Low Detergent Concentrations Research Articles

Preparing liposomes through frame guided assembly with high-loading functional nucleic acids.

Recently, a frame guided assembly (FGA) has been demonstrated as a robust tool to prepare liposomes with customized morphologies. However, the potential application of FGA liposomes in delivering nucleic acid drugs is still limited by the low payload. In this study, by systemically investigating the correlation between the leading hydrophobic group (LHG) density and the initial detergent concentration, it has been demonstrated that frames with a low LHG density, which may facilitate the increase of the load of the nucleic acid drug, could be guided to form liposomes at low initial detergent concentrations. By capitalizing on this phenomenon, FGA liposomes with a high loading of ASO/siRNA have been successfully prepared and applied to treat pathogenic genes.

Response Surface Methodology for Optimization Membrane Disruption Using Thermolysis in Lipase Lk2 and Lk3

Lk2 and Lk3 were thermostable recombinant lipase and highly expressed in Escherichia coli BL21 (DE3). However, Lk2 and Lk3 accumulated as an inclusion body. To further characterize both recombinant lipases, the soluble enzyme must be obtained first. This study aimed to optimize the disruption of the cell membrane in order to obtain soluble and active lipases. The effects of temperature lysis, pH, and SDS concentration on lipolytic activity Lk2 and Lk3 were investigated using a three-factor Box-Behnken design response surface methods. The optimum condition for the temperature variables at 50°C, pH 8, and 0.34% SDS which gave a lipolytic activity of 0.9 U for Lk2. Meanwhile, Lk3 lipolytic activity of 0.9 U obtained at the temperature of 50°C, pH 8, and 0.1% SDS. This result showed efficient one-step membrane disruption methods using thermolysis with addition of a low concentration of detergent at pH 8. The methods used were effective and applicable in the production of active and soluble thermostable recombinant lipase.

Effect of Laundry Parameters on Micro Fiber Loss during Washing and Its Correlation with Carbon Footprint

ABSTRACT Nowadays, with the fast growing fashion trend, a surge in fashion demand is there. In future, this demand may expect to increase further in multifold. A particular apparel design is not being used for longer period due to the fast changing fashion and this will cause the shedding of micro fibers. Most of the clothes are blends of polyester (synthetic fibers) and cotton (natural fibers) (P/C: 70:30) and when wash these clothes, the shed fibers coming out and pollute the environment. These shed fibers poses a major threat to aquatic and terrestrial ecosystem and also human health. The experimental study was performed on washing machine, considering three parameters – time (duration of washing), detergent concentration of washing liquor and mechanical stress level, to study the shed fibers. The study shows that the major contributing parameter causing more fiber loss was found to be 1% (lower) detergent concentration, this was perhaps due to decrease in inter-fiber friction. On the other hand, high micro fiber loss was achieved at higher mechanical stress and processing time. Also, the increased mechanical stress, increases the friction between the fabric and drum. Thus increases the electricity consumption. The combined impact of time and detergent concentration, increase the fiber loss. With higher processing time and lower detergent concentration, increases the micro fiber loss. The increased processing time and mechanical stress increases the micro fiber shedding and electricity consumption.

Purification of Crimean Congo Hemorrhagic Fever Virus (CCHFV) Nucleocapsid Protein Using Detergent Gradient and Free Thawing.

Protein aggregation remains a major challenge in the purification of recombinant proteins in both eukaryotic and prokaryotic expression systems. One such protein is the nucleocapsid protein of Crimean Congo Hemorrhagic fever virus (CCHFV), which has high aggregation tendency and rapidly precipitates upon purification by NiNTA chromatography. Using the detergent gradient purification approach reported here, the freshly purified protein by NiNTA chromatography was mixed with the dilution buffer containing a high detergent concentration, followed by overnight freezing at -80 °C. Thawing the resulting mixture at room temperature triggered the formation of a detergent concentration gradient containing the active protein in the low detergent concentration zone towards the top of the gradient. The inactive aggregates migrated to the high detergent concentration zone towards the bottom of the gradient. The method prevented further aggregation and retained the activity of the native protein despite numerous freeze-thaw cycles. This simple approach creates an appropriate microenvironment towards the top of the gradient for correctly folded proteins, and it prevents aggregation by rapidly separating the preformed early aggregates from the correctly folded protein in the mixture. This unique approach will be of potential importance for the biotechnological industry, as well as other fields of protein biochemistry that routinely purify recombinant proteins and face the challenges of protein aggregation. Graphical abstract.

