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Journal articles on the topic 'Dipalmitoylphosphatidylcholine'

Author: Grafiati

Published: 28 May 2022

Last updated: 31 July 2025

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1

Bonev, Boyan B., and Michael R. Morrow. "2H NMR studies of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine-cholesterol bilayers at high pressure." Canadian Journal of Chemistry 76, no. 11 (1998): 1512–19. http://dx.doi.org/10.1139/v98-116.

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Wideline deuterium nuclear magnetic resonance was used to investigate the phase behaviour of bi layer dispersions of chain-perdeuterated dipalmitoylphosphatidylcholine (DPPC-d62) and DPPC-d62 containing 28.5 mol% cholesterol for temperatures between 0°C and 90°C and pressures from ambient to 270 MPa. Spectra were obtained over a range of temperature at ambient pressure, 100 MPa, and 210 MPa and over a range of pressure at fixed temperatures of 0°C and 45°C (40°C for the sample containing cholesterol). The combination of complementary isobaric and isothermal scans produced observations that sug

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2

Allen, T. M., and L. Murray. "Effect of long-term Intralipid® administration in mice." Canadian Journal of Physiology and Pharmacology 64, no. 7 (1986): 1006–10. http://dx.doi.org/10.1139/y86-171.

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Intalipid® was administered intravenously to mice at a level of 2 g kg−1 day−1 for 23 days. No alterations in phagocytic index, liver or spleen size were observed in the chronically injected mice as compared with control mice that received saline injections. Tissue distribution of 0.45 μm multilamellar liposomes of egg phosphatidylcholine:cholesterol (2:1) was similar in mice that had been chronically injected with Intralipid® to that in control mice. Mice chronically given the same total amount of phospholipid in the form of 0.2 μm liposomes of phosphatidylcholine:cholesterol (2:1) rather tha

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3

Xu, Lu, Gordon Bosiljevac, Kyle Yu, and Yi Y. Zuo. "Melting of the Dipalmitoylphosphatidylcholine Monolayer." Langmuir 34, no. 15 (2018): 4688–94. http://dx.doi.org/10.1021/acs.langmuir.8b00579.

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4

Crowe, L. M., and J. H. Crowe. "Dry dipalmitoylphosphatidylcholine and trehalose revisited." Cryobiology 25, no. 6 (1988): 541. http://dx.doi.org/10.1016/0011-2240(88)90391-4.

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5

Crowe, Lois M., and John H. Crowe. "Trehalose and dry dipalmitoylphosphatidylcholine revisited." Biochimica et Biophysica Acta (BBA) - Biomembranes 946, no. 2 (1988): 193–201. http://dx.doi.org/10.1016/0005-2736(88)90392-6.

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6

Zuo, Yi Y., Rimei Chen, Xianju Wang, Jinlong Yang, Zdenka Policova, and A. Wilhelm Neumann. "Phase Transitions in Dipalmitoylphosphatidylcholine Monolayers." Langmuir 32, no. 33 (2016): 8501–6. http://dx.doi.org/10.1021/acs.langmuir.6b01482.

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7

Nguyen, Phuc Nghia, Mariam Veschgini, Motomu Tanaka, Gilles Waton, Thierry Vandamme, and Marie Pierre Krafft. "Counteracting the inhibitory effect of proteins towards lung surfactant substitutes: a fluorocarbon gas helps displace albumin at the air/water interface." Chem. Commun. 50, no. 78 (2014): 11576–79. http://dx.doi.org/10.1039/c3cc47840h.

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8

Sharifi, Soheil, and Aboozar Nasrollahi. "Effect of Dipalmitoylphosphatidylcholine on a Microemulsion." Оптика и спектроскопия 118, no. 6 (2015): 924–29. http://dx.doi.org/10.7868/s0030403415060203.

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9

Dhand, Rajiv, Jared Young, Andelle Teng, Subbiah Krishnasamy, and Nicholas J. Gross. "Is dipalmitoylphosphatidylcholine a substrate for convertase?" American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 1 (2000): L19—L24. http://dx.doi.org/10.1152/ajplung.2000.278.1.l19.

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Convertase has homology with carboxylesterases, but its substrate(s) is not known. Accordingly, we determined whether dipalmitoylphosphatidylcholine (DPPC), the major phospholipid in surfactant, was a substrate for convertase. We measured [3H]choline release during cycling of the heavy subtype containing [3H]choline-labeled DPPC with convertase, phospholipases A2, B, C, and D, liver esterase, and elastase. Cycling with liver esterase or peanut or cabbage phospholipase D produced the characteristic profile of heavy and light peaks observed on cycling with convertase. In contrast, phospholipases

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10

Sharifi, Soheil, and Aboozar Nasrollahi. "Effect of Dipalmitoylphosphatidylcholine on a microemulsion." Optics and Spectroscopy 118, no. 6 (2015): 893–98. http://dx.doi.org/10.1134/s0030400x1506020x.

