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Volumn 1764, Issue 3, 2006, Pages 424-433

Incorporation of α-chymotrypsin into the 3D channels of bicontinuous cubic lipid mesophases

Author keywords

chymotrypsin; Cubic phase; Cytochrome c; FT IR; High pressure; Lipid; Monoolein; SAXD

Indexed keywords

CHYMOTRYPSIN A; CYTOCHROME C; GLYCEROL OLEATE; LIPID; WATER;

EID: 33646478538     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.11.004     Document Type: Article
Times cited : (39)

References (44)
  • 1
  • 3
    • 4644332696 scopus 로고    scopus 로고
    • Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration and volumetric properties
    • Ravindra R., Zhao S., Gies H., and Winter R. Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration and volumetric properties. J. Am. Chem. Soc. 126 (2004) 12224-12225
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12224-12225
    • Ravindra, R.1    Zhao, S.2    Gies, H.3    Winter, R.4
  • 4
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter R. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Biochim. Biophys. Acta 1595 (2002) 160-184
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 160-184
    • Winter, R.1
  • 5
    • 21644459337 scopus 로고    scopus 로고
    • Temperature-pressure configurational landscape of lipid bilayers and proteins
    • Winter R., and Dzwolak W. Temperature-pressure configurational landscape of lipid bilayers and proteins. Cell. Mol. Biol. 50 (2004) 397-417
    • (2004) Cell. Mol. Biol. , vol.50 , pp. 397-417
    • Winter, R.1    Dzwolak, W.2
  • 7
    • 0000044172 scopus 로고
    • Cubic phases of self-assembled amphiphilic aggregates
    • Seddon J.M., and Templer R. Cubic phases of self-assembled amphiphilic aggregates. Philos. Trans. R. Soc. Lond., A 344 (1993) 377-401
    • (1993) Philos. Trans. R. Soc. Lond., A , vol.344 , pp. 377-401
    • Seddon, J.M.1    Templer, R.2
  • 8
    • 0025134135 scopus 로고
    • Structure of the inverted hexagonal (HII) phase, and non-lamellar phase transitions of lipids
    • Seddon J.M. Structure of the inverted hexagonal (HII) phase, and non-lamellar phase transitions of lipids. Biochim. Biophys. Acta 1301 (1990) 1-69
    • (1990) Biochim. Biophys. Acta , vol.1301 , pp. 1-69
    • Seddon, J.M.1
  • 9
    • 0034215980 scopus 로고    scopus 로고
    • Electron density modeling and reconstruction of infinite periodic minimal surfaces (IPMS) based phases in lipid-water systems
    • Harper P.E., and Gruner S.M. Electron density modeling and reconstruction of infinite periodic minimal surfaces (IPMS) based phases in lipid-water systems. Eur. Phys. J., E 2 (2000) 217-228
    • (2000) Eur. Phys. J., E , vol.2 , pp. 217-228
    • Harper, P.E.1    Gruner, S.M.2
  • 10
    • 0032705083 scopus 로고    scopus 로고
    • Cubic membrane structure in amoeba (chaos carolinensis) mitochondria determined by electron microscopic tomography
    • Deng Y., Marko M., Buttle K.F., Leith A., Mierczkowski M., and Mannella C.A. Cubic membrane structure in amoeba (chaos carolinensis) mitochondria determined by electron microscopic tomography. J. Struct. Biol. 127 (1999) 231-239
    • (1999) J. Struct. Biol. , vol.127 , pp. 231-239
    • Deng, Y.1    Marko, M.2    Buttle, K.F.3    Leith, A.4    Mierczkowski, M.5    Mannella, C.A.6
  • 11
    • 4243287522 scopus 로고    scopus 로고
    • A systematic approach to bicontinuous cubic phases in ternary amphiphilic systems
    • Schwarz U.S., and Gompper G. A systematic approach to bicontinuous cubic phases in ternary amphiphilic systems. Phys. Rev., E 59 (1999) 5528-5541
    • (1999) Phys. Rev., E , vol.59 , pp. 5528-5541
    • Schwarz, U.S.1    Gompper, G.2
  • 12
    • 0034250507 scopus 로고    scopus 로고
    • Stability of inverse bicontinuous cubic phases in lipid-water mixtures
    • Schwarz U.S., and Gompper G. Stability of inverse bicontinuous cubic phases in lipid-water mixtures. Phys. Rev. Lett. 85 (2000) 1472-1475
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 1472-1475
    • Schwarz, U.S.1    Gompper, G.2
  • 13
    • 2942515643 scopus 로고    scopus 로고
