Binding Of Sodium Dodecyl Sulfate Research Articles

Globin X: A target for surfactant-like molecules.

Globin X (GbX) is recognized as a novel, intrinsically hexacoordinate, member of the vertebrate globin family. Previously we showed that GbX is significantly more stable than pentacoordinate vertebrate globins (Hb and Mb) at elevated temperatures, acidic pH as well as in the presence of denaturants. Such a unique feature of this protein led us to examine how the GbX interacts with surfactant-like molecules such as perfluorooctanoic acid (PFOA) and sodium dodecyl sulfate (SDS). In addition to GbXWT protein, the effect of intraprotein disulfide bridge and the heme iron pentacordination on GbX interactions with surfactant-like molecules was investigated by characterizing the GbXC65A and GXH90V constructs. The impact of surfactant on the structural properties of GbX was evaluated based on changes in the Soret band region and the emission properties of intrinsic Trp residues. The Kd values for SDS binding to the deoxy form of GbXWT, GbXC65A, and GbXH90V were determined to be 251 ± 4 μM, 188 ± 7 μM, and 358 ± 91 μM respectively, indicating that the intramolecular disulfide bond and hexacoordination do not have a significant effect on the surfactant-protein complex. However, the met form of GbXWT and GbXC65A binds SDS with Kd of 1426 ± 224 μM and 2106 ± 26 μM, pointing towards a lower affinity of the met form of the protein for SDS surfactant. Interestingly, PFOA produces a minimal change in the Soret band region, suggesting a distinct mechanism of binding. Based on the Trp emission data, the Kd values for PFOA binding to the met form of the protein were determined to be 40 ± 28 μM for GbX WT and 25 ± 1 μM for GbXC65A. The molecular mechanism of surfactant-like molecules binding to GbX was also evaluated using molecular dynamic simulations.

Modifying interprotein interactions for controlling heat-induced protein gelation

Globular proteins undergo heat-induced denaturation and eventually gelation at significantly elevated temperatures. The present study provides pathways to control temperature-driven protein gelation, having potential applications in a wide range of fields, from medicine to cosmetics to the food industry. The sol-gel transitions have been directed via modifying interprotein (electrostatic and hydrophobic) interactions by complexation of protein with amphiphiles. The heat-induced gelation of bovine serum albumin protein (anionic) is prevented in the presence of anionic sodium dodecyl sulfate (SDS) surfactant without significantly altering its native conformation. The specific binding of SDS monomers on the oppositely charged sites of protein increases the electrostatic repulsion between protein molecules, thereby suppressing the protein gelation. On the other hand, incorporating nonionic decaoxyethylene $n\ensuremath{-}\mathrm{dodecylether}$ (${\mathrm{C}}_{12}{\mathrm{E}}_{10}$) surfactant along with ionic surfactant reverses this scenario, and the solution state of the bovine serum albumin-SDS system undergoes gelation. The preferential binding of SDS with ${\mathrm{C}}_{12}{\mathrm{E}}_{10}$ nonionic surfactant forms detached mixed micelles, resulting in the release of the SDS monomers from protein, hence reverting the SDS-induced prevention of protein gelation. The results are counterintuitive and explained based on the interplay of hydrophobic and electrostatic interactions among protein molecules, as probed by small-angle neutron scattering, dynamic light scattering, and rheology.

Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis of Proteins.

Most analytical electrophoreses of proteins are achieved by separation in polyacrylamide gels under conditions that ensure dissociation of proteins into individual polypeptide subunits and minimize aggregation. Most commonly, the anionic detergent sodium dodecyl sulfate (SDS) is used in combination with a reducing agent (β-mercaptoethanol or dithiothreitol) and with heating to dissociate proteins before loading onto the gel. SDS binding denatures the polypeptides and imparts a negative charge that masks their intrinsic charge. The amount of SDS bound is generally sequence-independent and proportional to molecular weight; at saturation, approximately one SDS molecule is bound per two amino acids, or ∼1.4 g of SDS per gram of polypeptide. Therefore, the migration of SDS-polypeptide complexes in an electric field is proportional to the relative size of the polypeptide chain, and its molecular weight can be estimated by comparison to protein markers of known molecular weight. However, hydrophobicity, highly charged sequences, and certain posttranslational modifications such as glycosylation or phosphorylation may also influence migration. Thus, the apparent molecular weight of modified proteins does not always accurately reflect the mass of the polypeptide chain. This protocol describes preparation and running of SDS-PAGE gels, followed by staining to detect proteins using Coomassie Brilliant Blue. Finally, the stained SDS-PAGE gel may be scanned to an image or preserved by drying.