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11

Tristram-Nagle, S., M. C. Wiener, C. P. Yang, and J. F. Nagle. "Kinetics of the subtransition in dipalmitoylphosphatidylcholine." Biochemistry 26, no. 14 (1987): 4288–94. http://dx.doi.org/10.1021/bi00388a016.

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12

Aruga, Shuji, Ryoichi Kataoka, and Shigeki Mitaku. "Interaction between Ca2+ and dipalmitoylphosphatidylcholine membranes." Biophysical Chemistry 21, no. 3-4 (1985): 265–75. http://dx.doi.org/10.1016/0301-4622(85)80014-4.

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13

Kataoka, Ryoichi, Shuji Aruga, Shigeki Mitaku, Kazuhiko Kinosita, and Akira Ikegami. "Interaction between Ca2+ and dipalmitoylphosphatidylcholine membranes." Biophysical Chemistry 21, no. 3-4 (1985): 277–84. http://dx.doi.org/10.1016/0301-4622(85)80015-6.

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14

Crowe, Lois M., John H. Crowe, and Dennis Chapman. "Interaction of carbohydrates with dry dipalmitoylphosphatidylcholine." Archives of Biochemistry and Biophysics 236, no. 1 (1985): 289–96. http://dx.doi.org/10.1016/0003-9861(85)90628-9.

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15

Wiedmann, Timothy S., Theodore Trouard, S. C. Shekar, Maria Polikandritou, and Yueh-Erh Rahman. "Interaction of cyclosporin A with dipalmitoylphosphatidylcholine." Biochimica et Biophysica Acta (BBA) - Biomembranes 1023, no. 1 (1990): 12–18. http://dx.doi.org/10.1016/0005-2736(90)90003-7.

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16

Mady, Mohsen M., Medhat W. Shafaa, Eman R. Abbase, and Amine H. Fahium. "Interaction of Doxorubicin and Dipalmitoylphosphatidylcholine Liposomes." Cell Biochemistry and Biophysics 62, no. 3 (2011): 481–86. http://dx.doi.org/10.1007/s12013-011-9334-x.

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17

Zolghadr, Amin Reza, and Sedigheh Saddat Moosavi. "Interactions of neutral gold nanoparticles with DPPC and POPC lipid bilayers: simulation and experiment." RSC Advances 9, no. 9 (2019): 5197–205. http://dx.doi.org/10.1039/c8ra06777e.

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Molecular dynamics simulations of neutral gold nanoparticles (AuNPs) interacting with dipalmitoylphosphatidylcholine (DPPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membranes were studied using a model system.

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18

Ruano, Miguel L. F., Kaushik Nag, Lynn-Anne Worthman, Cristina Casals, Jesús Pérez-Gil, and Kevin M. W. Keoughp. "Differential Partitioning of Pulmonary Surfactant Protein SP-A into Regions of Monolayers of Dipalmitoylphosphatidylcholine and Dipalmitoylphosphatidylcholine/Dipalmitoylphosphatidylglycerol." Biophysical Journal 74, no. 3 (1998): 1101–9. http://dx.doi.org/10.1016/s0006-3495(98)77828-2.

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19

Hao, Xiao-Lei, Hao-Yue Guo, Bobo Cao, Guang Mo, Zhi-Hong Li, and Zhi-Wu Yu. "The distinct effects of two imidazolium-based ionic liquids, [C4mim][OAc] and [C6mim][OAc], on the phase behaviours of DPPC." Physical Chemistry Chemical Physics 23, no. 33 (2021): 17888–93. http://dx.doi.org/10.1039/d1cp01220g.

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[C6mim][OAc] was found to eliminate the pre-transition of dipalmitoylphosphatidylcholine (DPPC), markedly affect the main phase transition, and insert into the bilayer at gel state to form an interdigitated phase. Differently, [C4mim][OAc] could not.

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20

Angelescu, Daniel G. "Structural behavior of amphiphilic polyion complexes interacting with saturated lipid membranes investigated by coarse-grained molecular dynamic simulations." RSC Advances 10, no. 64 (2020): 39204–16. http://dx.doi.org/10.1039/d0ra06894b.