A novel approach for the purification of aggregation prone proteins.

The protein aggregation is one of the major challenges of the biotechnological industry, especially in the areas of development and commercialization of successful protein-based drug products. The inherent high aggregation tendency of proteins during various manufacturing processes, storage, and administration has significant impact upon the product quality, safety and efficacy. We have developed an interesting protein purification approach that separates the functionally active protein from inactive aggregates using a detergent concentration gradient. The C-terminally His tagged nucleocapsid protein of Crimean Congo Hemorrhagic fever virus (CCHFV) has high aggregation tendency and rapidly precipitates upon purification by NiNTA chromatography. Using the new purification approach reported here, the freshly purified protein by NiNTA chromatography was further processed using a detergent gradient. In this new purification approach the active protein is retained in the low detergent concentration zone while the inactive aggregates are promptly removed by their rapid migration to the high detergent concentration zone. The method prevented further aggregation and retained the RNA binding activity in the native protein despite numerous freeze thaw cycles. This simple approach prevents protein aggregation by rapidly separating the preformed early aggregates and creating the appropriate microenvironment for correctly folded proteins to retain their biological activity. It will be of potential importance to the biotechnological industry and other fields of protein biochemistry that routinely face the challenges of protein aggregation.

A decellularized porcine pulmonary valved conduit embedded with gelatin.

To prepare a tissue-engineered pulmonary valved conduit (PVC) with good tensile strength and biocompatibility. Sixty adult porcine PVCs were used to determine the optimal decellularization time. Five juvenile porcine decellularized PVCs and five juvenile porcine crosslinked PVCs were subsequently prepared according to the optimized decellularization and crosslinking methods. All PVCs were implanted into juvenile sheep for 8months and then were harvested for staining. With a low concentration of detergent (0.25% Triton X-100+0.25% sodium deoxycholate), the decellularization effect on porcine PVCs was complete by 24hours, and there was minimal damage to the matrix. Gelatin embedding and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) crosslinking improved the biomechanical properties of decellularized PVCs and reduced their immunogenicity. After implantation, the diameter and thickness of the PVCs in the decellularized and crosslinked groups increased significantly. In both groups, the conduits were unobstructed, with soft and smooth inner walls and without thrombosis, ulceration or neoplasia. The valves slightly degenerated with mild to moderate regurgitation. CD31-positive endothelial cells were visible on the inner surface of the conduits and valves. Scattered smooth muscle actin-positive cells were found in the middle layer of the conduit. The percentage of CD4- and CD68-positive cells and the calcium content were highest in decellularized porcine PVCs and lowest in ovine PVCs. The percentage of the matrix that was laminin-positive in decellularized and crosslinked porcine PVCs was lower than it was in ovine PVCs. Gelatin-embedded and EDC-crosslinked porcine PVCs can be "hosted" in sheep, with good biocompatibility, growth potential, and reduced calcification.

Cryo-EM grid optimization for membrane proteins

SummaryCryo-EM grid preparation is an important bottleneck in protein structure determination, especially for membrane proteins, typically requiring screening of a large number of conditions. We systematically investigated the effects of buffer components, blotting conditions and grid types on the outcome of grid preparation of five different membrane protein samples. Aggregation was the most common type of problem which was addressed by changing detergents, salt concentration or reconstitution of proteins into nanodiscs or amphipols. We show that the optimal concentration of detergent is between 0.05 and 0.4% and that the presence of a low concentration of detergent with a high critical micellar concentration protects the proteins from denaturation at the air-water interface. Furthermore, we discuss the strategies for achieving an adequate ice thickness, particle coverage and orientation distribution on free ice and on support films. Our findings provide a clear roadmap for comprehensive screening of conditions for cryo-EM grid preparation of membrane proteins.