UV–VIS investigation of methyl red in presence of sodium dodecyl sulfate/methanol/ethanol/water system

This paper reports room temperature UV–VIS study of interaction of methyl red (MR) dye with sodium dodecyl sulfate (SDS)/methanol/ethanol/water systems in different ratios of the solvent components (R = 0, 10, 20, 30, and 40); where the concentration of water is represented by a R parameter. The concentration of SDS was varied from 1.4 × 10-4 to 2.8 × 10-3molL-1 for the SDS/methanol/water system and 2.2 × 10-4 to 4.4 × 10-3molL-1 for SDS/ethanol/water system. In all experiments, MR concentration was fixed to 7.4 × 10-6molL-1. The MR spectrum was very similar at lower R values. The solution appeared cloudy at R = 30. For R = 40, MR absorption maximum (λmax) strongly red-shifted from 412 nm to 493–495 nm on increasing the concentration of SDS in the methanol system but no such shift was observed in ethanol. The transparency of the solution again vanished at R = 50 and the experiment was not carried above. These observations suggested that MR exists in hydrazone and azo form in SDS/methanol and SDS/ethanol system; respectively. On increasing concentration of SDS, the MR absorbance increased in the methanol system (hyperchromic shift) and decreased in ethanol system (hypochromic shift). The distribution constant (K) and binding constant (K’) were evaluated through the NLREG procedure and the modified Benesi-Hildebrand equation was also introduced to calculate the binding constant (Kb) and Gibbs free energy of binding (ΔG0). With increasing R, the ΔG0 value became more negative in methanol system; whereas it became less negative in the ethanol system. The negative value of ΔG0 indicated the spontaneity of SDS binding with MR.

Investigation of the usage potential of calcium alginate beads functionalized with sodium dodecyl sulfate for wastewater treatment contaminated with waste motor oil.

In this study, calcium alginate (Ca-Alg) beads, an inexpensive, easily available, biodegradable material, were activated with anionic surfactant and used for the treatment of wastewater contaminated with waste motor oil. First, polyethyleneimine (PEI) was used to bind sodium dodecyl sulfate (SDS) onto the Ca-Alg beads' surface. Three different SDS concentrations (25, 50, & 100 mg/L) were prepared and treated with Ca-Alg beads for 1, 2, 4, 6, and 24 h. SDS binding yield reached equilibrium at the end of the 24 h, and the binding efficiencies of 25, 50, and 100 mg SDS/L were determined 84%, 72%, and 48%, respectively. The effect of pH between 2 and 10 was also investigated on oil adsorption. Maximum adsorption efficiency (77%) was obtained in the range of pH6-8. After determining the optimum pH value for oil adsorption, the effect of beads amount (2.5-30 g/L) was also investigated on oil removal efficiency. When the amount of beads increased from 2.5 to 30 g/L, the oil adsorption efficiency increased from 77% to 95%. It was also observed that the oil adsorption efficiency increased when the size of the beads decreased from 4 to 1mm. For the kinetic calculation, three different concentrations (250, 500, &1000 mg/L) of oily solution were prepared, and oil adsorption was investigated versus time. The kinetic studies for the adsorption of the oily solution using SDS functionalized Ca-Alg beads showed the second-order kinetics. When the initial oil concentration increased from 250 to 1000 mg/L, the amount of adsorbed oil molecules increased from 8.34 to 22.12 mg/g. Langmuir and Freundlich isotherm models were used to explain the relationship between adsorbent and adsorbate, and Langmuir isotherm was the most suitable model because of its high regression coefficient (r2 ) value. Column studies were also carried out, and it was concluded that the proposed adsorbent can be used effectively in the treatment of oily wastewater. PRACTITIONER POINTS: Although there are numerous adsorption studies and studies on the use of alginate beads in various fields in the literature, its use in oil treatment has not been found to our knowledge. The study aims to produce a selective adsorbent for the removal of oil from water by functionalizing the surface of the alginate beads with active agents. In conventional adsorption studies, pollutants are transported from liquid phase to solid phase. With the proposed new adsorbent material, oils will be specifically removed from wastewater and used as fuel. Thus, obtaining an organic origin adsorbent with high calorific value constitutes the original value of the study. In addition, no secondary pollutants will emerge after the adsorption process.

