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Artykuły w czasopismach na temat „Protein Conformation - Air/Water Interface”

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Data publikacji: 7 września 2023

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1

Han, Fei, Qian Shen, Wei Zheng, et al. "The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis." Foods 12, no. 8 (2023): 1601. http://dx.doi.org/10.3390/foods12081601.

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The characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen–deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformational information for proteins. In this work, an air/water interface, HDX-MS, for the adsorbed proteins at the interface was developed. The model protein bovine serum albumin (BSA) was deuterium-labeled at the air/water interface in situ for different predetermined times (10 min and 4 h), and then th
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2

Yano, Yohko F., Etsuo Arakawa, Wolfgang Voegeli, Chika Kamezawa, and Tadashi Matsushita. "Initial Conformation of Adsorbed Proteins at an Air–Water Interface." Journal of Physical Chemistry B 122, no. 17 (2018): 4662–66. http://dx.doi.org/10.1021/acs.jpcb.8b01039.

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3

Lad, Mitaben D., Fabrice Birembaut, Joanna M. Matthew, Richard A. Frazier, and Rebecca J. Green. "The adsorbed conformation of globular proteins at the air/water interface." Physical Chemistry Chemical Physics 8, no. 18 (2006): 2179. http://dx.doi.org/10.1039/b515934b.

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Belem-Gonçalves, Silvia, Pascale Tsan, Jean-Marc Lancelin, Tito L. M. Alves, Vera M. Salim, and Françoise Besson. "Interfacial behaviour of bovine testis hyaluronidase." Biochemical Journal 398, no. 3 (2006): 569–76. http://dx.doi.org/10.1042/bj20060485.

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The interfacial properties of bovine testicular hyaluronidase were investigated by demonstrating the association of hyaluronidase activity with membranes prepared from bovine testis. Protein adsorption to the air/water interface was investigated using surface pressure-area isotherms. In whichever way the interfacial films were obtained (protein injection or deposition), the hyaluronidase exhibited a significant affinity for the air/water interface. The isotherm obtained 180 min after protein injection into a pH 5.3 subphase was similar to the isotherm obtained after spreading the same amount o
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5

Bhuvanesh, Thanga, Rainhard Machatschek, Yue Liu, Nan Ma, and Andreas Lendlein. "Self-stabilized fibronectin films at the air/water interface." MRS Advances 5, no. 12-13 (2019): 609–20. http://dx.doi.org/10.1557/adv.2019.401.

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ABSTRACTFibronectin (FN) is a mediator molecule, which can connect cell receptors to the extracellular matrix (ECM) in tissues. This function is highly desirable for biomaterial surfaces in order to support cell adhesion. Controlling the fibronectin adsorption profile on substrates is challenging because of possible conformational changes after deposition, or due to displacement by secondary proteins from the culture medium. Here, we aim to develop a method to realize self-stabilized ECM glycoprotein layers with preserved native secondary structure on substrates. Our concept is the assembly of
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6

Guo, Dashan, Yuwei Hou, Hongshan Liang, Lingyu Han, Bin Li, and Bin Zhou. "Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly." Foods 12, no. 10 (2023): 1931. http://dx.doi.org/10.3390/foods12101931.

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The distinctive assembly behaviors of lysozyme (Lys) feature prominently in food, materials, biomedicine, and other fields and have intrigued many scholars. Although our previous work suggested that reduced glutathione (GSH) could induce lysozyme to form interfacial films at the air/water interface, the underlying mechanism is still obscure. In the present study, the effects of GSH on the disulfide bond and protein conformation of lysozyme were investigated by fluorescence spectroscopy, circular dichroism spectroscopy, and infrared spectroscopy. The findings demonstrated that GSH was able to b
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7

Renault, Anne, Jean-François Rioux-Dubé, Thierry Lefèvre, et al. "Surface Properties and Conformation of Nephila clavipes Spider Recombinant Silk Proteins at the Air−Water Interface." Langmuir 25, no. 14 (2009): 8170–80. http://dx.doi.org/10.1021/la900475q.

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8

Han, Meng-huai, and Chi-cheng Chiu. "Fast estimation of protein conformational preference at air/water interface via molecular dynamics simulations." Journal of the Taiwan Institute of Chemical Engineers 92 (November 2018): 42–49. http://dx.doi.org/10.1016/j.jtice.2018.02.026.