Ex-vivo recellularisation and stem cell differentiation of a decellularised rat dental pulp matrix

Implementing the principles of tissue engineering within the clinical management of non-vital immature permanent teeth is of clinical interest. However, the ideal scaffold remains elusive. The aim of this work was to assess the feasibility of decellularising rat dental pulp tissue and evaluate the ability of such scaffold to support stem cell repopulation. Rat dental pulps were retrieved and divided into control and decellularised groups. The decellularisation protocol incorporated a low detergent concentration and hypotonic buffers. After decellularisation, the scaffolds were characterised histologically, immunohistochemistry and the residual DNA content quantified. Surface topography was also viewed under scanning electron microscopy. Biocompatibility was evaluated using cytotoxicity assays utilising L-929 cell line. Decellularised scaffolds were recellularised with human dental pulp stem cells up to 14 days in vitro. Cellular viability was assessed using LIVE/DEAD stain kit and the recellularised scaffolds were further assessed histologically and immunolabelled using makers for odontoblastic differentiation, cytoskeleton components and growth factors. Analysis of the decellularised scaffolds revealed an acellular matrix with histological preservation of structural components. Decellularised scaffolds were biocompatible and able to support stem cell survival following recellularisation. Immunolabelling of the recellularised scaffolds demonstrated positive cellular expression against the tested markers in culture. This study has demonstrated the feasibility of developing a biocompatible decellularised dental pulp scaffold, which is able to support dental pulp stem cell repopulation. Clinically, decellularised pulp tissue could possibly be a suitable scaffold for use within regenerative (reparative) endodontic techniques.

Truncation of C-Terminal Intrinsically Disordered Region of Mycobacterial Rv1915 Facilitates Production of "Difficult-to-Purify" Recombinant Drug Target.

Availability of purified drug target is a prerequisite for its structural and functional characterization. However, aggregation of recombinant protein as inclusion bodies (IBs) is a common problem during the large scale production of overexpressed protein in heterologous host. Such proteins can be recovered from IB pool using some mild solubilizing agents such as low concentration of denaturants or detergents, alcohols and osmolytes. This study reports optimization of solubilization buffer for recovery of soluble and biologically active recombinant mycobacterial Rv1915/ICL2a from IBs. Even though the target protein could be solubilized successfully with mild agents (sarcosine and βME) without using denaturants, it failed to bind on Ni-NTA resin. The usual factors such as loss of His6-tag due to proteolysis, masking of the tag due to its location or protein aggregation were investigated, but the actual explanation, provided through bioinformatics analysis, turned out to be presence of intrinsically disordered protein regions (IDPRs) at the C-terminus. These regions due to their inability to fold into ordered structure may lead to non-specific protein aggregation and hence reduced binding to Ni-NTA affinity matrix. With this rationale, 90 residues from the C-terminal of Rv1915/ICL2 were truncated, the variant successfully purified and characterized for ICL and MICL activities, supporting the disordered nature of Rv1915/ICL2a C-terminal. When a region that has definite structure associated in some mycobaterial strains such as CDC 1551 and disorder in others for instance Mycobacterium tuberculosis H37Rv, it stands to reason that larger interface in the later may have implication in binding to other cellular partner.

A study of the influence of temperature and detergent concentration on the removal of lipstick stains using air‐supersaturated water, where fine bubbles are generated by ultrasonic stimulation

AbstractThe formation of fine bubbles with a diameter between 10 and 20 μm was observed upon the passage of air‐supersaturated water, in which air is pressurized and dissolved, through a water passage in which supersonic stimulation was given to the water. It was confirmed that the inside diameter of the fine bubbles increases as the distance from the ultrasonic stimulation point becomes greater. In verifying the efficiency of cleaning a lipstick stain, it was shown that by using water containing fine bubbles, there is a possibility of obtaining a cleaning efficiency almost equivalent to that achieved by cleaning with water of a high temperature or with a high concentration of detergent, even at a low temperature, with low detergent concentration. It was shown that the efficiency of cleaning the oil components, which were made easily soluble in water, had become extremely high, when using water containing fine bubbles. In conditions where the melting of the oil component itself is not accelerated (that is, at a low temperature, without using detergents), the cleaning efficiency of water containing fine bubbles tended to be increased compared with that of water not containing fine bubbles.

In Vitro Analysis of Histology, Mechanics, and Safety of Radiation-free Pre-hydrated Human Acellular Dermal Matrix.

