentration.

Sodium lauryl sulfate as lubricant in tablets formulations: Is it worth?

Lubricants are excipients used in tablet formulations to reduce friction and adhesion forces within the die or on the punches surface during the manufacturing process. Despite these excipients are always required for the tablets production, their amount must be carefully evaluated since lubricants can negatively impact on mechanical strength, disintegration and dissolution behavior of solid dosage forms. Alternative compounds have been suggested to overcome the issues of conventional lubricants and sodium lauryl sulfate (SDS) is one of the most promising one. Despite SDS has been object of several investigations, a definitive conclusion on its effectiveness cannot still be drawn. Particularly, its efficacy on tablets disaggregation and API dissolution is still unclear. Here, the effect of SDS on all the relevant features of tablets and tableting process has been evaluated on immediate release hydrophobic tablets formulations in comparison with conventional lubricants. The results of this investigation are quite outspoken: SDS has a low lubricant power while it determines only a limited improvement on tablets hardness. It greatly improves the tablets wettability but only on model formulations, the presence of superdisintegrants resets its effectiveness and any possible effect on tablets disaggregation. None of the tested formulations showed improvement on the API dissolution rate.

Anionic surfactant causes dual conformational changes in insulin.

Amyloid fibrillation is a process by which proteins aggregate and form insoluble fibrils that are implicated in several neurodegenerative diseases. In n this study, we aimed to investigate the impact of the negatively charged detergent sodium dodecyl sulfate (SDS) on insulin amyloid fibrillation at pH 7.4 and 2.0, as SDS has been linked to the acceleration of amyloid fibrillation in vitro, but the underlying molecular mechanism is not fully understood. Our findings show that insulin forms amyloid-like aggregates in the presence of SDS at concentrations ranging from 0.05 to 1.8 mM at pH 2.0, while no aggregates were observed at SDS concentrations greater than 1.8 mM, and insulin remained soluble. However, at pH 7.4, insulin remained soluble regardless of the concentration of SDS. Interestingly, the aggregated insulin had a cross-ß sheet secondary structure, and when incubated with higher SDS concentrations, it gained more alpha-helix. The electrostatics and hydrophobic interaction of SDS and insulin may contribute to amyloid induction. Moreover, the SDS-induced aggregation was not affected by the presence of salts. Furthermore, as the concentration of SDS increased, the preformed insulin amyloid induced by SDS began to disintegrate. Overall, our study sheds light on the mechanism of surfactant-induced amyloid fibrillation in insulin protein.

A method to determine two antibiotics prescribed to treat nosocomial infections in plasma and urine by micellar liquid chromatography.

Combined prescription of the antimicrobial drugs linezolid and meropenem is a common strategy to treat multidrug-resistant nosocomial infections. We propose an innovative method to determine these two drugs in plasma and urine, based on micellar liquid chromatography. Both biological fluids were diluted in mobile phase, filtered and directly injected, without any extraction step. Using a C18 column and a mobile phase of 0.1 M sodium dodecyl sulfate - 10 % methanol, phosphate buffered at pH 3, running under isocratic mode, both antibiotics were eluted without overlapping in<15 min. Detection was by absorbance: 255 nm for linezolid and 310 nm for meropenem. The influence of sodium dodecyl sulfate and methanol concentration on retention factor was established for both drugs using an interpretative approach assisted by chemometrics. The procedure was successfully validated following the guidelines of 2018 Bioanalytical Method Validation Guidance for Industry in terms of: linearity (determination coefficients over 0.99990), calibration range (1 - 50 mg/L), instrumental and method sensitivity, trueness (bias of -10.8 to + 2.4%), precision (relative standard deviation of < 10.2%), dilution integrity, carry-over effect, robustness and stability. It should be emphasized that the method uses low volumes of toxic and volatile solvents and can be achieved in a short period. The procedure was found useful for routine analysis, as it was cost-affordable, more eco-friendly and safer than hydroorganic HPLC, easy-to-handle and highly sample-throughput. Finally, it was applied to incurred samples of patients taking this medication.

Monitoring of low-molecular-weight protein aggregation by CE-SDS as a complementary method to SE-HPLC.

Capillary electrophoresis with sodium dodecyl sulfate (CE-SDS) has long been proven to have excellent performance in the analysis and characterization of therapeutic proteins. However, it is rarely used for the detection of low-molecular-weight proteins or peptides. Our research has proved the ability of CE-SDS to characterize the purity of low-molecular-weight proteins (i.e., <10 kDa) and even polypeptides. In this article, insulin glargine was used as a model protein, and CE-SDS was used to analyze the samples damaged by heating and light exposure. The monomers, dimers, and trimers of insulin glargine were effectively separated, and the results of the mass spectrometry also confirmed the existence of two kinds of insulin aggregates. For comparison, the size-exclusion high-performance liquid chromatography (SE-HPLC) only showed a single aggregate peak. In addition, the denaturation conditions caused only the covalent aggregates to appear in the CE-SDS analysis. These advantages also make CE-SDS an excellent supplementary technology to the traditional SE-HPLC, providing biopharmaceutical analysts with more information.

How eluents define proteomic fingerprinting of protein corona on nanoparticles.

