메뉴 건너뛰기




Volumn 74, Issue 4, 1998, Pages 1871-1888

Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion

Author keywords

[No Author keywords available]

Indexed keywords

CORTICOTROPIN; DODECYL SULFATE SODIUM; PHOSPHORYLCHOLINE; WATER;

EID: 0031920741     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77897-X     Document Type: Article
Times cited : (65)

References (43)
  • 2
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A., and D. G. Davis. 1985. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Keson. 63:207-213.
    • (1985) J. Magn. Keson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 3
    • 45149138663 scopus 로고
    • Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins
    • Bax, A., M. Ikura, L. E. Kay, D. A. Torchia, and R. Tschudin. 1990. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins. J. Magn. Reson. 86:304-318.
    • (1990) J. Magn. Reson. , vol.86 , pp. 304-318
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Torchia, D.A.4    Tschudin, R.5
  • 4
    • 0026808783 scopus 로고
    • Peptide binding to lipid bilayers: Nonclassical hydrophobic effect and membrane-induced pK shifts
    • Beschiaschvili, G., and J. Seelig. 1992. Peptide binding to lipid bilayers: nonclassical hydrophobic effect and membrane-induced pK shifts. Biochemistry: 31:10044-10053.
    • (1992) Biochemistry , vol.31 , pp. 10044-10053
    • Beschiaschvili, G.1    Seelig, J.2
  • 5
    • 48549112001 scopus 로고
    • Selection of coherence transfer pathways in NMR pulse experiments
    • Bodenhauscn, G., H. Kogler, and R. R. Ernst. 1984. Selection of coherence transfer pathways in NMR pulse experiments. J. Magn. Reson. 58: 370-388.
    • (1984) J. Magn. Reson. , vol.58 , pp. 370-388
    • Bodenhauscn, G.1    Kogler, H.2    Ernst, R.R.3
  • 6
    • 0344658997 scopus 로고
    • Partial molal volume and isentropic partial molal compressibilities of surface active agents in squeous solution
    • Brun,T. S., H. Hoiland, and E. Vikingstad. 1978. Partial molal volume and isentropic partial molal compressibilities of surface active agents in squeous solution. J. Colloid Interface Sci. 63:89-96.
    • (1978) J. Colloid Interface Sci. , vol.63 , pp. 89-96
    • Brun, T.S.1    Hoiland, H.2    Vikingstad, E.3
  • 8
    • 0001497127 scopus 로고
    • Influence of salt, detergent concentration, and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecylsulfate with mdichlorobenzene
    • Croonen, Y., E. Gelade, M. Van der Zegel, N. Van der Auweraer, H. Vandendriessche, F. C. DeSchryver, and M. Almgren. 1983. Influence of salt, detergent concentration, and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecylsulfate with mdichlorobenzene. J. Phys. Chem. 87:1426-1431.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1426-1431
    • Croonen, Y.1    Gelade, E.2    Van Der Zegel, M.3    Van Der Auweraer, N.4    Vandendriessche, H.5    DeSchryver, F.C.6    Almgren, M.7
  • 9
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartman-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartman-Hahn spectroscopy. J. Am. Chem. Soc. 107:2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, G.1    Bax, A.2
  • 11
    • 0021115856 scopus 로고
    • Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • Gremlich, H. U., U. P. Frigeli, and R. Schwyzer. 1983. Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry: 22:4257-4264.
    • (1983) Biochemistry , vol.22 , pp. 4257-4264
    • Gremlich, H.U.1    Frigeli, U.P.2    Schwyzer, R.3
  • 12
    • 0021327175 scopus 로고
    • Interaction of adrenocorticotropin-(11-24)-tetradecapeptide with neutral lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • Gremlich, H. U., U. P. Frigeli, and R. Schwyzer. 1984. Interaction of adrenocorticotropin-(11-24)-tetradecapeptide with neutral lipid membranes revealed by infrared attenuated total reflection spectroscopy. Biochemistry: 23:1808-1810.
    • (1984) Biochemistry , vol.23 , pp. 1808-1810
    • Gremlich, H.U.1    Frigeli, U.P.2    Schwyzer, R.3
  • 14
    • 0021319101 scopus 로고
    • Hydrophobic and electrostatic interactions between adrenocorticotropin-(1-24)-tetracosapeptide and lipid vesicles. Amphiphilic primary structures
    • Gysin, B., and R. Schwyzer. 1984. Hydrophobic and electrostatic interactions between adrenocorticotropin-(1-24)-tetracosapeptide and lipid vesicles. Amphiphilic primary structures. Biochemistry. 23:1811-1818.
    • (1984) Biochemistry , vol.23 , pp. 1811-1818