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9

Flach, Carol R., Joseph W. Brauner, and Richard Mendelsohn. "Coupled External Reflectance FT-IR/Miniaturized Surface Film Apparatus for Biophysical Studies." Applied Spectroscopy 47, no. 7 (1993): 982–85. http://dx.doi.org/10.1366/0003702934415147.

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An FT-IR spectrophotometer has been interfaced to a miniaturized surface film apparatus for external reflection studies of insoluble monolayers in situ at the air/water interface. Signal-to-noise ratios of 200:1 were routinely achieved for the CH2 stretching vibrations of phospholipids. We have monitored, using the acyl chain symmetric CH2 stretching frequency near 2850 cm−1 as a structural probe, lipid conformational order changes that occur during the surface pressure-induced two-dimensional phase transition in monolayers of 1,2-dipalmitoylphosphatidylserine. In addition, the small volume of
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10

Tanaka, Takumi, Yuki Terauchi, Akira Yoshimi, and Keietsu Abe. "Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation." Microorganisms 10, no. 8 (2022): 1498. http://dx.doi.org/10.3390/microorganisms10081498.

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Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of Aspergillus hydrophobins are comprehensively discussed on the basis of recent findings. Multiple Aspergillus hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some Aspergillus hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air–liquid interface, RolA of Aspergillus oryzae self-assembles via four stages, an
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11

LARVOR, Marie-Pierre, Rachel CERDAN, Catherine GUMILA, et al. "Characterization of the lipid-binding domain of the Plasmodium falciparum CTP:phosphocholine cytidylyltransferase through synthetic-peptide studies." Biochemical Journal 375, no. 3 (2003): 653–61. http://dx.doi.org/10.1042/bj20031011.

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Phospholipid biosynthesis plays a key role in malarial infection and is regulated by CCT (CTP:phosphocholine cytidylyltransferase). This enzyme belongs to the group of amphitropic proteins which are regulated by reversible membrane interaction. To assess the role of the putative membrane-binding domain of Plasmodium falciparum CCT (PfCCT), we synthesized three peptides, K21, V20 and K54 corresponding to residues 274–294, 308–327 and 274–327 of PfCCT respectively. Conformational behaviour of the peptides, their ability to bind to liposomes and to destabilize lipid bilayers, and their insertion
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12

Alamdari, Sarah, Steven J. Roeters, Thaddeus W. Golbek, Lars Schmüser, Tobias Weidner, and Jim Pfaendtner. "Orientation and Conformation of Proteins at the Air–Water Interface Determined from Integrative Molecular Dynamics Simulations and Sum Frequency Generation Spectroscopy." Langmuir 36, no. 40 (2020): 11855–65. http://dx.doi.org/10.1021/acs.langmuir.0c01881.

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13

Kennedy, Malcolm W. "Latherin and other biocompatible surfactant proteins." Biochemical Society Transactions 39, no. 4 (2011): 1017–22. http://dx.doi.org/10.1042/bst0391017.

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Horses and other equids are unusual in producing protein-rich sweat for thermoregulation, a major component of which is latherin, a highly surface-active, non-glycosylated protein that is a member of the PLUNC (palate, lung and nasal epithelium clone) family. Latherin produces a significant reduction in water surface tension at low concentrations (≤1 mg/ml), and probably acts as a wetting agent to facilitate evaporative cooling through a thick, waterproofed pelt. Latherin binds temporarily to hydrophobic surfaces, and so may also have a disruptive effect on microbial biofilms. It may consequen
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14

Dai, Guoliang, Jinru Li, and Long Jiang. "Conformation change of glucose oxidase at the water–air interface." Colloids and Surfaces B: Biointerfaces 13, no. 2 (1999): 105–11. http://dx.doi.org/10.1016/s0927-7765(98)00113-1.

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15

Wren, Sumi N., Brittany P. Gordon, Nicholas A. Valley, Laura E. McWilliams, and Geraldine L. Richmond. "Hydration, Orientation, and Conformation of Methylglyoxal at the Air–Water Interface." Journal of Physical Chemistry A 119, no. 24 (2015): 6391–403. http://dx.doi.org/10.1021/acs.jpca.5b03555.

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16

Shibata, Akira, Takashi Kai, Shinsuke Yamashita, Yoshihiro Itoh, and Takuya Yamashita. "Conformation of poly(l-glutamic acid) at the air/water interface." Biochimica et Biophysica Acta (BBA) - Biomembranes 812, no. 2 (1985): 587–90. http://dx.doi.org/10.1016/0005-2736(85)90334-7.

