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Regulation of Aquaporin Z osmotic permeability in ABA tri-block copolymer

  • Received: 15 May 2015 Accepted: 20 August 2015 Published: 31 August 2015
  • Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle solutions were adjusted within wide ranges to investigate the regulation of osmotic permeability of aquaporin Z through external conditions. Our results show that aquaporin Z permeability was enhanced by hydrophobic mismatch. In addition, the water filtration mechanism of aquaporin Z is significantly affected by the concentration of H+ and OH- ions.

    Citation: Wenyuan Xie, Jason Wei Jun Low, Arunmozhiarasi Armugam, Kandiah Jeyaseelan, Yen Wah Tong. Regulation of Aquaporin Z osmotic permeability in ABA tri-block copolymer[J]. AIMS Biophysics, 2015, 2(3): 381-397. doi: 10.3934/biophy.2015.3.381

    Related Papers:

  • Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle solutions were adjusted within wide ranges to investigate the regulation of osmotic permeability of aquaporin Z through external conditions. Our results show that aquaporin Z permeability was enhanced by hydrophobic mismatch. In addition, the water filtration mechanism of aquaporin Z is significantly affected by the concentration of H+ and OH- ions.


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    [1] Kumar M, Grzelakowski M, Zilles J, et al. (2007) Highly permeable polymeri membranes based on the incorporation of the functional water channel protein Aquaporin Z. PNAS 104: 20719-20724. doi: 10.1073/pnas.0708762104
    [2] Service RF (2006) Desalination freshens up. Science 313:1088-1090.
    [3] Tal A (2006) Seeking sustainability: Israel's evolving water management strategy. Science 313: 1081-1084.
    [4] Discher BM, Won YY, Ege DS, et al. (1999) Polymersomes: tough vesicles made from diblock copolymers. Science 284:1143-1146. doi: 10.1126/science.284.5417.1143
    [5] Calamita G, Kempf B, Rudd KE, et al. (1997) The aquaporin-Z water channel gene of Escherichia coli: Structure, organization and phylogeny. Biology of the Cell 89: 321-329. doi: 10.1111/j.1768-322X.1997.tb01029.x
    [6] Calamita G, Bishai WR, Preston GM, et al. (1995) Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli. J Biol Chem 270: 29063-29066. doi: 10.1074/jbc.270.49.29063
    [7] Scheuring S, Ringler P, Borgnia M, et al. (1999) High resultion AFM topographs of the Escherichia coli water channel aquaporin Z. EMBO J 18: 4981-4987.
    [8] Gorin MB, Yancey SB, Cline J, et al. (1984) The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning. Cell 39: 49-59.
    [9] Ishibashi K, Kuwahara M, Gu Y, et al. (1997) Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol and urea. J Biol Chem 272: 20782-20786. doi: 10.1074/jbc.272.33.20782
    [10] Soupene E, King N, Lee H, et al. (2001) Aquaporin Z of Escherichia coli: Reassessment of Its Regulation and Physiological Role. J Bacter 184: 4304-4307.
    [11] Calamita G, Kempf B, Bonhivers B, et al. (1998) Regulation of the Escherichia coli water channel gene AqpZ. Proc Natl Acad Sci U S A 95: 3627-3631. doi: 10.1073/pnas.95.7.3627
    [12] Borgnia MJ, Kozono D, Calamita G, et al. (1999) Funcation Reconstitution and Characterization of AqpZ, the E. coli Water Channel Protein. J Mol Biol 291: 1169-1179.
    [13] Kozono D, Yasui M, King LS, et al. (2002). Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine. J Clin Inves 109: 1395-1399. doi: 10.1172/JCI0215851
    [14] Nemeth-Cahalan KL, Hall JE (2000) pH and Calcium Regulate the Water Permeability of Aquaporin 0. J Biol Chem 275: 6777-6782. doi: 10.1074/jbc.275.10.6777
    [15] Cahalan K, Kalman K, Hall JE (2004) Molecular Basis of pH and Ca2+ Regulation of Aquaporin Water Permeability. J Gen Physiol 123: 573-580
    [16] Zhou W, Jones SW (1996) The effects of external pH on calcium channel currents in bullfrog sympathetic neurons. Biophys J 70: 1326-1334
    [17] Gonen T, Walz T (2006) The structure of aquaporins. Q Rev Biophys 39: 361-396.
    [18] Chaumont F, Moshelion F, Daniels MJ (2005) Regulation of plant aquaporin activity. Biol Cell 97: 749-764. doi: 10.1042/BC20040133
    [19] Tong J, Canty JT, Briggs MM, et al. (2013) The water permeability of lens aquaporin-0 depends on its lipid bilayer environment. Exp Eye Res 113: 32-40. doi: 10.1016/j.exer.2013.04.022
