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Relevant bibliographies by topics / Protein-Lipid/ Surfactant Interaction

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Academic literature on the topic 'Protein-Lipid/ Surfactant Interaction'

Author: Grafiati

Published: 7 September 2023

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Journal articles on the topic "Protein-Lipid/ Surfactant Interaction"

1

Tazhibayeva, Sagdat, Kuanyshbek Musabekov, Zhenis Kusainova, Ardak Sapieva, and Nurlan Musabekov. "Complex Formation of Polyacrylic Acid with Surfactants of Different Hydrophobicity." Applied Mechanics and Materials 752-753 (April 2015): 212–16. http://dx.doi.org/10.4028/www.scientific.net/amm.752-753.212.

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Complex formation processes of polyelectrolytes with surfactant ions are close model to protein - lipid interactions in living organisms. Furthermore, polymer – surfactant complexes are widely used as stabilizers of industrial dispersions and structurants of soil. When using the polymer-surfactant complexes the hydrophilic-lipophilic balance has the great importance. The interaction of polyacrylic acid with alkylammonium salts of different hydrophobicity: cetyltrimethylammonium bromide, dilaurildimethylammonium bromide and dioctadecyldimethylammonium chloride was studied by potentiometry, spectrophotometry, viscometry and electrophoresis methods. It was established that the complex formation of polyacrylic acid with cationic surfactants is carried out due to the electrostatic interaction between carboxyl groups of the polymer and cations of surfactants, which stabilized by hydrophobic interactions between their non-polar parts. The phenomenon of hysteresis in the change of the reduced viscosity of system surfactant /polyacrylic acid with temperature variation in the range of 20-60 °C was found. The possibility of using the complex formation process for water purification from CTAB has been shown. The degree of purification is 99.6-99.8%.

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Parsi, Kurosh. "Interaction of detergent sclerosants with cell membranes." Phlebology: The Journal of Venous Disease 30, no. 5 (May 14, 2014): 306–15. http://dx.doi.org/10.1177/0268355514534648.

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Commonly used detergent sclerosants including sodium tetradecyl sulphate (STS) and polidocanol (POL) are clinically used to induce endovascular fibrosis and vessel occlusion. They achieve this by lysing the endothelial lining of target vessels. These agents are surface active (surfactant) molecules that interfere with cell membranes. Surfactants have a striking similarity to the phospholipid molecules of the membrane lipid bilayer. By adsorbing at the cell membrane, surfactants disrupt the normal architecture of the lipid bilayer and reduce the surface tension. The outcome of this interaction is concentration dependent. At high enough concentrations, surfactants solubilise cell membranes resulting in cell lysis. At lower concentrations, these agents can induce a procoagulant negatively charged surface on the external aspect of the cell membrane. The interaction is also influenced by the ionic charge, molecular structure, pH and the chemical nature of the diluent (e.g. saline vs. water). The ionic charge of the surfactant molecule can influence the effect on plasma proteins and the protein contents of cell membranes. STS, an anionic detergent, denatures the tertiary complex of most proteins and in particular the clinically relevant clotting factors. By contrast, POL has no effect on proteins due to its non-ionic structure. These agents therefore exhibit remarkable differences in their interaction with lipid membranes, target cells and circulating proteins with potential implications in a range of clinical applications.

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Augusto, Luis, Karine Le Blay, Genevieve Auger, Didier Blanot, and Richard Chaby. "Interaction of bacterial lipopolysaccharide with mouse surfactant protein C inserted into lipid vesicles." American Journal of Physiology-Lung Cellular and Molecular Physiology 281, no. 4 (October 1, 2001): L776—L785. http://dx.doi.org/10.1152/ajplung.2001.281.4.l776.

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Infection of the respiratory tract is a frequent cause of lung pathologies, morbidity, and death. When bacterial endotoxin [lipopolysaccharide (LPS)] reaches the alveolar spaces, it encounters the lipid-rich surfactant that covers the epithelium. Although binding of hydrophilic surfactant protein (SP) A and SP-D with LPS has been established, nothing has been reported to date on possible cross talks between LPS and hydrophobic SP-B and SP-C. We designed a new binding technique based on the incorporation of surfactant components to lipid vesicles and the separation of unbound from vesicle-bound LPS on a density gradient. We found that among the different hydrophobic components of mouse surfactant separated by gel filtration or reverse-phase HPLC, only SP-C exhibited the capacity to bind to a tritium-labeled LPS. The binding of LPS to vesicles containing SP-C was saturable, temperature dependent, related to the concentrations of SP-C and LPS, and inhibitable by distinct unlabeled LPSs. Unlike SP-A and SP-D, the binding of SP-C to LPS did not require calcium ions. This LPS binding capacity of SP-C may represent another antibacterial defense mechanism of the lung.