A complex unfolding pathway of α-helical membrane proteins in SDS-containing micelles

The thermodynamic and kinetic principles guiding folding of transmembrane (TM) proteins are still not very well understood, at least when compared with soluble proteins. However, there is a considerable interest in better understanding these processes, not just since membrane proteins are important drug targets. Membrane proteins constitute ∼25–30% of total proteins encoded in any organism, and many diseases are caused by alterations in TM protein structure and function ( 1 Wallin E. von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998; 7: 1029-1038 Crossref PubMed Scopus (1229) Google Scholar , 2 Marinko J.T. Huang H. Sanders C.R. et al. Folding and misfolding of human membrane proteins in health and disease: from single molecules to cellular proteostasis. Chem. Rev. 2019; 119: 5537-5606 Crossref PubMed Scopus (97) Google Scholar ). The thermodynamic stability of soluble proteins is classically studied via protein denaturation induced by heat or chaotropic salts, typically urea or guanidine hydrochloride, followed by refolding. Yet, TM proteins typically aggregate at increasing temperatures, preventing refolding, and as for in vitro studies, isolated TM proteins are analyzed when incorporated into a lipid bilayer or a detergent micelle, where individual TM helices are shielded from the aqueous environment. Consequently, whereas urea or GdnHCl can unfold extramembranous domains to disrupt TM contacts, the properties of the intimate solvent (here, the membrane or detergent micelles) have to be modified. Cys-labeling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes?Otzen et al.Biophysical JournalAugust 6, 2021In BriefEmpirically, α-helical membrane protein folding stability in surfactant micelles can be tuned by varying the mole fraction MFSDS of anionic (sodium dodecyl sulfate (SDS)) relative to nonionic (e.g., dodecyl maltoside (DDM)) surfactant, but we lack a satisfying physical explanation of this phenomenon. Cysteine labeling (CL) has thus far only been used to study the topology of membrane proteins, not their stability or folding behavior. Here, we use CL to investigate membrane protein folding in mixed DDM-SDS micelles. Full-Text PDF

Cys-labeling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes?

Empirically, α-helical membrane protein folding stability in surfactant micelles can be tuned by varying the mole fraction MFSDS of anionic (sodium dodecyl sulfate (SDS)) relative to nonionic (e.g., dodecyl maltoside (DDM)) surfactant, but we lack a satisfying physical explanation of this phenomenon. Cysteine labeling (CL) has thus far only been used to study the topology of membrane proteins, not their stability or folding behavior. Here, we use CL to investigate membrane protein folding in mixed DDM-SDS micelles. Labeling kinetics of the intramembrane protease GlpG are consistent with simple two-state unfolding-and-exchange rates for seven single-Cys GlpG variants over most of the explored MFSDS range, along with exchange from the native state at low MFSDS (which inconveniently precludes measurement of unfolding kinetics under native conditions). However, for two mutants, labeling rates decline with MFSDS at 0–0.2 MFSDS (i.e., native conditions). Thus, an increase in MFSDS seems to be a protective factor for these two positions, but not for the five others. We propose different scenarios to explain this and find the most plausible ones to involve preferential binding of SDS monomers to the site of CL (based on computational simulations) along with changes in size and shape of the mixed micelle with changing MFSDS (based on SAXS studies). These nonlinear impacts on protein stability highlights a multifaceted role for SDS in membrane protein denaturation, involving both direct interactions of monomeric SDS and changes in micelle size and shape along with the general effects on protein stability of changes in micelle composition.

Conformational flexibility and ligand binding properties of ovine β-lactoglobulin.