    [20] Andersen OS, Bruno MJ, Sun H, et al. (2007) Single-molecule methods for monitoring changes in bilayer elastic properties. Meth Mol Biol 400: 543-570 doi: 10.1007/978-1-59745-519-0_37
    [21] Hong H, Tamm LK (2004) Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc Natl Acad Sci U S A 101: 4065-4070. doi: 10.1073/pnas.0400358101
    [22] Nyholm TK, Ozdirekcan S, Killian JA (2007) How protein transmembrane segments sense the lipid environment. Biochemistry 46: 1457-1465. doi: 10.1021/bi061941c
    [23] Phillips R, Ursell T, Wiggins P, et al. (2009) Emerging roles for lipids in shaping membrane-protein function. Nature 459: 379-385. doi: 10.1038/nature08147
    [24] Yuan C, O'Connell RJ, Jacob RF, et al. (2007) Regulation of the gating of BKCa channel by lipid bilayer thickness. J Biol Chem 282: 7276-7286.
    [25] Dumas F, Tocanne JF, Leblanc G, et al. (2000) Consequences of hydrophobic mismatch between lipids and melibiose permease on melibiose transport. Biochem 39: 4846-4854. doi: 10.1021/bi992634s
    [26] Perozo E, Kloda A, Cortes DM, et al. (2002) Physical principles underlying the transduction of bilayer deformation forces during mechano senditive channel gating. Nat Struct Biol 9: 696-703. doi: 10.1038/nsb827
    [27] Xie W, He F, Wang B, et al. (2013) An aquaporin-based vesicle-embedded polymeric membrane for low energy water filtration. J Mater Chem A 1: 7592-7600. doi: 10.1039/c3ta10731k
    [28] Wang H, Chung TS, Tong YW, et al. (2011) Preparation and characterization of pore-suspending biomimetic membranes embedded with Aquaporin Z on carboxylated polyethylene glycol polymer cushion. Soft Matter 7: 7274-7280.
    [29] Wang H, Chung TS, Tong YW, et al. (2012) Highly permeable and selective pore-spanning biomimetic membrane embedded with aquaporin Z. Small 8: 1185-1190, 1125.
    [30] Duong PHH, Chung TS, Jeyaseelan K, et al. (2012) Planar biomimetic aquaporin-incorporated triblock copolymer membranes on porous alumina supports for nanofiltration. J Membr Sci 409: 34-43.
    [31] Zhong PS, Chung TS, Jeyaseelan K, et al. (2012) Aquaporin-embedded biomimetic membranes for nanofiltration. J Membr Sci 407: 27-33.
    [32] Savage DF, Egea PF, Colmenares YR, et al. (2013) Architecture and selectivity in aquaporins: 2.5A X-Ray Structure of Aquaporin Z. PLoS Biol 1: 334-340.
    [33] Nielsen CH (2009) Biomimetic membranes for sensor and separation applications. Bioanal Chem 395: 697-718. doi: 10.1007/s00216-009-2960-0
    [34] Discher DE, Eisenberg A(2002) Polymer vesicles. Science 297: 967-973.
    [35] Ahmed F, Photos PJ, Discher DE (2006) Polymersomes as viral capsid mimics. Drug Develop Res 67: 4-14. doi: 10.1002/ddr.20062
    [36] Lewis BA, Engelman DM (1983) Lipid Bilayer Thickness Varies Linearly with Acyl Chain Length in Fluid Phosphatidylcholine Vesicles. J Mol Biol 166: 211-217. doi: 10.1016/S0022-2836(83)80007-2
    [37] Dave PC, Tiburu EK, Damodaran K, et al. (2004) Investigating Structural Changes in the Lipid Bilayer upon Insertion of the Transmembrane Domain of the Membrane-Bound Protein Phospholamban Utilizing 31P and 2H Solid-State NMR Spectroscopy. Biophys J 86: 1564-1573. doi: 10.1016/S0006-3495(04)74224-1
    [38] Marsh D (2008) Energetics of Hydrophobic Matching in Lipid-Protein Interactions. Biophys J 94: 3996-4013.
    [39] Xu Q, Kim M, David Ho KW, et al. (2008) Membrane Hydrocarbon Thickness Modulates the Dynamics of a Membrane Transport Protein. Biophys J 95: 2849-2858. doi: 10.1529/biophysj.108.133629
    [40] He F, Tong YW (2014) A mechanistic study on amphiphilic block co-polymer poly(butadiene-b-(ethylene oxide)) vesicles reveals the water permeation mechanism through a polymeric bilayer. RSC Adv 4: 15304-15313. doi: 10.1039/c3ra48063a
    [41] Yang B, Verkman AS (1997) Water and Glycerol Permeabilities of Aquaporins 1-5 and MIP Determined Quantitatively by Expression of Epitope-tagged Constructs in Xenopus Oocytes. J Biol Chem 272: 16140-16146. doi: 10.1074/jbc.272.26.16140
    [42] Mehdizadeh H, Dickson JM, Eriksson PK (1989) Temperature effects on the performance of thin-film composite, aromatic polyamide membranes. Ind Eng Chem Res 28: 814-824. doi: 10.1021/ie00090a025
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