PurposeAcellular dermal matrix (ADM) supports tissue expanders or implants in implant-based breast reconstruction. The characteristics of ADM tissue are defined by the manufacturing procedure, such as decellularization, preservation, and sterilization, and are directly related to clinical outcomes. This study aimed to compare the properties of a new pre-hydrated-ADM (H-ADM-low) obtained using a decellularization reagent reduction process with a low concentration of detergent with those of radiation-sterilized H-ADM and freeze-dried ADM (FD-ADM).MethodsADMs were evaluated in terms of structure, mechanical quality, and cytotoxicity using histochemical staining, tensile strength testing, and in vitro cell viability analysis.ResultsThe tissue structure of H-ADM-low (CGDERM ONE-STEP) was similar to that of native skin despite complete decellularization. By contrast, in FD-ADM, the tissue structure was damaged by the freeze-drying process, and radiation-sterilized H-ADM showed a compact fibrillar arrangement. Furthermore, matrix components such as collagen and elastin were preserved in H-ADM-low, whereas a loss of elastin fibers with fragmented distribution was observed in radiation-sterilized H-ADMs. H-ADM-low's tensile strength (58.84 MPa) was significantly greater than that of FD-ADM (38.60 MPa) and comparable with that of radiation-sterilized H-ADMs. The residual detergent content in H-ADM-low (47.45 mg/L) was 2.67-fold lower than that of H-ADM decellularized with a conventional detergent concentration (126.99 mg/mL), and this finding was consistent with the cell viability results (90.7% and 70.7%, respectively), indicating that H-ADM-low has very low cytotoxicity.ConclusionsH-ADM-low produced through aseptic processes retains the original tissue structure, demonstrates excellent mechanical properties, and does not affect cell viability. Therefore, this newer H-ADM is suitable for use in implant-based breast reconstruction.

Solubilization of inclusion body proteins using low and very low concentrations of chemicals: implications of novel combined chemical treatment designs in enhancement of post‐solubilization target protein purity and biological activity

AbstractBACKGROUNDSolubilization of inclusion body (IB) proteins by conventional methods (i.e. high concentrations of denaturants such as chaotropes) is a challenging process due to denaturation of the native‐like secondary structures and subsequently low recovery into bioactive forms. The main objective of this work was to study the effect of a range of chemicals at low and very low concentrations on the solubilization of IB proteins produced in Escherichia coli and the enhancement of the target protein biological activity subsequent to refolding.RESULTSPerformance of chemical combinations at low and very low concentrations through the solubilization process of recombinant streptokinase (rSK) from IBs isolated from E. coli was appraised based on values pertinent to three parameters including target protein solubilization yield, purity and biological activity. In comparison with the conventional IBs' solubilization method (i.e. 4 mol L‐1 urea), combinations of 0.5–1 mol L‐1 urea with very low to low concentrations (0.05–1%) of detergents resulted in considerable target protein solubilization (by 100%), very high post‐solubilization target protein purities (up to 100%) and biological activities (up by 360%).CONCLUSIONOwing to the improvements in the abovementioned integral parameters, these chemical treatments are good candidates to be considered for more efficient and cost‐effective recovery of recombinant target proteins from IBs. © 2017 Society of Chemical Industry

Microcosm trial of the use of detergent for mitigation of crude oil toxicity for optimal growth of maize (<i>Zea mays</i>, L)

Study on the use of detergent as an ameliorating agent in crude oil polluted soil on hydrocarbon reduction and optimal growth of maize was carried out at the Centre for Ecological Studies, University of Port Harcourt. Pollution level of 3% w/v was remediated with 20 g detergent and 40 g detergent alongside a control (polluted soil without amendment). The amended soil was allowed for 4 weeks before maize seeds were planted in them. Soil total hydrocarbon content (THC) was determined at initial and end of the experiment. Measurements of growth parameters of maize were done monthly for three (3) months. Significant reduction in THC was observed in the treatment soils in the order of 20 g detergent (44.2%)> control (28.0%) > 40 g detergent (19.9%). Maize parameters such as germination, plant height, root length, leaf number, leaf area, fresh and dry weights and chlorophyll content showed significant (P=0.05) increase in 20 g detergent treatment than 40 g detergent and control treatments, except in moisture content (%) and shoot/root ratio which recorded highest level in the 40 g detergent. Therefore, low concentration of detergent is effective for the remediation of crude oil polluted soil for optimal growth performance of maize. Keywords: detergent, crude oil, toxicity, remediation, maize, hydrocarbon

Biological recovery and properties of poly(3-hydroxybutyrate) from Cupriavidus necator H16

Abstract In the present study, we observed that laboratory rats readily consumed lyophilized cells of Cupriavidus necator H16 cultivated using palm oil containing 39 wt% poly(3-hydroxybutyrate) [P(3HB)] as sole diet source. The test animals excreted whitish fecal pellets containing 82–97 wt% P(3HB). The remaining impurities could be easily removed by washing the pellets with water and/or low concentrations of detergent, which resulted in P(3HB) granules of a high purity. The molecular masses and thermal properties of P(3HB) obtained by this method were almost similar to P(3HB) extracted from bacterial cells using chloroform. The method reported here is simple and eliminates the need for solvents and strong chemicals, thus resulting in P(3HB) production that is more ecofriendly.

