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Molecules (Basel, Switzerland) Mar 2022Products designed to cleanse the skin commonly do so through surfactant action, which leads to the lowering of the surface tension of the skin to facilitate the removal... (Review)
Review
Products designed to cleanse the skin commonly do so through surfactant action, which leads to the lowering of the surface tension of the skin to facilitate the removal of dirt from its surface. Skin cleansers generally come in one of two types: soap-based and synthetic detergents, or syndets. While the latter can effectively maintain the native skin structure, function and integrity, the former tends to negatively affect the skin by causing barrier disruption, lipid dissolution and pH alteration. Despite this, soap is still often preferred, possibly due to the negative connotations around anything that is not perceived as 'natural'. It is, therefore, important that the science behind cleansers, especially those designed for the maintenance of healthy skin and the management of common skin conditions such as eczema, be understood by both formulators and end-users. Here, we carefully weigh the advantages and disadvantages of the different types of surfactant-the key ingredient(s) in skin cleansers-and provide insight into surfactants' physicochemical properties, biological activity and potential effects. Fine-tuning of the complex characteristics of surfactants can successfully lead to an 'optimal' skin cleanser that can simultaneously be milder in nature, highly effective and beneficial, and offer minimal skin interference and environmental impact.
Topics: Detergents; Skin; Skin Care; Soaps; Surface-Active Agents
PubMed: 35335373
DOI: 10.3390/molecules27062010 -
Allergy Jan 2023Eosinophilic esophagitis (EoE) is a chronic allergic disease associated with type 2 inflammation and epithelial barrier dysfunction. The etiology is unknown, however,...
BACKGROUND
Eosinophilic esophagitis (EoE) is a chronic allergic disease associated with type 2 inflammation and epithelial barrier dysfunction. The etiology is unknown, however, genetic heritability studies suggest environmental factors play a key role in pathogenesis. Detergents, such as sodium dodecyl sulfate (SDS), are common ingredients in household products such as dish soap and toothpaste. We hypothesized detergent exposure decreases epithelial barrier function and induces esophageal inflammation.
METHODS
Immortalized esophageal epithelial cells (EPC2) were cultured in air-liquid interface (ALI) and exposed to SDS. Barrier function/activity was assessed by transepithelial electrical resistance (TEER), FITC-dextran flux, and RT-PCR. Additionally, SDS-treated mouse esophageal organoids were evaluated for morphology. To investigate the effects of SDS in vivo, mice were treated with 0.5% SDS in drinking water for 14 days. Esophagi were assessed by gross morphology, histopathology, protein expression, and bulk RNA sequencing.
RESULTS
When EPC2 cells were exposed to SDS (5 μg/ml) for 96 h, TEER decreased (p = 0.03), and FITC-dextran flux increased (p = 0.0002). mRNA expression of IL-33 increased 4.5-fold (p = 0.02) at 6 h and DSG1 decreased (p < 0.0001) by 72 h. Disrupted epithelial integrity was noted in SDS-treated esophageal organoids. When mice were exposed to SDS, they showed increased esophageal width, chemokine, and metalloprotease levels. Mice treated with SDS also showed increased IL-33 protein expression, basal zone hyperplasia, CD4 cell infiltration, and esophageal eosinophilia. RNA sequencing revealed upregulation of immune response pathway genes.
CONCLUSION
Exposure to SDS decreases esophageal barrier integrity, stimulates IL-33 production, and promotes epithelial hyperplasia and tissue eosinophilia. Detergents may be a key environmental trigger in EoE pathogenesis.
Topics: Animals; Mice; Detergents; Eosinophilic Esophagitis; Epithelial Cells; Hyperplasia; Inflammation; Interleukin-33
PubMed: 35899466
DOI: 10.1111/all.15457 -
Biochemical Society Transactions Jun 2021Membrane proteins play vital roles in living organisms, serving as targets for most currently prescribed drugs. Membrane protein structural biology aims to provide... (Review)
Review
Membrane proteins play vital roles in living organisms, serving as targets for most currently prescribed drugs. Membrane protein structural biology aims to provide accurate structural information to understand their mechanisms of action. The advance of membrane protein structural biology has primarily relied on detergent-based methods over the past several decades. However, detergent-based approaches have significant drawbacks because detergents often damage the native protein-lipid interactions, which are often crucial for maintaining the natural structure and function of membrane proteins. Detergent-free methods recently have emerged as alternatives with a great promise, e.g. for high-resolution structure determinations of membrane proteins in their native cell membrane lipid environments. This minireview critically examines the current status of detergent-free methods by a comparative analysis of five groups of membrane protein structures determined using detergent-free and detergent-based methods. This analysis reveals that current detergent-free systems, such as the styrene-maleic acid lipid particles (SMALP), the diisobutyl maleic acid lipid particles (DIBMALP), and the cycloalkane-modified amphiphile polymer (CyclAPol) technologies are not better than detergent-based approaches in terms of maintenance of native cell membrane lipids on the transmembrane domain and high-resolution structure determination. However, another detergent-free technology, the native cell membrane nanoparticles (NCMN) system, demonstrated improved maintenance of native cell membrane lipids with the studied membrane proteins, and produced particles that were suitable for high-resolution structural analysis. The ongoing development of new membrane-active polymers and their optimization will facilitate the maturation of these new detergent-free systems.