    • Phase behavior of amphiphilic systems
    • Schwarz U.S. Phase behavior of amphiphilic systems. Acta Phys. Pol., B 29 (1998) 1815-1825
    • (1998) Acta Phys. Pol., B , vol.29 , pp. 1815-1825
    • Schwarz, U.S.1
  • 14
    • 0032974263 scopus 로고    scopus 로고
    • Stabilization of monoolein Pn3m cubic structure on trehalose glasses
    • Mariani P., Rustichelli F., Saturni L., and Cordone L. Stabilization of monoolein Pn3m cubic structure on trehalose glasses. Eur. Biophys. J. 28 (1999) 294-301
    • (1999) Eur. Biophys. J. , vol.28 , pp. 294-301
    • Mariani, P.1    Rustichelli, F.2    Saturni, L.3    Cordone, L.4
  • 15
    • 0037134580 scopus 로고    scopus 로고
    • Pressure induced cubic-to-cubic phase transition in monoolein hydrated system
    • Pisani M., Bernstorff S., Ferrero C., and Mariani P. Pressure induced cubic-to-cubic phase transition in monoolein hydrated system. J. Phys. Chem., B 105 (2001) 3109-3119
    • (2001) J. Phys. Chem., B , vol.105 , pp. 3109-3119
    • Pisani, M.1    Bernstorff, S.2    Ferrero, C.3    Mariani, P.4
  • 16
    • 0033813740 scopus 로고    scopus 로고
    • Pressure effects on the structure of lyotropic lipid mesophases and model biomembrane systems
    • Winter R., and Czeslik C. Pressure effects on the structure of lyotropic lipid mesophases and model biomembrane systems. Z. Kristallogr. 215 (2000) 454-474
    • (2000) Z. Kristallogr. , vol.215 , pp. 454-474
    • Winter, R.1    Czeslik, C.2
  • 17
    • 0042890298 scopus 로고    scopus 로고
    • Lipid cubic phases as stable nanochannel network structures for protein biochip development: X-ray diffraction study
    • Angelova A., Ollivon M., Campitelli A., and Bourgaux C. Lipid cubic phases as stable nanochannel network structures for protein biochip development: X-ray diffraction study. Langmuir 19 (2003) 6928-6935
    • (2003) Langmuir , vol.19 , pp. 6928-6935
    • Angelova, A.1    Ollivon, M.2    Campitelli, A.3    Bourgaux, C.4
  • 20
    • 0033361183 scopus 로고    scopus 로고
    • Surfactant self-assembly objects as novel drug delivery vehicles
    • Drummond C.J., and Fong C. Surfactant self-assembly objects as novel drug delivery vehicles. Curr. Opin. Colloid Interface Sci. 4 (1999) 449-456
    • (1999) Curr. Opin. Colloid Interface Sci. , vol.4 , pp. 449-456
    • Drummond, C.J.1    Fong, C.2
  • 21
    • 0031713288 scopus 로고    scopus 로고
    • Bioadhesive drug delivery systems: I. Characterisation of mucoadhesive properties of systems based on glyceryl mono-oleate and glyceryl monolinoleate
    • Nielsen L.S., Schubert L., and Hansen J. Bioadhesive drug delivery systems: I. Characterisation of mucoadhesive properties of systems based on glyceryl mono-oleate and glyceryl monolinoleate. Eur. J. Pharm. Sci. 6 (1998) 231-239
    • (1998) Eur. J. Pharm. Sci. , vol.6 , pp. 231-239
    • Nielsen, L.S.1    Schubert, L.2    Hansen, J.3
  • 23
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey M. Membrane protein crystallization. J. Struct. Biol. 142 (2003) 108-132
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 24
    • 85032428758 scopus 로고    scopus 로고
    • Crystallization of a globular protein in lipid cubic phase
    • (128102-1-4)
    • Tanaka S., Egelhaaf S.U., and Poon W.C.K. Crystallization of a globular protein in lipid cubic phase. Phys. Rev. Lett. 92 (2004) (128102-1-4)
    • (2004) Phys. Rev. Lett. , vol.92
    • Tanaka, S.1    Egelhaaf, S.U.2    Poon, W.C.K.3
  • 25
    • 0037390283 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cubic monoolein mesophases under limited hydration conditions: the effects of concentration, temperature and pressure
    • Lendermann J., and Winter R. Interaction of cytochrome c with cubic monoolein mesophases under limited hydration conditions: the effects of concentration, temperature and pressure. Phys. Chem. Chem. Phys. 5 (2003) 1440-1450
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 1440-1450
    • Lendermann, J.1    Winter, R.2
  • 26
    • 17444397095 scopus 로고    scopus 로고