Isolation of Nuclei.

The isolation of nuclei is often the first step in studying processes such as nuclear-cytoplasmic shuttling, subcellular localization of proteins, and protein-chromatin or nuclear protein-protein interactions in response to diverse stimuli. Therefore, rapidly obtaining nuclei from cells with relatively high purity and minimal subcellular contamination, protein degradation, or postharvesting modification is highly desirable. Historically, the isolation of nuclei involved a homogenization step followed by centrifugation through high-density glycerol or sucrose. Although clean nuclei with little cytoplasmic contamination can be prepared using this method, it is typically time consuming and can allow protein degradation, protein modification, and leaching of components from the nuclei to occur. We have developed a rapid and simple fractionation method that is based on the selective dissolution of the cytoplasmic membrane (but not the nuclear membrane) using a low concentration of a nonionic detergent and rapid centrifugation steps. Here we describe important considerations when isolating nuclei from cells, introduce our rapid method, and compare this method to a more traditional protocol for isolating nuclei, noting the strengths and limitations of each approach.

Novel extracellular medium-chain-length polyhydroxyalkanoate depolymerase from Streptomyces exfoliatus K10 DSMZ 41693: a promising biocatalyst for the efficient degradation of natural and functionalized mcl-PHAs.

Cloning and biochemical characterization of a novel extracellular medium-chain-length polyhydroxyalkanoate (mcl-PHA) depolymerase from Streptomyces exfoliatus K10 DSMZ 41693 are described. The primary structure of the depolymerase (PhaZSex2) includes the lipase consensus sequence (serine-histidine-aspartic acid) which is known for serine hydrolases. Secondary structure analysis shows 7.9 % α-helix, 43.9 % β-sheet, 19.4 % β-turns, and 31.2 % random coil, suggesting that this enzyme belongs to the α/β hydrolase fold family, in agreement with other PHA depolymerases and lipases. The enzyme was efficiently produced as an extracellular active form in Rhodococcus and purified by two consecutive hydrophobic chromatographic steps. Matrix-assisted laser desorption-time-of-flight (MALDI-TOF) analysis of the purified enzyme revealed a monomer of 27.6 kDa with a midpoint transition temperature of 44.2 °C. Remarkably, the activity is significantly enhanced by low concentrations of nonionic and anionic detergents and thermal stability is improved by the presence of 10 % glycerol. PhaZSex2 is an endo-exohydrolase that cleaves both large and small PHA molecules, producing (R)-3-hydroxyoctanoic acid monomers as the main reaction product. Markedly, PhaZSex2 is able to degrade functionalized polymers containing thioester groups in the side chain (PHACOS), releasing functional thioester-based monomers and oligomers demonstrating the potentiality of this novel biocatalyst for the industrial production of enantiopure (R)-3-hydroxyalkanoic acids.

Investigating Bax subcellular localization and membrane integration.

Bax is a pivotal effector of apoptosis responsible for permeabilization of the mitochondrial outer membrane (MOM). A key event in mitochondrial damage is the translocation of Bax from the cytosol to the MOM. A simple and effective method for assessing the cytosol vs. mitochondrial localization of Bax is digitonin fractionation, which uses a low concentration of detergent to permeabilize the plasma membrane without damaging intracellular membranes. This allows separation of the cytosol (light membranes) from the heavy membranes (with mitochondria and nuclei) by centrifugation. Localization of Bax can then be assessed by immunoblotting. To further differentiate membrane-integrated Bax from that which is peripherally associated, carbonate extraction of the membrane fraction can be performed before immunoblotting. Treatment of membranes at high pH disrupts protein-protein interactions, whereas protein-lipid interactions are largely retained, although membrane integrity is lost.

A quantitative assessment method for Ascaris eggs on hands.