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17

Ishikawa, Daisuke, Taizo Mori, Yusuke Yonamine, et al. "Mechanochemical Tuning of the Binaphthyl Conformation at the Air-Water Interface." Angewandte Chemie International Edition 54, no. 31 (2015): 8988–91. http://dx.doi.org/10.1002/anie.201503363.

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18

Ishikawa, Daisuke, Taizo Mori, Yusuke Yonamine, et al. "Mechanochemical Tuning of the Binaphthyl Conformation at the Air-Water Interface." Angewandte Chemie 127, no. 31 (2015): 9116–19. http://dx.doi.org/10.1002/ange.201503363.

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19

Lad, Mitaben D., Fabrice Birembaut, Richard A. Frazier, and Rebecca J. Green. "Protein–lipid interactions at the air/water interface." Physical Chemistry Chemical Physics 7, no. 19 (2005): 3478. http://dx.doi.org/10.1039/b506558p.

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20

Junghans, Ann, Chlóe Champagne, Philippe Cayot, Camille Loupiac, and Ingo Köper. "Protein−Lipid Interactions at the Air−Water Interface." Langmuir 26, no. 14 (2010): 12049–53. http://dx.doi.org/10.1021/la100036v.

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21

Rodrı́guez Patino, Juan M., M. Rosario Rodrı́guez Niño, and Cecilio Carrera Sánchez. "Protein–emulsifier interactions at the air–water interface." Current Opinion in Colloid & Interface Science 8, no. 4-5 (2003): 387–95. http://dx.doi.org/10.1016/s1359-0294(03)00095-5.

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22

Samantray, Suman, and David L. Cheung. "Effect of the air–water interface on the conformation of amyloid beta." Biointerphases 15, no. 6 (2020): 061011. http://dx.doi.org/10.1116/6.0000620.

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23

O'Driscoll, Benjamin M. D., Jeremy L. Ruggles, Garry J. Foran, and Ian R. Gentle. "Thin Films of a Tetracationic Porphyrin." Australian Journal of Chemistry 56, no. 10 (2003): 1059. http://dx.doi.org/10.1071/ch03123.

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Langmuir–Blodgett films of the tetracationic porphyrin tetrakis(octadecyl-4-pyridinium)porphinatozinc(II) bromide transferred from subphases containing different salts were studied using X-ray photoelectron spectroscopy (XPS) and X-ray reflectometry. In contrast to previous results at the air/water interface, we found that the porphyrin adopted a fixed conformation at the air/solid interface regardless of composition of the subphase or whether the films were transferred above or below the primary phase transition. This conformation was assigned to the formation of an interdigitated bilayer str
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24

Liao, Yi-Ting, Anthony C. Manson, Michael R. DeLyser, William G. Noid, and Paul S. Cremer. "TrimethylamineN-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine." Proceedings of the National Academy of Sciences 114, no. 10 (2017): 2479–84. http://dx.doi.org/10.1073/pnas.1614609114.

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We report experimental and computational studies investigating the effects of three osmolytes, trimethylamineN-oxide (TMAO), betaine, and glycine, on the hydrophobic collapse of an elastin-like polypeptide (ELP). All three osmolytes stabilize collapsed conformations of the ELP and reduce the lower critical solution temperature (LSCT) linearly with osmolyte concentration. As expected from conventional preferential solvation arguments, betaine and glycine both increase the surface tension at the air–water interface. TMAO, however, reduces the surface tension. Atomically detailed molecular dynami
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25

Martin, Anneke H., Marcel B. J. Meinders, Martin A. Bos, Martien A. Cohen Stuart, and Ton van Vliet. "Conformational Aspects of Proteins at the Air/Water Interface Studied by Infrared Reflection−Absorption Spectroscopy." Langmuir 19, no. 7 (2003): 2922–28. http://dx.doi.org/10.1021/la0208629.

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26

Dalgicdir, Cahit, та Mehmet Sayar. "Conformation and Aggregation of LKα14 Peptide in Bulk Water and at the Air/Water Interface". Journal of Physical Chemistry B 119, № 49 (2015): 15164–75. http://dx.doi.org/10.1021/acs.jpcb.5b08871.

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27

Chang, Su-Hwa, Liang-Yu Chen, and Wen-Yih Chen. "The effects of denaturants on protein conformation and behavior at air/solution interface." Colloids and Surfaces B: Biointerfaces 41, no. 1 (2005): 1–6. http://dx.doi.org/10.1016/j.colsurfb.2004.10.015.