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Seifert, M., D. Breitenstein, U. Klenz, M. C. Meyer, and H. J. Galla. "Solubility versus Electrostatics: What Determines Lipid/Protein Interaction in Lung Surfactant." Biophysical Journal 93, no. 4 (August 2007): 1192–203. http://dx.doi.org/10.1529/biophysj.107.106765.

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5

Herbein, Joel F., Jordan Savov, and Jo Rae Wright. "Binding and uptake of surfactant protein D by freshly isolated rat alveolar type II cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 4 (April 1, 2000): L830—L839. http://dx.doi.org/10.1152/ajplung.2000.278.4.l830.

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Alveolar type II cells secrete, internalize, and recycle pulmonary surfactant, a lipid and protein complex that increases alveolar compliance and participates in pulmonary host defense. Surfactant protein (SP) D, a collagenous C-type lectin, has recently been described as a modulator of surfactant homeostasis. Mice lacking SP-D accumulate surfactant in their alveoli and type II cell lamellar bodies, organelles adapted for recycling and secretion of surfactant. The goal of current study was to characterize the interaction of SP-D with rat type II cells. Type II cells bound SP-D in a concentration-, time-, temperature-, and calcium-dependent manner. However, SP-D binding did not alter type II cell surfactant lipid uptake. Type II cells internalized SP-D into lamellar bodies and degraded a fraction of the SP-D pool. Our results also indicated that SP-D binding sites on type II cells may differ from those on alveolar macrophages. We conclude that, in vitro, type II cells bind and recycle SP-D to lamellar bodies, but SP-D may not directly modulate surfactant uptake by type II cells.

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6

Cifuentes, J., J. Ruiz-Oronoz, C. Myles, B. Nieves, W. A. Carlo, and S. Matalon. "Interaction of surfactant mixtures with reactive oxygen and nitrogen species." Journal of Applied Physiology 78, no. 5 (May 1, 1995): 1800–1805. http://dx.doi.org/10.1152/jappl.1995.78.5.1800.

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Increased concentrations of partially reduced oxygen and nitrogen reactive species damage the alveolar epithelium and either cause or exacerbate surfactant deficiency. For this reason, there is a quest to identify surfactant replacement mixtures, which in addition to repleting depleted surfactant stores can also reduce the steady-state concentrations of reactive species in the alveolar space. Herein, we evaluated the ability of natural lung surfactant (NLS) and two mixtures (Exosurf and Survanta) used clinically for the correction of surfactant deficiency to scavenge hydroxyl radical-type species (.OH), generated either by the decomposition of peroxynitrite or by Fenton reagents (FeCl3 + H2O2). Exosurf or Survanta decreased .OH only when present at high lipid concentrations (6.5 mM). On the other hand, 40 microM of NLS decreased .OH concentrations from 75 +/- 2 to 53 +/- 2 microM (P < 0.05), most likely because of the interaction of .OH with protein sulfhydryl groups. Similarly, 40 microM of NLS incubated with a bolus of H2O2 (400 microM) decreased the H2O2 concentration in the supernatant by approximately 50%, due to the presence of catalase-type activity. In contrast to NLS, neither Exosurf nor Survanta scavenged H2O2, even when present at millimolar lipid concentrations. We concluded that Exosurf and Survanta contain limited antioxidant activity compared with NLS.

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7

Reilly, Kim E., Alan J. Mautone, and Richard Mendelsohn. "Fourier-transform infrared spectroscopy studies of lipid/protein interaction in pulmonary surfactant." Biochemistry 28, no. 18 (September 1989): 7368–73. http://dx.doi.org/10.1021/bi00444a033.

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8

Palaniyar, Nades, Ross A. Ridsdale, Stephen A. Hearn, Fred Possmayer, and George Harauz. "Formation of membrane lattice structures and their specific interactions with surfactant protein A." American Journal of Physiology-Lung Cellular and Molecular Physiology 276, no. 4 (April 1, 1999): L642—L649. http://dx.doi.org/10.1152/ajplung.1999.276.4.l642.

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Biological membranes exist in many forms, one of which is known as tubular myelin (TM). This pulmonary surfactant membranous structure contains elongated tubes that form square lattices. To understand the interaction of surfactant protein (SP) A and various lipids commonly found in TM, we undertook a series of transmission-electron-microscopic studies using purified SP-A and lipid vesicles made in vitro and also native surfactant from bovine lung. Specimens from in vitro experiments were negatively stained with 2% uranyl acetate, whereas fixed native surfactant was delipidated, embedded, and sectioned. We found that dipalmitoylphosphatidylcholine-egg phosphatidylcholine (1:1 wt/wt) bilayers formed corrugations, folds, and predominantly 47-nm-square latticelike structures. SP-A specifically interacted with these lipid bilayers and folds. We visualized other proteolipid structures that could act as intermediates for reorganizing lipids and SP-As. Such a reorganization could lead to the localization of SP-A in the lattice corners and could explain, in part, the formation of TM-like structures in vivo.