Topics: Cell Membrane; Cryoelectron Microscopy; Detergents; Lipid Bilayers; Membrane Lipids; Membrane Proteins; Nanoparticles; Polymers; Protein Binding; Protein Conformation
PubMed: 34110369
DOI: 10.1042/BST20201080 -
Archives of Biochemistry and Biophysics Aug 2017Membrane proteins present a challenge for structural biology. In this article, we review some of the recent developments that advance the application of NMR to membrane... (Review)
Review
Membrane proteins present a challenge for structural biology. In this article, we review some of the recent developments that advance the application of NMR to membrane proteins, with emphasis on structural studies in detergent-free, lipid bilayer samples that resemble the native environment. NMR spectroscopy is not only ideally suited for structure determination of membrane proteins in hydrated lipid bilayer membranes, but also highly complementary to the other principal techniques based on X-ray and electron diffraction. Recent advances in NMR instrumentation, spectroscopic methods, computational methods, and sample preparations are driving exciting new efforts in membrane protein structural biology.
Topics: Detergents; Humans; Lipid Bilayers; Membrane Proteins; Nanostructures; Nuclear Magnetic Resonance, Biomolecular
PubMed: 28529197
DOI: 10.1016/j.abb.2017.05.011 -
Journal of Clinical Laboratory Analysis 2005Different approaches have been used to extract DNA from whole blood. In most of these methods enzymes (such as proteinase K and RNAse A) or toxic organic solvents (such...
Different approaches have been used to extract DNA from whole blood. In most of these methods enzymes (such as proteinase K and RNAse A) or toxic organic solvents (such as phenol or guanidine isothiocyanate) are used. Since these enzymes are expensive, and most of the materials that are used routinely are toxic, it is desirable to apply an efficient DNA extraction procedure that does not require the use of such materials. In this study, genomic DNA was extracted by the salting-out method, but instead of using an analytical-grade enzyme and chemical detergents, as normally used for DNA isolation, a common laundry powder was used. Different concentrations of the powder were tested, and proteins were precipitated by NaCl-saturated distilled water. Finally, DNA precipitation was performed with the use of 96% ethanol. From the results, we conclude that the optimum concentration of laundry powder for the highest yield and purity of isolated DNA is 30 mg/mL. The procedure was optimized, and a final protocol is suggested. Following the same protocol, DNA was extracted from 100 blood samples, and their amounts were found to be >50 microg/mL of whole blood. The integrity of the DNA fragments was confirmed by agarose gel electrophoresis. Furthermore, the extracted DNA was used as a template for PCR reaction. The results obtained from PCR showed that the final solutions of extracted DNA did not contain any inhibitory material for the enzyme used in the PCR reaction, and indicated that the isolated DNA was of good quality. These results show that this method is simple, fast, safe, and cost-effective, and can be used in medical laboratories and research centers.
Topics: DNA; Detergents; Genomics; Humans; Polymerase Chain Reaction; Sodium Chloride
PubMed: 16302208
DOI: 10.1002/jcla.20083 -
Analytical and Bioanalytical Chemistry Jul 2023Detergents enable the investigation of membrane proteins by mass spectrometry. Detergent designers aim to improve underlying methodologies and are confronted with the... (Review)
Review
Detergents enable the investigation of membrane proteins by mass spectrometry. Detergent designers aim to improve underlying methodologies and are confronted with the challenge to design detergents with optimal solution and gas-phase properties. Herein, we review literature related to the optimization of detergent chemistry and handling and identify an emerging research direction: the optimization of mass spectrometry detergents for individual applications in mass spectrometry-based membrane proteomics. We provide an overview about qualitative design aspects including their relevance for the optimization of detergents in bottom-up proteomics, top-down proteomics, native mass spectrometry, and Nativeomics. In addition to established design aspects, such as charge, concentration, degradability, detergent removal, and detergent exchange, it becomes apparent that detergent heterogeneity is a promising key driver for innovation. We anticipate that rationalizing the role of detergent structures in membrane proteomics will serve as an enabling step for the analysis of challenging biological systems.
Topics: Detergents; Proteomics; Mass Spectrometry; Membrane Proteins
PubMed: 36808272
DOI: 10.1007/s00216-023-04584-z -
Biochimica Et Biophysica Acta.... Sep 2022Non-ionic detergents are important tools for the investigation of interactions between membrane proteins and lipid membranes. Recent studies led to the question as to...