    • Kinetics of lamellar-to-cubic and intercubic phase transitions of pure and cytochrome c containing monoolein dispersions monitored by time-resolved small-angle X-ray diffraction
    • Kraineva J., Narayanan R., Kondrashkina E., Thiyagarajan P., and Winter R. Kinetics of lamellar-to-cubic and intercubic phase transitions of pure and cytochrome c containing monoolein dispersions monitored by time-resolved small-angle X-ray diffraction. Langmuir 21 (2005) 3559-3571
    • (2005) Langmuir , vol.21 , pp. 3559-3571
    • Kraineva, J.1    Narayanan, R.2    Kondrashkina, E.3    Thiyagarajan, P.4    Winter, R.5
  • 27
    • 0025357111 scopus 로고
    • Protein secondary structures in water from 2nd-derivative amide-I infrared spectra
    • Dong A., Huang P., and Caughey W.S. Protein secondary structures in water from 2nd-derivative amide-I infrared spectra. Biochemistry 29 (1990) 3303-3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 28
    • 17444382363 scopus 로고    scopus 로고
    • Pressure-induced protein unfolding in the ternary system AOT-octane-water is different from that in bulk water
    • Meersman F., Dirix C., Shipovskov S., Klyachko N.L., and Heremans K. Pressure-induced protein unfolding in the ternary system AOT-octane-water is different from that in bulk water. Langmuir 21 (2005) 3599-3604
    • (2005) Langmuir , vol.21 , pp. 3599-3604
    • Meersman, F.1    Dirix, C.2    Shipovskov, S.3    Klyachko, N.L.4    Heremans, K.5
  • 29
    • 0000706608 scopus 로고    scopus 로고
    • High pressure-jump apparatus for kinetic studies of protein folding reactions using the small-angle synchrotron X-ray scattering technique
    • Woenckhaus J., Köhling R., Winter R., Thiyagarajan P., and Finet S. High pressure-jump apparatus for kinetic studies of protein folding reactions using the small-angle synchrotron X-ray scattering technique. Rev. Sci. Instrum. 71 (2000) 3895-3899
    • (2000) Rev. Sci. Instrum. , vol.71 , pp. 3895-3899
    • Woenckhaus, J.1    Köhling, R.2    Winter, R.3    Thiyagarajan, P.4    Finet, S.5
  • 30
    • 0033580649 scopus 로고    scopus 로고
    • Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering
    • Panick G., Malessa R., and Winter R. Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry 38 (1999) 6512-6519
    • (1999) Biochemistry , vol.38 , pp. 6512-6519
    • Panick, G.1    Malessa, R.2    Winter, R.3
  • 31
    • 0038690115 scopus 로고    scopus 로고
    • Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein-a static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study
    • Herberhold H., Marchal S., Lange R., Scheyhing C.H., Vogel R.F., and Winter R. Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein-a static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study. J. Mol. Biol. 330 (2003) 1153-1164
    • (2003) J. Mol. Biol. , vol.330 , pp. 1153-1164
    • Herberhold, H.1    Marchal, S.2    Lange, R.3    Scheyhing, C.H.4    Vogel, R.F.5    Winter, R.6
  • 32
    • 0001090283 scopus 로고
    • Crystalline quartz as an internal pressure calibrant for high-pressure infrared spectroscopy
    • Wong P.T.T., Moffatt J., and Baudais F.L. Crystalline quartz as an internal pressure calibrant for high-pressure infrared spectroscopy. Appl. Spectrosc. 39 (1985) 733-735
    • (1985) Appl. Spectrosc. , vol.39 , pp. 733-735
    • Wong, P.T.T.1    Moffatt, J.2    Baudais, F.L.3
  • 33
    • 0030148764 scopus 로고    scopus 로고
    • The temperature-composition phase diagram and mesophase structure characterization of the monoolein/water system
    • Briggs J., Chung H., and Caffrey M. The temperature-composition phase diagram and mesophase structure characterization of the monoolein/water system. J. Phys. II 6 (1996) 723-751
    • (1996) J. Phys. II , vol.6 , pp. 723-751
    • Briggs, J.1    Chung, H.2    Caffrey, M.3
  • 34
    • 0032754454 scopus 로고    scopus 로고
    • FTIR-monitoring reveals different mechanisms for the alkaline isomerization of tuna compared to horse and bovine cytochromes c
    • Filosa A., Ismail A.A., and English A.M. FTIR-monitoring reveals different mechanisms for the alkaline isomerization of tuna compared to horse and bovine cytochromes c. J. Biol. Inorg. Chem. 4 (1999) 717-726