Ovine β‑lactoglobulin was characterized by spectroscopic (CD), calorimetric (ITC) and X-ray structural studies. The structure of ovine β‑lactoglobulin complex with decanol showed that tight packing of molecules in the crystalline phase enforces a distortion of protein flexible loops resulting in the formation of an asymmetric dimer. The loops surrounding β-barrel in ovine lactoglobulin possessed the same conformational flexibility as observed previously in other lactoglobulins and the change of their conformation regulates the access to the binding pocket. The structure of asymmetric dimer revealed a new region in β-barrel where ligand polar group can be located. These findings indicated protein adaptability to ligand dimensions and inter- and intramolecular interactions in the crystalline phase. Calorimetric and crystallographic studies provided the experimental evidence that ovine lactoglobulin is able to bind aliphatic ligands. Thermodynamic parameters of sodium dodecyl sulfate binding determined by ITC at pH 7.5 had Ka, ΔH, TΔS and ΔG values similar to those observed for bovine and caprine protein indicating the same mechanism of ligand binding.

Silk Fibroin-Sodium Dodecyl Sulfate Gelation: Molecular, Structural, and Rheological Insights.

A gelling agent is necessary to accelerate sol to gel transition in an aqueous solution of silk fibroin (SF), which otherwise takes several days to complete. In this paper, we investigate the mechanism of gelation of Bombyx mori SF by a model anionic surfactant, sodium dodecyl sulfate (SDS). Even though interactions between SDS and proteins have been extensively investigated, most of these studies have focused on globular proteins, which undergo denaturation. The interaction with a fibrous protein such as SF is different and results in an altered secondary structure leading to gelation. In this work, the concentration-dependent gelation process of the SF-SDS system is examined using rheology, SANS, FTIR, and NMR. We observed preferential binding of SDS to specific regions on the SF chain, which aids structural changes favoring β-sheet formation. We propose a mechanism for the accelerated sol-gel transition in the SF-SDS system.

Effect of Added Surfactant on Poly(Ethylenimine)-Assisted Gold Nanoparticle Formation.

In a variety of applications, functionalization of gold nanoparticles is needed to ensure adequate surface charge and hydrophobicity for their biodistribution, interparticle interactions, or self-organization. In the present paper, we provide an economic way for the synthesis of hydrophobized poly(ethylenimine) (PEI) capped gold nanoparticles at room temperature using sodium dodecyl sulfate (SDS). The approach is based on the controlled competition between the nucleation of gold nanophases within the PEI molecules and the SDS binding onto their amine groups. This can be achieved via utilizing the strongly irreversible nature of the association between the oppositely charged polymer and that of the surfactant molecules. Specifically, by varying the order and timing of SDS addition during the process of gold nanoassembly formation, the size distribution, the morphology, and the local hydrophobic environment of the produced Au-PEI/SDS nanohybrids can be tuned even at one composition of the system. The results may be further exploited for the preparation of noble metal nanoassemblies with controlled hydrophobicity and charge.

Molecular Modeling Investigation of the Interaction between Humicola insolens Cutinase and SDS Surfactant Suggests a Mechanism for Enzyme Inactivation.

One of the largest commercial applications of enzymes and surfactants is as main components in modern detergents. The high concentration of surfactant compounds usually present in detergents can, however, negatively affect the enzymatic activity. To remedy this drawback, it is of great importance to characterize the interaction between the enzyme and the surfactant molecules at an atomistic resolution. The protein enzyme cutinase from the thermophilic and saprophytic fungus called Humicola insolens (HiC) is a promising candidate for use in detergents thanks to its hydrolase activity targeting mostly biopolyesters (e.g., cutin). HiC is, however, inhibited by low concentrations of sodium dodecyl sulfate (SDS), an ubiquitous surfactant. In this work, we investigate the interaction between HiC and SDS using molecular dynamics simulations. Simulations of HiC dissolved in different aqueous concentrations of SDS show the interaction between HiC and SDS monomers, as well as the formation and dynamics of SDS micelles on the surface of the enzyme. These results suggest a mechanism of cutinase inhibition by SDS, which involves the nucleation of aggregates of SDS molecules on hydrophobic patches on the cutinase surface. Notably, a primary binding site for monomeric SDS is identified near the active site of HiC constituting a possible nucleation point for micelles and leading to the blockage of the entrance to the enzymatic site. Detailed analysis of the simulations allow us to suggest a set of residues from the SDS binding site on HiC to probe as engineered mutations aimed at reducing SDS binding to HiC, thereby decreasing SDS inhibition of HiC.