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28

Yano, Yohko F., Tomoya Uruga, Hajime Tanida, Yasuko Terada, and Hironari Yamada. "Protein Salting Out Observed at an Air−Water Interface." Journal of Physical Chemistry Letters 2, no. 9 (2011): 995–99. http://dx.doi.org/10.1021/jz200111q.

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29

Yang, Yuhong, Cedric Dicko, Colin D. Bain, et al. "Behavior of silk protein at the air–water interface." Soft Matter 8, no. 37 (2012): 9705. http://dx.doi.org/10.1039/c2sm26054a.

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30

MARTINEZ, K., C. CARRERASANCHEZ, V. PIZONESRUIZHENESTROSA, J. RODRIGUEZPATINO, and A. PILOSOF. "Soy protein–polysaccharides interactions at the air–water interface." Food Hydrocolloids 21, no. 5-6 (2007): 804–12. http://dx.doi.org/10.1016/j.foodhyd.2006.11.005.

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31

Diamant, Haim, and David Andelman. "Dimeric Surfactants: Spacer Chain Conformation and Specific Area at the Air/Water Interface." Langmuir 10, no. 9 (1994): 2910–16. http://dx.doi.org/10.1021/la00021a012.

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32

Lu, J. R., T. J. Su, R. K. Thomas, J. Penfold, and J. Webster. "Structural conformation of lysozyme layers at the air/water interface studied by neutron reflection." Journal of the Chemical Society, Faraday Transactions 94, no. 21 (1998): 3279–87. http://dx.doi.org/10.1039/a805731a.

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33

Mohwald, H. "Phospholipid and Phospholipid-Protein Monolayers at the Air/Water Interface." Annual Review of Physical Chemistry 41, no. 1 (1990): 441–76. http://dx.doi.org/10.1146/annurev.pc.41.100190.002301.

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34

Niño, M. Rosario Rodríguez, Cecilio Carrera Sánchez, Marta Cejudo Fernández, and Juan M. Rodríguez Patino. "Protein and lipid films at equilibrium at air-water interface." Journal of the American Oil Chemists' Society 78, no. 9 (2001): 873–79. http://dx.doi.org/10.1007/s11746-001-0358-0.

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35

RODRIGUEZNINO, M., C. SANCHEZ, V. RUIZHENESTROSA, and J. PATINO. "Milk and soy protein films at the air?water interface." Food Hydrocolloids 19, no. 3 (2005): 417–28. http://dx.doi.org/10.1016/j.foodhyd.2004.10.008.

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36

Gálvez-Ruiz, María José. "Different approaches to study protein films at air/water interface." Advances in Colloid and Interface Science 247 (September 2017): 533–42. http://dx.doi.org/10.1016/j.cis.2017.07.015.

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37

Dutka, Volodymyr, Olena Aksimentyeva, Yaroslav Kovalskyi, and Natalya Oshchapovska. "Monomolecular Films of Organic Diacyl Diperoxides on the Interface of the Phases Water–Air." Chemistry & Chemical Technology 15, no. 4 (2021): 536–42. http://dx.doi.org/10.23939/chcht15.04.536.

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Monomolecular films of diacyl diperoxides at the water–air phase interface have been studied. Their behaviour is influenced by the structure of the molecule and the solvent. The numerical values of the areas of molecules that are extrapolated to zero pressure are different, which indicates a different conformation of the molecules in the monolayer. The conformational states of diperoxides were calculated by quantum chemical methods. Experimental data and quantum chemical calculations are consistent with each other.
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38

Ozgur, Beytullah, Cahit Dalgicdir та Mehmet Sayar. "Correction to “Conformation and Aggregation of LKα14 Peptide in Bulk Water and at the Air/Water Interface”". Journal of Physical Chemistry B 123, № 10 (2019): 2463–65. http://dx.doi.org/10.1021/acs.jpcb.9b01566.

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39

Terme, Nolwenn, Alicia Jacquemet, Thierry Benvegnu, Véronique Vié, and Loïc Lemiègre. "Modification of bipolar lipid conformation at the air/water interface by a single stereochemical variation." Chemistry and Physics of Lipids 183 (October 2014): 9–17. http://dx.doi.org/10.1016/j.chemphyslip.2014.04.008.