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 717-726
    • Filosa, A.1    Ismail, A.A.2    English, A.M.3
  • 35
    • 1642463952 scopus 로고    scopus 로고
    • Superactivity and conformational changes on α-chymotrypsin upon interfacial binding to cationic micelles
    • Celej M.S., D'Andrea M.G., Campana P.T., Fidelio G.D., and Bianconi M.L. Superactivity and conformational changes on α-chymotrypsin upon interfacial binding to cationic micelles. Biochem. J. 378 (2004) 1059-1066
    • (2004) Biochem. J. , vol.378 , pp. 1059-1066
    • Celej, M.S.1    D'Andrea, M.G.2    Campana, P.T.3    Fidelio, G.D.4    Bianconi, M.L.5
  • 36
    • 0028290981 scopus 로고
    • Fourier transform infrared spectra studies of protein in reverse micelles: effect of AOT/isooctane on the secondary structure of α-chymotrypsin
    • Qinglong C., Huizhou L., and Jiayong C. Fourier transform infrared spectra studies of protein in reverse micelles: effect of AOT/isooctane on the secondary structure of α-chymotrypsin. Biochim. Biophys. Acta 1206 (1994) 247-252
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 247-252
    • Qinglong, C.1    Huizhou, L.2    Jiayong, C.3
  • 37
    • 0000810947 scopus 로고
    • Spectroscopic and rheological studies of enzymes in rigid lipidic matrices: the case of α-chymotrypsin in lysolectin/water phase
    • Portmann M., Landau E.M., and Luisi P.L. Spectroscopic and rheological studies of enzymes in rigid lipidic matrices: the case of α-chymotrypsin in lysolectin/water phase. J. Phys. Chem. 95 (1991) 8437-8440
    • (1991) J. Phys. Chem. , vol.95 , pp. 8437-8440
    • Portmann, M.1    Landau, E.M.2    Luisi, P.L.3
  • 38
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 39
    • 3543030409 scopus 로고    scopus 로고
    • Hydration and packing effects on prion folding and β-sheet conversion: high-pressure spectroscopy and pressure perturbation calorimetry studies
    • Cordeiro Y., Kraineva J., Ravindra R., Lima L.M.T.R., Gomes M.P.B., Foguel D., Winter R., and Silva J.L. Hydration and packing effects on prion folding and β-sheet conversion: high-pressure spectroscopy and pressure perturbation calorimetry studies. J. Biol. Chem. 279 (2004) 32354-32359
    • (2004) J. Biol. Chem. , vol.279 , pp. 32354-32359
    • Cordeiro, Y.1    Kraineva, J.2    Ravindra, R.3    Lima, L.M.T.R.4    Gomes, M.P.B.5    Foguel, D.6    Winter, R.7    Silva, J.L.8
  • 40
    • 0141567910 scopus 로고    scopus 로고
    • Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy
    • Dzwolak W., Ravindra R., Lendermann J., and Winter R. Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy. Biochemistry 42 (2003) 11347-11355
    • (2003) Biochemistry , vol.42 , pp. 11347-11355
    • Dzwolak, W.1    Ravindra, R.2    Lendermann, J.3    Winter, R.4
  • 41
    • 1542461687 scopus 로고    scopus 로고
    • Temperature- and pressure-induced unfolding of α-chymotrypsin
    • Winter R. (Ed), Springer-Verlag, Heidelberg
    • Sun Z., and Winter R. Temperature- and pressure-induced unfolding of α-chymotrypsin. In: Winter R. (Ed). High Pressure Bioscience and Biotechnology II (2003), Springer-Verlag, Heidelberg 117-120
    • (2003) High Pressure Bioscience and Biotechnology II , pp. 117-120
    • Sun, Z.1    Winter, R.2
  • 42
    • 0014335164 scopus 로고
    • Molecular conformation of chymotrypsinogen and chymotrypsin by low-angle X-ray diffraction
    • Krigbaum W.R., and Godwin R.W. Molecular conformation of chymotrypsinogen and chymotrypsin by low-angle X-ray diffraction. Biochemistry 7 (1968) 3126-3131
    • (1968) Biochemistry , vol.7 , pp. 3126-3131
    • Krigbaum, W.R.1    Godwin, R.W.2
  • 43
    • 0014955652 scopus 로고
    • Concerning the mechanism of autolysis of α-chymotrypsin
    • Kumar S., and Hein G.E. Concerning the mechanism of autolysis of α-chymotrypsin. Biochemistry 9 (1970) 291-297
    • (1970) Biochemistry , vol.9 , pp. 291-297
    • Kumar, S.1    Hein, G.E.2
  • 44


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