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Neutral polyelectrolyte complexes (PECs) made from an amphiphilic multiblock copolymer of type (A<sub>n</sub>B<sub>n</sub>)<sub>m</sub> and an oppositely charged polyion and interacting with a dipalmitoylphosphatidylcholine (DPPC) lipid membrane.

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21

Yoshida, Kazunari, Akito Takashima, and Izumi Nishio. "Effect of dibucaine hydrochloride on raft-like lipid domains in model membrane systems." MedChemComm 6, no. 8 (2015): 1444–51. http://dx.doi.org/10.1039/c5md00108k.

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To clarify the biophysical and/or physicochemical mechanism of anaesthesia, we investigated the influence of dibucaine hydrochloride (DC·HCl), a local anaesthetic, on raft-like domains in ternary liposomes composed of dioleoylphosphatidylcholine (DOPC), dipalmitoylphosphatidylcholine (DPPC) and cholesterol (Chol).

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22

Yang, Haiyang, Zhiheng Huang, and Yong Zhang. "Effect of C60 on the phase transition behavior of a lipid bilayer under high pressure." RSC Advances 8, no. 2 (2018): 655–61. http://dx.doi.org/10.1039/c7ra09514g.

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By employing coarse-grained molecular dynamics simulations, we obtained the temperature–pressure phase diagrams of a dipalmitoylphosphatidylcholine bilayer, which exhibits a gel phase and a fluid phase, with variation of the C<sub>60</sub>versus lipid ratios.

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23

Kamogawa, Marina, Takuji Ube, Junichi Shimanuki, Takashi Harumoto, Makoto Yuasa, and Takashi Ishiguro. "Synthesis of Liposome Reinforced with Cholesterol and Application to Transmission Electron Microscopy Observation." MRS Proceedings 1498 (2013): 227–32. http://dx.doi.org/10.1557/opl.2013.341.

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ABSTRACTLiposome was synthesized by using mixture of dipalmitoylphosphatidylcholine and cholesterol in the ultrapure water or physiological saline. Phase transformation temperature and vibrational mode of dipalmitoylphosphatidylcholine molecule were detected by using transmission Fourier-transform infrared spectroscopy for aqueous solution, which we developed. The liposomes were fixed on an amorphous carbon mesh for ultra-high resolution transmission electron microscopy observation and stained with platinum thymidine blue. As-prepared liposomes reinforced with cholesterol were spherical in sha

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24

de Groot, Carolin, Mathias Müsken та Christel Müller-Goymann. "Novel Colloidal Microstructures of β-Escin and the Liposomal Components Cholesterol and DPPC". Planta Medica 84, № 16 (2018): 1219–27. http://dx.doi.org/10.1055/a-0624-2706.

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AbstractThe discovery of immunostimulating complex formation by the saponin Quil A from the plant Quillaja saponaria with cholesterol and a phospholipid opened up new avenues for the development of drug delivery systems for vaccine application with additional adjuvant properties. In this study, β-escin, a monodesmosidic triterpene saponin from horse chestnut, was investigated in terms of its interaction with liposomal components (cholesterol, dipalmitoylphosphatidylcholine) by Langmuir film balance studies and with regard to particle formation visualized by transmission electron microscopy. A

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25

Hill, Warren G., Rickey L. Rivers, and Mark L. Zeidel. "Role of Leaflet Asymmetry in the Permeability of Model Biological Membranes to Protons, Solutes, and Gases." Journal of General Physiology 114, no. 3 (1999): 405–14. http://dx.doi.org/10.1085/jgp.114.3.405.

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Bilayer asymmetry in the apical membrane may be important to the barrier function exhibited by epithelia in the stomach, kidney, and bladder. Previously, we showed that reduced fluidity of a single bilayer leaflet reduced water permeability of the bilayer, and in this study we examine the effect of bilayer asymmetry on permeation of nonelectrolytes, gases, and protons. Bilayer asymmetry was induced in dipalmitoylphosphatidylcholine liposomes by rigidifying the outer leaflet with the rare earth metal, praseodymium (Pr3+). Rigidification was demonstrated by fluorescence anisotropy over a range o

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26

Kuboki, Noritaka, Naoaki Yokoyama, Naoya Kojima, Tatsuya Sakurai, Noboru Inoue, and Chihiro Sugimoto. "EFFICACY OF DIPALMITOYLPHOSPHATIDYLCHOLINE LIPOSOME AGAINST AFRICAN TRYPANOSOMES." Journal of Parasitology 92, no. 2 (2006): 389–93. http://dx.doi.org/10.1645/ge-667r.1.