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40

Kim, Chanjoong, Marc C. Gurau, Paul S. Cremer, and Hyuk Yu. "Chain Conformation of Poly(dimethyl siloxane) at the Air/Water Interface by Sum Frequency Generation." Langmuir 24, no. 18 (2008): 10155–60. http://dx.doi.org/10.1021/la800349q.

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41

Zhu, Yang-Ming, Zu-Hong Lu, and Yu Wei. "Surface-pressure-induced conformation changes of a polymer liquid crystal at the air-water interface." Physical Review E 49, no. 6 (1994): 5316–18. http://dx.doi.org/10.1103/physreve.49.5316.

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42

Wang, Chengshan, Nilam Shah, Garima Thakur, Feimeng Zhou та Roger M. Leblanc. "α-Synuclein in α-helical conformation at air–water interface: implication of conformation and orientation changes during its accumulation/aggregation". Chemical Communications 46, № 36 (2010): 6702. http://dx.doi.org/10.1039/c0cc02098b.

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43

Martini, Silvia, Claudia Bonechi, Alberto Foletti, and Claudio Rossi. "Water-Protein Interactions: The Secret of Protein Dynamics." Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/138916.

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Water-protein interactions help to maintain flexible conformation conditions which are required for multifunctional protein recognition processes. The intimate relationship between the protein surface and hydration water can be analyzed by studying experimental water properties measured in protein systems in solution. In particular, proteins in solution modify the structure and the dynamics of the bulk water at the solute-solvent interface. The ordering effects of proteins on hydration water are extended for several angstroms. In this paper we propose a method for analyzing the dynamical prope
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44

Rabe, Martin, Andreas Kerth, Alfred Blume, and Patrick Garidel. "Albumin displacement at the air–water interface by Tween (Polysorbate) surfactants." European Biophysics Journal 49, no. 7 (2020): 533–47. http://dx.doi.org/10.1007/s00249-020-01459-4.

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AbstractTween (polysorbate) 20 and 80 are surfactants used for the development of parenteral protein drugs, due to their beneficial safety profile and stabilisation properties. To elucidate the mechanism by which Tween 20 and 80 stabilise proteins in aqueous solutions, either by a “direct” protein to surfactant interaction and/or by an interaction with the protein film at the air–water interface, we used spectroscopic (Infrared Reflection Absorption Spectroscopy, IRRAS) and microscopic techniques (Brewster Angle Microscopy, BAM) in combination with surface pressure measurements. To this end, t
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45

Wang, Lei, Fredrik G. Bäcklund, Yusheng Yuan, et al. "Air–Water Interface Assembly of Protein Nanofibrils Promoted by Hydrophobic Additives." ACS Sustainable Chemistry & Engineering 9, no. 28 (2021): 9289–99. http://dx.doi.org/10.1021/acssuschemeng.1c01901.

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46

Liao, Zhengzheng, Joshua W. Lampe, Portonovo S. Ayyaswamy, David M. Eckmann, and Ivan J. Dmochowski. "Protein Assembly at the Air–Water Interface Studied by Fluorescence Microscopy." Langmuir 27, no. 21 (2011): 12775–81. http://dx.doi.org/10.1021/la203053g.

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47

Saint-Pierre-Chazalet, M., C. Fressigné, F. Billoudet, and M. P. Pileni. "Phospholipid-protein interactions at the air-water interface: a monolayer study." Thin Solid Films 210-211 (April 1992): 743–46. http://dx.doi.org/10.1016/0040-6090(92)90391-n.

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48

Tronin, Andrey, Timothy Dubrovsky, Svetlana Dubrovskaya, Giuliano Radicchi, and Claudio Nicolini. "Role of Protein Unfolding in Monolayer Formation on Air−Water Interface." Langmuir 12, no. 13 (1996): 3272–75. http://dx.doi.org/10.1021/la950879+.

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49

Yano, Yohko F., Yuki Kobayashi, Toshiaki Ina, Kiyofumi Nitta, and Tomoya Uruga. "Hofmeister Anion Effects on Protein Adsorption at an Air–Water Interface." Langmuir 32, no. 38 (2016): 9892–98. http://dx.doi.org/10.1021/acs.langmuir.6b02352.

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50

Kundu, Sarathi, H. Matsuoka, and H. Seto. "Zwitterionic lipid (DPPC)–protein (BSA) complexes at the air–water interface." Colloids and Surfaces B: Biointerfaces 93 (May 2012): 215–18. http://dx.doi.org/10.1016/j.colsurfb.2012.01.008.

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