Cooperative Binding of Sodium Dodecyl Sulfate with Chitosan in Water–Alcohol Mixtures

The formation of polymer-colloid complexes of chitosan and anionic surfactant—sodium dodecyl sulfate—in water–alcohol mixtures is studied by potentiometry using ion-selective electrodes. The influence of the nature and content of organic cosolvent (methanol, ethanol, and 2-propanol) on the parameters of binding of surfactant with chitosan and the stability of complexes is discussed. The obtained data are analyzed in terms of the model of cooperative binding and pseudophase model. It is shown that addition of 10–20 vol % of ethanol and 2-propanol to aqueous solution intensifies cooperative binding of sodium dodecyl sulfate with chitosan, which leads to the decrease in the critical association concentration and increase in the parameters of cooperativity and stability of complexes.

Overcoming Surfactant-Induced Morphology Instability of Noncrosslinked Diblock Copolymer Nano-Objects Obtained by RAFT Emulsion Polymerization.

RAFT emulsion polymerization techniques including polymerization-induced self-assembly (PISA) and temperature-induced morphological transformation (TIMT) are widely used to produce noncrosslinked nano-objects with various morphologies. However, the worm, vesicle and lamellar morphologies produced by these techniques typically cannot tolerate the presence of added surfactants, thus limiting their potential applications. Herein we report the surfactant tolerance of noncrosslinked worms, vesicles, and lamellae prepared by RAFT emulsion polymerizations using poly(di(ethylene glycol) ethyl ether methacrylate-co-N-(2-hydroxypropyl) methacrylamide) (P(DEGMA-co-HPMA)) as a macromolecular chain transfer agent (macro-CTA). Significantly, these P(DEGMA-co-HPMA) nanoparticles are highly stable in concentrated solutions of surfactants (e.g., sodium dodecyl sulfate (SDS)). We also demonstrate that the surfactant tolerance is related to the limited binding of SDS to the main-chain of the P(DEGMA-co-HPMA) macro-CTA constituting the particle shell. This work provides new insight into the interactions between surfactants and thermoresponsive copolymers and expands the scope of RAFT emulsion polymerization techniques for the preparation of noncrosslinked and surfactant-tolerant nanomaterials.

Inhibition of Amyloid Aggregation of Bovine Serum Albumin by Sodium Dodecyl Sulfate at Submicellar Concentrations.

Sodium dodecyl sulfate (SDS), as an anionic surfactant, can induce protein conformational changes. Recent investigations demonstrated different effects of SDS on protein amyloid aggregation. In the present study, the effect of SDS on amyloid aggregation of bovine serum albumin (BSA) was evaluated. BSA transformed to β-sheet-rich amyloid aggregates upon incubation at pH7.4 and 65°C, as demonstrated by thioflavin T fluorescence, circular dichroism, and transmission electron microscopy. SDS at submicellar concentrations inhibited BSA amyloid aggregation with IC50 of 47.5µM. The inhibitory effects of structural analogs of SDS on amyloid aggregation of BSA were determined to explore the structure-activity relationship, with results suggesting that both anionic and alkyl moieties of SDS were critical, and that an alkyl moiety with chain length ≥10 carbon atoms was essential to amyloid inhibition. We attributed the inhibitory effect of SDS on BSA amyloid aggregation to interactions between the detergent molecule and the fatty acid binding sites on BSA. The bound SDS stabilized BSA, thereby inhibiting protein transformation to amyloid aggregates. This study reports for the first time that the inhibitory effect of SDS on albumin fibrillation is closely related to its alkyl structure. Moreover, the specific binding of SDS to albumin is the main driving force in amyloid inhibition. This study not only provides fresh insight into the role of SDS in amyloid aggregation of serum albumin, but also suggests rational design of novel anti-amyloidogenic reagents based on specific-binding ligands.

Triblock-Copolymer-Assisted Mixed-Micelle Formation Results in the Refolding of Unfolded Protein.