The importance of hands in the transmission of soil transmitted helminths, especially Ascaris and Trichuris infections, is under-researched. This is partly because of the absence of a reliable method to quantify the number of eggs on hands. Therefore, the aim of this study was to develop a method to assess the number of Ascaris eggs on hands and determine the egg recovery rate of the method. Under laboratory conditions, hands were seeded with a known number of Ascaris eggs, air dried and washed in a plastic bag retaining the washing water, in order to determine recovery rates of eggs for four different detergents (cationic [benzethonium chloride 0.1% and cetylpyridinium chloride CPC 0.1%], anionic [7X 1% - quadrafos, glycol ether, and dioctyl sulfoccinate sodium salt] and non-ionic [Tween80 0.1% -polyethylene glycol sorbitan monooleate]) and two egg detection methods (McMaster technique and FLOTAC). A modified concentration McMaster technique showed the highest egg recovery rate from bags. Two of the four diluted detergents (benzethonium chloride 0.1% and 7X 1%) also showed a higher egg recovery rate and were then compared with de-ionized water for recovery of helminth eggs from hands. The highest recovery rate (95.6%) was achieved with a hand rinse performed with 7X 1%. Washing hands with de-ionized water resulted in an egg recovery rate of 82.7%. This washing method performed with a low concentration of detergent offers potential for quantitative investigation of contamination of hands with Ascaris eggs and of their role in human infection. Follow-up studies are needed that validate the hand washing method under field conditions, e.g. including people of different age, lower levels of contamination and various levels of hand cleanliness.

Conformational changes induced by detergents during the refolding of chemically denatured cysteine protease ppEhCP-B9 from Entamoeba histolytica

EhCP-B9, a cysteine protease (CP) involved in Entamoeba histolytica virulence, is a potential target for disease diagnosis and drug design. After purification from inclusion bodies produced in Escherichia coli, the recombinant EhCP-B9 precursor (ppEhCP-B9) can be refolded using detergents as artificial chaperones. However, the conformational changes that occur during ppEhCP-B9 refolding remain unknown. Here, we comprehensively describe conformational changes of ppEhCP-B9 that are induced by various chemical detergents acting as chaperones, including non-ionic, zwitterionic, cationic and anionic surfactants. We monitored the effect of detergent concentration and incubation time on the secondary and tertiary structures of ppEhCP-B9 using fluorescence and circular dichroism (CD) spectroscopy. In the presence of non-ionic and zwitterionic detergents, ppEhCP-B9 adopted a β-enriched structure (ppEhCP-B9β1) without proteolytic activity at all detergent concentrations and incubation times evaluated. ppEhCP-B9 also exhibits a β-rich structure in low concentrations of ionic detergents, but at concentrations above the critical micelle concentration (CMC), the protein acquires an α+β structure, similar to that of papain but without proteolytic activity (ppEhCP-B9α+β1). Interestingly, only within a narrow range of experimental conditions in which SDS concentrations were below the CMC, ppEhCP-B9 refolded into a β-sheet rich structure (ppEhCP-B9β2) that slowly transforms into a different type of α+β conformation that exhibited proteolytic activity (ppEhCP-B9α+β2) suggesting that enzymatic activity is gained as slow transformation occurs.

Cryo-TEM structural analysis of conjugated nonionic engineered-micelles.

Conjugated engineered-micelles, i.e. micelles that are composed of nonionic detergents and hydrophobic chelators and subsequently conjugated in the presence of divalent metal ions, have been shown to be remarkably suited to the task of membrane protein purification, maintaining these proteins in their native state. They also efficiently solubilize highly hydrophobic antibiotics. To date, however, the morphological changes induced in the initially spherical or ellipsoidal micelles by conjugation have not been explored. In this study, the very rapid sample-vitrification protocol of cryogenic transmission electron microscopy (cryo-TEM) has been used to capture structural transformations that engineered-micelles undergo immediately following conjugation with the [(bathophenanthroline)3:Fe(2+)] hydrophobic complex. We found that condensed thread-like aggregates are formed when the detergents used are: octyl β-D-glucopyranoside (OG), octyl β-D-thioglucopyranoside (OTG) or pentaethylene glycol monododecyl ether (C12E5). However, with β-D-maltoside (DM), n-dodecyl β-D-maltoside (DDM) or β-D-glucopyranoside (DDG), lamellar structures, some of which appear as stacked lamellae or multilamellar vesicles (MLV's), were observed. Such architectural changes occur under very mild conditions i.e. low detergent concentration, no temperature or pH alterations and without the presence of any precipitants such as PEG or ammonium sulfate.