Nanoparticles (NPs) have broad application prospects in the field of biomedicine due to their excellent physicochemical properties. When entering biological fluids, NPs inevitably encountered proteins and were subsequently surrounded by them, forming the termed protein corona (PC). As PC has been evidenced to have critical roles in deciding the biological fates of NPs, how to precisely characterize PC is vital to promote the clinical translation of nanomedicine by understanding and harnessing NPs' behaviors. During the centrifugation-based separation techniques for the PC preparation, direct elution has been most widely used to strip proteins from NPs due to its simpleness and robustness, but the roles of multifarious eluents have never been systematically declared. Herein, seven eluents composed of three denaturants, sodium dodecyl sulfate (SDS), dithiothreitol (DTT), and urea (Urea), were applied to detach PC from gold nanoparticles (AuNPs) and silica nanoparticles (SiNPs), and eluted proteins in PC have been carefully characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and chromatography coupled tandem mass spectrometry (LC-MS/MS). Our results showed that SDS and DTT were the main contributors to the efficient desorption of PC on SiNPs and AuNPs, respectively. The molecular reactions between NPs and proteins were explored and verified by SDS-PAGE analysis of PC formed in the serums pretreated with protein denaturing or alkylating agents. The proteomic fingerprinting analysis indicated the difference of the eluted proteins brought by the seven eluents was the abundance rather than the species. The enrichment of some opsonins and dysopsonins in a special elution reminds us that the possibility of biased judgments on predicting NPs' biological behaviors under different elution conditions. The synergistic effects or antagonistic effects among denaturants for eluting PC were manifested in a nanoparticle-type dependent way by integrating the properties of the eluted proteins. Collectively, this study not only underlines the urgent need of choosing the appropriate eluents for identifying PC robustly and unbiasedly, but also provides an insight into the understanding of molecular interactions during PC formation.

Boosting the Separation of Adeno-Associated Virus Capsid Proteins by Liquid Chromatography and Capillary Electrophoresis Approaches.

The purity of the three capsid proteins that make up recombinant adeno-associated virus (rAAV) is considered a critical quality attribute of gene therapy products. As such, there is a clear need to develop separation methods capable of rapidly characterizing these three viral proteins (VPs). In this study, the potential benefits and limitations of different electrophoretic and chromatographic methods were evaluated, including capillary electrophoresis-sodium dodecyl sulfate (CE-SDS), reversed phase liquid chromatography (RPLC), hydrophilic interaction chromatography (HILIC), and hydrophobic interaction chromatography (HIC), for the analysis of VPs obtained from different serotypes (i.e., AAV2, AAV5, AAV8, and AAV9). CE-SDS is considered to be the reference method and provides a suitable separation of VP1-3 proteins using generic conditions and laser induced fluorescence detection. However, the characterization of post-translational modifications (i.e., phosphorylation, oxidation) remains difficult, and species identification is almost impossible due to the lack of compatibility between CE-SDS and mass spectrometry (MS). In contrast, RPLC and HILIC were found to be less generic than CE-SDS and require tedious optimization of the gradient conditions for each AAV serotype. However, these two chromatographic approaches are inherently compatible with MS, and were shown to be particularly sensitive in detecting capsid protein variants resulting from different post-translational modifications. Finally, despite being non-denaturing, HIC offers disappointing performance for viral capsid proteins characterization.

Preferential Removal of Alkali Metal Using Dodecanoic Acid and Sodium Dodecyl Sulfate in Foam Separation System.

The selectivity of adsorption between alkali metal ions (Li+, Na+, K+, Rb+, and Cs+) based on the ionic functional groups of the surfactants was studied using two types of surfactants, dodecanoic acid (DA) and sodium dodecyl sulfate (SDS), in the foam separation system. The results showed that Li+ was preferably removed by foam separation using DA. The removal rates of other alkali metal ions were relatively low, and there were no significant differences among other alkali metal ions (Na+, K+, Rb+, and Cs+). However, Cs+ exhibited the highest removal rate among the mixed alkali metals by foam separation using SDS. From these results, the selectivity of the alkali metal in foam separation was dependent on the type of surfactant.

Ultrathin Micellar Foam Films of Sodium Caseinate Protein Solutions.

Sodium caseinates (NaCas), derived from milk proteins called caseins, are often added to food formulations as emulsifiers, foaming agents, and ingredients for producing dairy products. In this contribution, we contrast the drainage behavior of single foam films made with micellar NaCas solutions with well-established features of stratification observed for the micellar sodium dodecyl sulfate (SDS) foam films. In reflected light microscopy, the stratified SDS foam films display regions with distinct gray colors due to differences in interference intensity from coexisting thick-thin regions. Using IDIOM (interferometry digital imaging optical microscopy) protocols we pioneered for mapping nanotopography of foam films, we showed that drainage via stratification in SDS films proceeds by the expansion of flat domains that are thinner than surrounding by a concentration-dependent step-size, and nonflat features (nanoridges and mesas) form at the moving front. Furthermore, stratifying SDS foam films show stepwise thinning, such that the step-size and terminal film thickness decrease with concentration. Here we visualize the nanotopography in protein films with high spatiotemporal resolution using IDIOM protocols to address two long-standing questions. Do protein foam films formulated with NaCas undergo drainage via stratification? Are thickness transitions and variations in protein foam films determined by intermicellar interactions and supramolecular oscillatory disjoining pressure? In contrast with foam films containing micellar SDS, we find that micellar NaCas foam films display just one step, nonflat and noncircular domains that expand without forming nanoridges and a terminal thickness that increases with NaCas concentration. We infer that the differences in adsorbing and self-assembling unimers triumph over any similarities in the structure and interactions of their micelles.