The present work reports a new strategy for triblock-copolymer-assisted refolding of sodium dodecyl sulfate (SDS)-induced unfolded serum protein human serum albumin (HSA) by mixed-micelle formation of SDS with poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) triblock copolymer EO20PO68EO20 (P123) under physiological conditions. The steady-state and time-resolve fluorescence results show that the unfolding of HSA induced by SDS occurs in a stepwise manner through three different phases of binding of SDS, which is followed by a saturation of interaction. Interestingly, the addition of polymeric surfactant P123 to the unfolded protein results in the recovery of ∼87% of its α-helical structure, which was lost during SDS-induced unfolding. This is further corroborated by the return of the steady-state and time-resolved fluorescence decay parameters of the intrinsic tryptophan (Trp214) residue of HSA to the initial nativelike condition. The isothermal titration calorimetry (ITC) data also substantiates that there is almost no interaction between P123 and the native state of the protein. However, the mixed-micelle formation, accompanied by substantial binding affinities, removes the bound SDS molecules from the scaffolds of the unfolded state of the protein. On the basis of our experiments, we conclude that the formation of mixed micelles between SDS and P123 plays a pivotal role in refolding the protein back to its nativelike state.

SDS-induced Peptide Conformational Changes: From Triglycyl-glycine to Amyloid-β Oligomers Associated with Alzheimer’s Disease

Sodium dodecyl sulfate (SDS) was introduced in polyacrylamide gel electrophoresis (PAGE) due to its capacity of helping proteins to become fully denatured and dissociated from each other. Numerous studies which have been undertaken, using electrospray ionization mass spectrometry (ESI–MS), reported on the process of peptide oligomerization. Many of these investigations have included tetraglycine (H2N–Gly–Gly–Gly–Gly–COOH; G4) as model peptide. The aim of this research is to investigate the effect of SDS on G4 oligomerization, and, especially, to emphasize the dismantling of oligomers under micellar conditions. In water, G4 peptide develops dimers and oligomers, which can also be evidenced in high proportion by MS in the gas phase. Although our results show that SDS is able to reduce the proportion of G4 oligomers, the aqueous G4-SDS system may contain G4 dimers, G4-SDS adducts alongside with the expected monomers and some alkaline metal adducts. The mechanism by which SDS disassembled G4 dimers, which includes sodium ion affinity toward negatively charged carboxyl and sulfonyl groups, was also discussed. Amyloid-β peptide1–40 conformation changed considerably and, especially, the proportion of α-helical populations increased upon SDS binding in a concentration-dependent manner. Molecular dynamics studies confirmed the tendency of Aβ molecules to form α-helical conformers, as the CD and FTIR studies showed.

Structural aspects of a protein-surfactant assembly: native and reduced States of human serum albumin.

The inherently present seventeen disulfide bonds of the circulatory protein, human serum albumin (HSA) provide the necessary structural stability. Various spectroscopic approaches were used to investigate the effect of reduction of these disulfide bonds and its binding with the anionic surfactant, sodium dodecyl sulfate (SDS). Based on several spectroscopic analyses, our investigations highlight the following interesting aspects: (1) HSA on reduction loses not only its tertiary structure but also a significant amount of secondary structure as well. However, the reduced state of the protein is not like the molten-globule, (2) this structural loss of the protein due to reduction is more prominent than that caused by higher SDS concentrations alone and can certainly be attributed to the role of disulfide bonds, (3) lower surfactant concentrations provide marginal structural rigidity to the native state of the protein, whereas, higher concentrations of SDS induces secondary structure to the reduced state of HSA, (4) the binding of SDS with both the native and reduced states of HSA, occurred in three distinct stages which was followed by a saturation stage. However, the nature of such binding is different for both the states as investigated by using the Stern-Volmer equations and estimating the thermodynamic parameters. Besides, in contrast to the native state, the reduced state of HSA shows that the lone tryptophan residue gets more buried. However, there occurs a sudden decrement in the lifetime of the tryptophan and the hydrodynamic diameter increases by twofold.