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27

Lehmler, Hans-Joachim, Azarih Fortis-Santiago, Dhananjaya Nauduri, and Paul M. Bummer. "Interaction of long-chain nicotinates with dipalmitoylphosphatidylcholine." Journal of Lipid Research 46, no. 3 (2004): 535–46. http://dx.doi.org/10.1194/jlr.m400406-jlr200.

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28

ISHINAGA, Masataka, Yasuko OKITA, and Akiko ITO. "Calorimetric Study on a Dipalmitoylphosphatidylcholine-Propylgallate Mixture1." Journal of Biochemistry 100, no. 6 (1986): 1663–68. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a121875.

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29

Ikegami, Machiko, Alan Jobe, and Gloria Duane. "Liposomes of dipalmitoylphosphatidylcholine associate with natural surfactant." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 835, no. 2 (1985): 352–59. http://dx.doi.org/10.1016/0005-2760(85)90291-7.

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30

Gurrieri, Salvatore, and Francesco Castelli. "Thermotropic behaviour of dipalmitoylphosphatidylcholine liposomes containing retinoids." Thermochimica Acta 122, no. 1 (1987): 117–22. http://dx.doi.org/10.1016/0040-6031(87)80111-9.

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31

Lehmler, H. J., and P. M. Bummer. "Mixing of perfluorinated carboxylic acids with dipalmitoylphosphatidylcholine." Biochimica et Biophysica Acta (BBA) - Biomembranes 1664, no. 2 (2004): 141–49. http://dx.doi.org/10.1016/j.bbamem.2004.05.002.

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32

Tosh, Ronald E., and Peter J. Collings. "High pressure volumetric measurements in dipalmitoylphosphatidylcholine bilayers." Biochimica et Biophysica Acta (BBA) - Biomembranes 859, no. 1 (1986): 10–14. http://dx.doi.org/10.1016/0005-2736(86)90312-3.

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33

Gooris, G. S., M. Kamran, A. Kros, D. J. Moore, and J. A. Bouwstra. "Interactions of dipalmitoylphosphatidylcholine with ceramide-based mixtures." Biochimica et Biophysica Acta (BBA) - Biomembranes 1860, no. 6 (2018): 1272–81. http://dx.doi.org/10.1016/j.bbamem.2018.02.024.

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34

Dabkowska, Aleksandra P., Louise E. Collins, David J. Barlow, et al. "Modulation of Dipalmitoylphosphatidylcholine Monolayers by Dimethyl Sulfoxide." Langmuir 30, no. 29 (2014): 8803–11. http://dx.doi.org/10.1021/la501275h.

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35

Shafaa, Medhat, Hossam Kareem, Amany Elshazly, Amira Dakrory, and Maha Elsyed. "Interaction of Coenzyme Q10 with Dipalmitoylphosphatidylcholine Liposomes." Journal of Scientific Research in Science 34, part1 (2018): 245–57. http://dx.doi.org/10.21608/jsrs.2018.14047.

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36

Kafalieva, D., P. N. Shek, and N. Z. Stanacev. "Topological distribution of atropine in dipalmitoylphosphatidylcholine liposomes." Journal of Microencapsulation 7, no. 2 (1990): 219–27. http://dx.doi.org/10.3109/02652049009021835.

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37

Akiyama, Morio, Norio Matsushita, and Yoshio Terayama. "sKinetics of the Subtransition of Multilamellar Dipalmitoylphosphatidylcholine." Japanese Journal of Applied Physics 26, Part 1, No. 9 (1987): 1587–91. http://dx.doi.org/10.1143/jjap.26.1587.

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38

Muramatsu, K., Y. Maitani, Y. Machida, and T. Nagai. "Effect of soybean-derived sterol and its glucoside mixtures on the stability of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/cholesterol liposomes." International Journal of Pharmaceutics 107, no. 1 (1994): 1–8. http://dx.doi.org/10.1016/0378-5173(94)90296-8.

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39

Hermans, Eline, M. Saad Bhamla, Peter Kao, Gerald G. Fuller, and Jan Vermant. "Lung surfactants and different contributions to thin film stability." Soft Matter 11, no. 41 (2015): 8048–57. http://dx.doi.org/10.1039/c5sm01603g.

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In the present work, we investigate the mechanisms affecting the stability of surfactant-laden thin films during spreading, using drainage flows from a hemispherical dome. Three commercial lung surfactant replacements Survanta, Curosurf and Infasurf, along with the phospholipid dipalmitoylphosphatidylcholine (DPPC), are used.