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9

He, Peng, Shannon Faris, Reddy Sudheer Sagabala, Payel Datta, Zihan Xu, Brian Callahan, Chunyu Wang, Benoit Boivin, Fuming Zhang, and Robert J. Linhardt. "Cholesterol Chip for the Study of Cholesterol–Protein Interactions Using SPR." Biosensors 12, no. 10 (September 25, 2022): 788. http://dx.doi.org/10.3390/bios12100788.

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Cholesterol, an important lipid in animal membranes, binds to hydrophobic pockets within many soluble proteins, transport proteins and membrane bound proteins. The study of cholesterol–protein interactions in aqueous solutions is complicated by cholesterol’s low solubility and often requires organic co-solvents or surfactant additives. We report the synthesis of a biotinylated cholesterol and immobilization of this derivative on a streptavidin chip. Surface plasmon resonance (SPR) was then used to measure the kinetics of cholesterol interaction with cholesterol-binding proteins, hedgehog protein and tyrosine phosphatase 1B.

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10

CRUZ, Antonio, Cristina CASALS, Kevin M. W. KEOUGH, and Jesús PÉREZ-GIL. "Different modes of interaction of pulmonary surfactant protein SP-B in phosphatidylcholine bilayers." Biochemical Journal 327, no. 1 (October 1, 1997): 133–38. http://dx.doi.org/10.1042/bj3270133.

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Pulmonary surfactant-associated protein B (SP-B) has been incorporated into vesicles of dipalmitoyl phosphatidylcholine (DPPC) or egg yolk phosphatidylcholine (PC) by two different procedures to characterize the dependence of lipid–protein interactions on the method of reconstitution. In method A the protein was dissolved in a small volume of either methanol or 60% (v/v) acetonitrile and injected into an aqueous phase containing phospholipid vesicles. In method B the vesicles were prepared by injection of a mixture of phospholipid and SP-B dissolved in methanol or aqueous acetonitrile. Both methods of reconstitution led to the extensive interaction of SP-B with PC bilayers as demonstrated by co-migration during centrifugation, marked protection against proteolysis, change in the fluorescence emission intensity of SP-B, and protection of SP-B tryptophan fluorescence from quenching by acrylamide. SP-B promoted the rapid adsorption of DPPC on an air/liquid interface irrespective of the method of protein reconstitution. However, the interfacial adsorption activity of SP-B reconstituted by method B remained stable for hours, but that of SP-B prepared by method A decreased with time. Electron microscopy showed that the injection of SP-B into an aqueous phase containing PC or DPPC vesicles (method A) induced a rapid aggregation of vesicles. By contrast, a much longer time was required for detecting vesicle aggregation when the protein was reconstituted by co-injection of SP-B and phospholipids (method B). The presence of 5% (w/w) SP-B in DPPC bilayers prepared by method B broadened the differential scanning calorimetry thermogram and decreased the enthalpy of the transition. In contrast, the injection of SP-B into preformed DPPC vesicles (method A) did not influence the gel-to-liquid phase transition of DPPC bilayers. Taken together, these results indicate that the mode and extent of interaction of SP-B with surfactant phospholipids depends on the conditions of preparation of lipid/protein samples, and that care should be taken in the interpretation of findings from reconstituted systems on the role of these surfactant proteins in the alveolar space.

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Dissertations / Theses on the topic "Protein-Lipid/ Surfactant Interaction"

1

Ocampo, Minette C. "Protein-Lipid Interactions with Pulmonary Surfactant Using Atomic Force Microscopy." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1395050693.

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Burridge, Kevin Michael. "Application and characterization of polymer-protein and polymer-membrane interactions." Miami University / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=miami1624882451668094.

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3

Abu-Libdeh, Nidal M. "Interaction of pulmonary surfactant protein A (SP-A) with DPPC/egg-PG bilayers /." 2003.

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Book chapters on the topic "Protein-Lipid/ Surfactant Interaction"

1

Sun, Shuo, Caleb I. Neufeld, Ramil F. Latypov, Bernardo Perez-Ramirez, and Qiaobing Xu. "Biophysical Methods for the Studies of Protein-Lipid/Surfactant Interactions." In ACS Symposium Series, 355–75. Washington, DC: American Chemical Society, 2015. http://dx.doi.org/10.1021/bk-2015-1215.ch017.

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2

Faucon, J. F., J. L. Dasseux, J. Dufourcq, M. Lafleur, M. Pezolet, M. Le Maire, and T. Gulik-Krzywicki. "Lipid-Protein Interactions: A Reinvestigation of Melittin Induced Effects on the Structure and Dynamics of Phosphatidylcholines." In Surfactants in Solution, 873–84. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7981-6_26.

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3

Pérez-Gil, Jesús, Cristina Casals, and Derek Marsh. "Lipid-Protein Interactions with the Hydrophobic SP-B and SP-C Lung Surfactant Proteins in Dipalmitoylphosphatidylcholine Bilayers." In Biological Membranes: Structure, Biogenesis and Dynamics, 93–100. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78846-8_9.

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