Comparing foam and interfacial properties of similarly charged protein–surfactant mixtures

The foam stability of protein–surfactant mixtures strongly depends on the charge of the protein and the surfactant, as well as on their mixing ratio. Depending on the conditions, the mixtures will contain free proteins, free surfactants and/or protein–surfactant complexes. To be able to compare different protein–surfactant mixtures, generic knowledge about the occurrence of each of these states and their relative contribution to foam stability is essential. In this work, the foam stability and interfacial properties of bovine serum albumin (BSA) mixed with sodium dodecyl sulphate (SDS) as well the binding of SDS to BSA as are studied at different molar ratios (MR). A comparison is made with β-lactoglobulin (BLG) mixed with SDS. Both proteins and SDS are negatively charged at pH 7. The foam stability in the presence of small amounts (up to MR 1) of SDS is half the value of the pure protein solutions. The foam stability for both protein surfactant mixtures reaches a minimum at MR 20. A further increase of the MR leads to an increase of foam stability. The foam stability of BLG–SDS at MR >20 follows the foam stability of pure SDS solutions at equivalent concentrations, while BSA–SDS mixtures have an offset and begin to increase from MR >50. This behaviour was also reflected in the surface pressure and complex dilatational elastic moduli, and could be linked to the binding of the surfactant to the proteins. Both proteins bind SDS at high and low affinity binding sites. BSA's high affinity binding sites have a binding stoichiometry of 5.5 molSDS/molprotein, and BLG's high affinity binding site has a stoichiometry of 0.8 molSDS/molprotein (determined by isothermal titration calorimetry). Binding to the low affinity binding sites, occurs with a binding ratio, leading to an accumulation of free surfactants. While the basic mechanisms underlying the foam properties of mixed systems are not explained in detail by this approach, the foam stability plots of both protein surfactant mixtures could be superimposed using the concentration of free SDS.

Polymeric Suppression of Dopant‐Enhanced Surfactant Supramicellar Assemblies

Certain hydrophobic dopants in surfactant solutions cause massive “supramicellar assemblies” (SAs) to form near the critical micelle concentration (CMC), characterized by a light‐scattering peak (LSP). The SAs are large, dynamic, metastable nanostructures composed of surfactant/dopant. Here, a water‐soluble polymer, poly(vinylpyrollidone) (PVP) suppresses SA formation in sodium dodecyl sulfate (SDS) solutions doped with dodecanol, but increases solution instability. Binding of SDS to PVP is stronger than micellization in the LSP regime, reflected in a decreased SA population and a dramatic reduction and inversion of Rayleigh scattering IR as [PVP] increases, since SAs are much more massive than PVP/SDS association structures. Above the LSP regime, SAs no longer exist and thus IR must re‐establish its order, increasing with increasing [PVP]. This causes a cross‐over in IR vs [SDS] with an “iso‐scattering point,” where IR converges at a specific [SDS]. Weak LSP suppression is found using dodecyl tri­ethyl ammonium bromide (DTAB). Poly(ethylene oxide) (PEO)’s effect is small compared with PVP. image

Poly(amidoamine) and Poly(propyleneimine) Dendrimers Show Distinct Binding Behaviors with Sodium Dodecyl Sulfate: Insights from SAXS and NMR Analysis

We investigate the interactions of generation 3 (G3) poly(amidoamine) (PAMAM) and G3 poly(propylenimine) (PPI) dendrimers with sodium dodecyl sulfate (SDS) in aqueous solution. Size and structure of the dendrimer-SDS aggregates as a function of SDS/dendrimer molar ratio were revealed by SAXS and NMR. G3 PAMAM has a relatively open and dense-core structure, while G3 PPI with the same number of surface amine groups possesses a compact and uniform structure. Upon addition of SDS, much more SDS monomers were encapsulated in the interior of PPI rather than in PAMAM. More significant size increase in PAMAM-SDS aggregate is observed at low SDS concentrations, due to the binding of SDS on PAMAM surface and further assembly into larger supramolecular structures. Both noncooperative and cooperative binding of SDS on G3 PPI surface are observed, while only noncooperative binding is proposed on G3 PAMAM, due to its open surface and large surface group distance. The size of the PPI-SDS complex is larger than that of PAMAM-SDS at higher SDS concentrations. Within the investigated SDS concentrations, SDS exhibits much stronger interactions with G3 PPI than with G3 PAMAM. These results provide new insights into dendrimer-surfactant interactions and explain why PPI is much more cytotoxic than PAMAM.