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40

Fresta, M., P. M. Furneri, E. Mezzasalma, V. M. Nicolosi, and G. Puglisi. "Correlation of trimethoprim and brodimoprim physicochemical and lipid membrane interaction properties with their accumulation in human neutrophils." Antimicrobial Agents and Chemotherapy 40, no. 12 (1996): 2865–73. http://dx.doi.org/10.1128/aac.40.12.2865.

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Dipalmitoylphosphatidylcholine vesicles were used as a biological membrane model to investigate the interaction and the permeation properties of trimethoprim and brodimoprim as a function of drug protonation. The drug-membrane interaction was studied by differential scanning calorimetry. Both drugs interacted with the hydrophilic phospholipid head groups when in a protonated form. An experiment on the permeation of the two drugs through dipalmitoylphosphatidylcholine biomembranes showed higher diffusion rate constants when the two drugs were in the uncharged form; lowering of the pH (formation

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41

Nishikawa, Naoyuki, Hideto Mori, and Mitsunori Ono. "Stabilizing Effect of Diphytanylphosphate on Dipalmitoylphosphatidylcholine Bilayer Membrane." Chemistry Letters 23, no. 4 (1994): 767–70. http://dx.doi.org/10.1246/cl.1994.767.

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42

HITZEMANN, ROBERT J., CINDY GRAHAM-BRITTAIN, HAROLD E. SCHUELER, and GEORGE P. KREISHMAN. "Ordering/Disordering Effects of Ethanol in Dipalmitoylphosphatidylcholine Liposomes." Annals of the New York Academy of Sciences 492, no. 1 Alcohol and t (1987): 142–44. http://dx.doi.org/10.1111/j.1749-6632.1987.tb48663.x.

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43

Peters-Libeu, Clare A., Yvonne Newhouse, Steven C. Hall, H. Ewa Witkowska, and Karl H. Weisgraber. "Apolipoprotein E•dipalmitoylphosphatidylcholine particles are ellipsoidal in solution." Journal of Lipid Research 48, no. 5 (2007): 1035–44. http://dx.doi.org/10.1194/jlr.m600545-jlr200.

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44

Akiyama, Morio. "X-Ray Diffraction Studies of Subtransition in Dipalmitoylphosphatidylcholine." Japanese Journal of Applied Physics 24, Part 1, No. 2 (1985): 231–34. http://dx.doi.org/10.1143/jjap.24.231.

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45

Alsina, M. A., C. Mestres, F. Rabanal, M. A. Busquets, and F. Reig. "Miscibility of HBV peptides and dipalmitoylphosphatidylcholine in monolayers." Langmuir 9, no. 4 (1993): 1129–33. http://dx.doi.org/10.1021/la00028a042.

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46

YAMAUCHI, Ryo, Masahiro KOJIMA, Koji KATO, and Yoshimitsu UENO. "Lipoxygenase-catalyzed oxygenation of monogalactosyldilinolenoylglycerol in dipalmitoylphosphatidylcholine liposomes." Agricultural and Biological Chemistry 49, no. 8 (1985): 2475–77. http://dx.doi.org/10.1271/bbb1961.49.2475.

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47

JIZOMOTO, Hiroaki, Eri KANAOKA, and Koichiro HIRANO. "Encapsulation of drugs by lyophilized, empty dipalmitoylphosphatidylcholine liposomes." CHEMICAL & PHARMACEUTICAL BULLETIN 37, no. 7 (1989): 1895–98. http://dx.doi.org/10.1248/cpb.37.1895.

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48

Zaitsev, S. Yu, V. P. Vereschetin, V. P. Zubov, W. Zeiss, and D. Möbius. "Ionic selectivity of valinomycin in the dipalmitoylphosphatidylcholine monolayers." Thin Solid Films 284-285 (September 1996): 667–70. http://dx.doi.org/10.1016/s0040-6090(95)08417-7.

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49

Bhattacharya, Soumendu, Robert A. Moss, Helmut Ringsdorf, and Joachim Simon. "A polymeric "flippase" for surface-differentiated dipalmitoylphosphatidylcholine liposomes." Journal of the American Chemical Society 115, no. 9 (1993): 3812–13. http://dx.doi.org/10.1021/ja00062a072.

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50

Bottiglieri, Denise F., and Edwin M. Meyer. "Dipalmitoylphosphatidylcholine liposomes inhibit calcium-dependent [3H]acetylcholine release." Neurochemical Research 12, no. 8 (1987): 739–44. http://dx.doi.org/10.1007/bf00970530.

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