    • Gysin, B.1    Schwyzer, R.2
  • 15
    • 0001404190 scopus 로고
    • Distance distribution function of sodium dodecylsulfate micelles by x-ray scattering
    • Itri, R., and L. Q. Amaral. 1991. Distance distribution function of sodium dodecylsulfate micelles by x-ray scattering. J. Phys. Chem. 95:423-427.
    • (1991) J. Phys. Chem. , vol.95 , pp. 423-427
    • Itri, R.1    Amaral, L.Q.2
  • 16
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., B. Meier, P. Bachman, and R. R. Ernst. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.2    Bachman, P.3    Ernst, R.R.4
  • 19
    • 0029981186 scopus 로고    scopus 로고
    • The conformation of substance P in lipid environment
    • Keire, D., and T. G. Fletcher. 1996. The conformation of substance P in lipid environment. Biophys. J. 70:1716-1727.
    • (1996) Biophys. J. , vol.70 , pp. 1716-1727
    • Keire, D.1    Fletcher, T.G.2
  • 20
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOR) experiment for the elucidation of complete proton-proton cross relaxation networks in biological macromolecules
    • Kumar, A., R. R. Ernst, and K. Wuthrich. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOR) experiment for the elucidation of complete proton-proton cross relaxation networks in biological macromolecules. Biochim. Biophys. Res. Commun. 95:1-10.
    • (1980) Biochim. Biophys. Res. Commun. , vol.95 , pp. 1-10
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 21
    • 0018798032 scopus 로고
    • Physico-chemical studies of the protein-lipid interactions in melittin-containing micelles
    • Lauterwein, J., C. Bosch, L. R. Brown, and K. Wuthrich. 1979. Physico-chemical studies of the protein-lipid interactions in melittin-containing micelles. Biochim. Biophys. Acta. 556:244-264.
    • (1979) Biochim. Biophys. Acta. , vol.556 , pp. 244-264
    • Lauterwein, J.1    Bosch, C.2    Brown, L.R.3    Wuthrich, K.4
  • 22
    • 0347963579 scopus 로고
    • Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution. Decreased fluidity of the micelle hydrocarbon interior
    • MacKerell, A. D. 1995. Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution. Decreased fluidity of the micelle hydrocarbon interior. J. Phys. Chem. 99:1946-1855.
    • (1995) J. Phys. Chem. , vol.99 , pp. 1946-11855
    • MacKerell, A.D.1
  • 23
    • 0042936805 scopus 로고
    • Self-diffusion in normal and heavy water in the range 1-45°
    • Mills, R. 1973. Self-diffusion in normal and heavy water in the range 1-45°. J. Phys. Chem. 77:685-688.
    • (1973) J. Phys. Chem. , vol.77 , pp. 685-688
    • Mills, R.1
  • 24
    • 33751157899 scopus 로고
    • Diffusion study of the polymer-induced non-Newtonian to Newtonian transition in the viscoelastic CTAB/sodium salicylate/water system by diffusion ordered spectroscopy (DOSY)
    • Morris, K. F., C. S. Johnson, Jr., and T. C. Wong. 1994. Diffusion study of the polymer-induced non-Newtonian to Newtonian transition in the viscoelastic CTAB/sodium salicylate/water system by diffusion ordered spectroscopy (DOSY). J. Phys. Chem. 98.603-608.
    • (1994) J. Phys. Chem. , vol.98 , pp. 603-608
    • Morris, K.F.1    Johnson C.S., Jr.2    Wong, T.C.3
  • 25
    • 37049105858 scopus 로고
    • 1H nuclear magnetic resonance studies of the conformations of adrenocorticotropic hormone ACTH (1-10) and related peptides in aqueous and trifluoroethanol solutions
    • 1H nuclear magnetic resonance studies of the conformations of adrenocorticotropic hormone ACTH (1-10) and related peptides in aqueous and trifluoroethanol solutions. J. Chem. Soc. Perkin Trans. II. 1471-1477.
    • (1982) J. Chem. Soc. Perkin Trans. II , pp. 1471-1477
    • Rawson, B.J.1    Feeney, J.2    Kimber, B.J.3
  • 26
    • 0038757797 scopus 로고
    • Membrane lipid phase as catalyst for peptide-receptor interactions
    • Sargent, D. F., and R. Schwyzer. 1986. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Natl. Acad. Sci. USA. 83:5774-5778.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5774-5778
    • Sargent, D.F.1    Schwyzer, R.2
  • 27
    • 0017620408 scopus 로고
    • ACTH: A short introductory review
    • Schwyzer, R. 1977. ACTH: a short introductory review. Ann. N.Y. Acad. Sci. 297:3-26.
    • (1977) Ann. N.Y. Acad. Sci. , vol.297 , pp. 3-26
    • Schwyzer, R.1
  • 28
    • 0023024852 scopus 로고
    • Molecular mechanism of opioid receptor selection
    • Schwyzer, R. 1986. Molecular mechanism of opioid receptor selection. Biochemistry: 25:6335-6342.