Non-ionic detergents are important tools for the investigation of interactions between membrane proteins and lipid membranes. Recent studies led to the question as to whether the ability to capture protein-lipid interactions depends on the properties of detergents or their concentration in purification buffers. To address this question, we present the synthesis of an asymmetric, hybrid detergent that combines the head groups of detergents with opposing delipidating properties. We discuss detergent properties and protein purification outcomes to reveal whether the properties of detergent micelles or the detergent concentration in purification buffers drive membrane protein delipidation. We anticipate that our findings will enable the development of rationally design detergents for future applications in membrane protein research.
Topics: Detergents; Lipids; Membrane Proteins; Micelles
PubMed: 35551920
DOI: 10.1016/j.bbamem.2022.183958 -
Brazilian Journal of Microbiology :... Jun 2023Detergent-compatible enzymes are the new trend followed by most in the detergent industry. Cellulases, lipases, proteases, and amylases are among the enzymes frequently...
Detergent-compatible enzymes are the new trend followed by most in the detergent industry. Cellulases, lipases, proteases, and amylases are among the enzymes frequently used in detergents. Detergent-compatible enzymes can be obtained from many organisms, but the stability, cheapness, and availability of microbial enzymes make them preferable in industrial areas. In the present study, soil samples contaminated with household waste were collected from different regions of Trabzon (Turkey) for amylase-, cellulase-, protease-, and lipase-producing bacteria. A total of 55 bacterial isolates differing in colony morphology were purified from the samples and 25 of the isolates gave positive results in enzyme screening. The enzyme screening experiments revealed that 10 isolates produced amylase, 9 produced lipase, 7 produced cellulase, and 6 produced protease. While 2 isolates showed both protease and lipase activity, for 2 different isolates cellulose and amylase activity were detected together. It was also observed that one isolate, C37PLCA, produced all four enzymes. The morphological, physiological, and biochemical analyses of the bacteria from which we obtained the enzymes were performed and species close to them were determined using 16S rRNA sequences. Based on the results obtained, our enzymes show tremendous promise for the detergent industry.
Topics: Peptide Hydrolases; Lipase; Detergents; Amylases; Cellulase; RNA, Ribosomal, 16S; Bacterial Proteins; Bacteria; Cellulases
PubMed: 36890351
DOI: 10.1007/s42770-023-00944-0 -
Biochemical Society Transactions Jun 2023Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and... (Review)
Review
Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and biophysical methods, membrane proteins must first be extracted from cellular membranes - often using detergents. Detergent-extracted membrane proteins are amenable to analysis by structural, biochemical, and biophysical techniques. In certain cases, however, detergents can disturb native protein conformations and/or biological activity. This has led to the development of membrane mimetics, which stabilize membrane proteins in a native membrane-like environment that is water-soluble and detergent-free. This review provides an overview of recent developments in the membrane mimetic field, with a focus on nanodiscs, Saposin lipid nanoparticles (SapNPs), peptidiscs, and SMA lipid particles (SMALPs) - and highlights their utility for supporting biophysical, biochemical, and structural characterization of membrane proteins and complexes.
Topics: Membrane Proteins; Cell Membrane; Biomimetics; Lipid Bilayers; Detergents
PubMed: 37345653
DOI: 10.1042/BST20230164 -
Biophysical Journal Jul 2013Multiple data are available on the self-assembly of mixtures of bilayer-forming amphiphiles, particularly phospholipids and micelle-forming amphiphiles, commonly denoted... (Review)
Review
Multiple data are available on the self-assembly of mixtures of bilayer-forming amphiphiles, particularly phospholipids and micelle-forming amphiphiles, commonly denoted detergents. The structure of such mixed assemblies has been thoroughly investigated, described in phase diagrams, and theoretically rationalized in terms of the balance between the large spontaneous curvature of the curvophilic detergent and the curvophobic phospholipids. In this critical review, we discuss the mechanism of this process and try to explain the actual mechanism involved in solubilization. Interestingly, membrane solubilization by some detergents is relatively slow and the common attribute of these detergents is that their trans-bilayer movement, commonly denoted flip-flop, is very slow. Only detergents that can flip into the inner monolayer cause relatively rapid solubilization of detergent-saturated bilayers. This occurs via the following sequence of events: 1), relatively rapid penetration of detergent monomers into the outer monolayer; 2), trans-membrane equilibration of detergent monomers between the two monolayers; 3), saturation of the bilayer by detergents and consequent permeabilization of the membrane; and 4), transition of the whole bilayer to thread-like mixed micelles. When the detergent cannot flip to the inner monolayer, the outer monolayer becomes unstable due to mass imbalance between the monolayers and inclusion of the curvophilic detergent molecules in a flat surface. Consequently, the outer monolayer forms mixed micellar structures within the outer monolayer. Shedding of these micelles into the aqueous solution results in partial solubilization. The consequent leakage of detergent into the liposome results in trans-membrane equilibration of detergent and subsequent micellization through the rapid bilayer-saturation mechanism.
Topics: Detergents; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Liposomes; Micelles; Solubility
PubMed: 23870250
DOI: 10.1016/j.bpj.2013.06.007