    • (1986) Biochemistry , vol.25 , pp. 6335-6342
    • Schwyzer, R.1
  • 29
    • 0026155119 scopus 로고
    • Peptide membrane interactions and a new principle in quantitative structure activity relationships
    • Schwyzer, R. 1991. Peptide membrane interactions and a new principle in quantitative structure activity relationships. Biopolymers. 31:785-792.
    • (1991) Biopolymers , vol.31 , pp. 785-792
    • Schwyzer, R.1
  • 30
    • 0000404051 scopus 로고
    • Conformations and orientations of amphiphilic peptides induced by artificial lipid membranes: Correlations with biological activity
    • Schwyzer, R. 1992. Conformations and orientations of amphiphilic peptides induced by artificial lipid membranes: correlations with biological activity. Chemtracts Biochem. Mol. Biol. 3:347-379.
    • (1992) Chemtracts Biochem. Mol. Biol. , vol.3 , pp. 347-379
    • Schwyzer, R.1
  • 31
    • 0027525276 scopus 로고
    • Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = +1 to z = +3
    • Seelig, J., S. Nebel, P. Ganz, and C. Bruns. 1993. Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = +1 to z = +3. Biochemistry. 32:9714-9721.
    • (1993) Biochemistry , vol.32 , pp. 9714-9721
    • Seelig, J.1    Nebel, S.2    Ganz, P.3    Bruns, C.4
  • 32
    • 0003062277 scopus 로고
    • Simplification of NMR spectra through multiple-quantum coherence
    • Shaka, A. J., and R. Freeman. 1983. Simplification of NMR spectra through multiple-quantum coherence. J. Magn. Reson. 51:169-173.
    • (1983) J. Magn. Reson. , vol.51 , pp. 169-173
    • Shaka, A.J.1    Freeman, R.2
  • 34
  • 35
    • 0009595872 scopus 로고
    • Fourier transform NMR pulsed-gradiem spin-echo (FTPGSE) self-diffusion measurements of solubilization equilibria in SDS solutions
    • Stilbs, P. 1982. Fourier transform NMR pulsed-gradiem spin-echo (FTPGSE) self-diffusion measurements of solubilization equilibria in SDS solutions J. Colloid Interface Sci. 87:385-394.
    • (1982) J. Colloid Interface Sci. , vol.87 , pp. 385-394
    • Stilbs, P.1
  • 36
    • 0000570993 scopus 로고
    • A comparative study of micellar solubilization for combinations of surfactants and solubilizates using the Fourier transform pulsed-gradient spin-echo NMR multicomponent self-diffusion technique
    • Stilbs, P. 1983. A comparative study of micellar solubilization for combinations of surfactants and solubilizates using the Fourier transform pulsed-gradient spin-echo NMR multicomponent self-diffusion technique. J. Colloid Interface Sci. 94:463-469.
    • (1983) J. Colloid Interface Sci. , vol.94 , pp. 463-469
    • Stilbs, P.1
  • 37
    • 34047191652 scopus 로고
    • Fourier transform pulsed field gradient spin-echo studies of molecular diffusion
    • Stilbs, P. 1987. Fourier transform pulsed field gradient spin-echo studies of molecular diffusion. Prog. NMR Spectrosc. 19:1-45.
    • (1987) Prog. NMR Spectrosc. , vol.19 , pp. 1-45
    • Stilbs, P.1
  • 38
    • 36849101148 scopus 로고
    • Use of the stimulated echo in NMR diffusion studies
    • Tanner, J. E. 1970. Use of the stimulated echo in NMR diffusion studies. J. Chem. Phys. 52:2523-2526.
    • (1970) J. Chem. Phys. , vol.52 , pp. 2523-2526
    • Tanner, J.E.1
  • 40
    • 0019466008 scopus 로고
    • 13C NMR studies of ACTH: Assignment of resonances and conformational feat tures
    • 13C NMR studies of ACTH: assignment of resonances and conformational feat tures. Biopolymers. 20:901-913.
    • (1981) Biopolymers , vol.20 , pp. 901-913
    • Toma, F.1    Fermandjian, S.2    Low, M.3    Kisfaludy, L.4
  • 41
    • 0026873397 scopus 로고
    • Two-dimensional NMR studies on 1-10 fragment of adrenocorticotropic hormone
    • Tunga, A., and R. V. Hosur. 1992. Two-dimensional NMR studies on 1-10 fragment of adrenocorticotropic hormone. Indian J. Biochem. Biophys. 29:231-235.
    • (1992) Indian J. Biochem. Biophys. , vol.29 , pp. 231-235
    • Tunga, A.1    Hosur, R.V.2
  • 42
    • 0029671284 scopus 로고    scopus 로고
    • 15N labeling method of peptides using a thioredoxin gene fusion expression system: An application to ACTh (1-24)
    • 15N labeling method of peptides using a thioredoxin gene fusion expression system: an application to ACTh (1-24). FEBS Lett. 379:47-50.
    • (1996) FEBS Lett. , vol.379 , pp. 47-50
    • Uegaki, K.1    Nemoto, N.2    Shimizu, M.3    Wada, T.4    Kyogoku, Y.5    Kobayashi, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.