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Volumn 93, Issue 3, 2007, Pages 866-875

Real-time structural investigation of a lipid bilayer during its interaction with melittin using sum frequency generation vibrational spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

DIPALMITOYLPHOSPHATIDYLGLYCEROL; MELITTIN; MOLECULAR MOTOR; PEPTIDE; PROTEIN;

EID: 34547653932     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.099739     Document Type: Article
Times cited : (83)

References (79)
  • 1
    • 26644444070 scopus 로고    scopus 로고
    • How lipids and proteins interact in a membrane: A molecular approach
    • Lee, A. G. 2005. How lipids and proteins interact in a membrane: a molecular approach. Mol. Biosyst. 1:203-212.
    • (2005) Mol. Biosyst , vol.1 , pp. 203-212
    • Lee, A.G.1
  • 2
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • McIntosh, T. J., and S. A. Simon. 2006. Roles of bilayer material properties in function and distribution of membrane proteins. Annu. Rev. Biophys. Biomol. Struct. 35:177-198.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature. 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. 2005. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3:238-250.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 5
    • 1942502913 scopus 로고    scopus 로고
    • pH-sensitive toxins: Interactions with membrane bilayers and application to drug delivery
    • Cabiaux, V. 2004. pH-sensitive toxins: interactions with membrane bilayers and application to drug delivery. Adv. Drug Deliv. Rev. 56: 987-997.
    • (2004) Adv. Drug Deliv. Rev , vol.56 , pp. 987-997
    • Cabiaux, V.1
  • 6
    • 0031695897 scopus 로고    scopus 로고
    • A new look at lipid-membrane structure in relation to drug research
    • Mouritsen, O. G., and K. Jorgensen. 1998. A new look at lipid-membrane structure in relation to drug research. Pharm. Res. 15:1507-1519.
    • (1998) Pharm. Res , vol.15 , pp. 1507-1519
    • Mouritsen, O.G.1    Jorgensen, K.2
  • 7
    • 0033350530 scopus 로고    scopus 로고
    • Nonlinear optics as a detection scheme for biomimetic sensors: SFG spectroscopy of hybrid bilayer membrane formation
    • Petralli-Mallow, T. P., K. A. Briggman, L. J. Richter, J. C. Stephenson, and A. L. Plant. 1999. Nonlinear optics as a detection scheme for biomimetic sensors: SFG spectroscopy of hybrid bilayer membrane formation. Proc. SPIE. 3858:25-31.
    • (1999) Proc. SPIE , vol.3858 , pp. 25-31
    • Petralli-Mallow, T.P.1    Briggman, K.A.2    Richter, L.J.3    Stephenson, J.C.4    Plant, A.L.5
  • 8
    • 6444223732 scopus 로고    scopus 로고
    • Protein deformation of lipid hybrid bilayer membranes studied by sum frequency generation vibrational spectroscopy
    • Doyle, A. W., J. Fick, M. Himmelhaus, W. Eck, I. Graziani, I. Prudovsky, M. Grunze, T. Maciag, and D. J. Neivandt. 2004. Protein deformation of lipid hybrid bilayer membranes studied by sum frequency generation vibrational spectroscopy. Langmuir. 20:8961-8965.
    • (2004) Langmuir , vol.20 , pp. 8961-8965
    • Doyle, A.W.1    Fick, J.2    Himmelhaus, M.3    Eck, W.4    Graziani, I.5    Prudovsky, I.6    Grunze, M.7    Maciag, T.8    Neivandt, D.J.9
  • 9
    • 26444482165 scopus 로고    scopus 로고
    • Structure of a gel phase lipid bilayer prepared by the Langmuir-Blodgett/Langmuir-Schaefer method characterized by sum-frequency vibrational spectroscopy
    • Liu, J., and J. C. Conboy. 2005. Structure of a gel phase lipid bilayer prepared by the Langmuir-Blodgett/Langmuir-Schaefer method characterized by sum-frequency vibrational spectroscopy. Langmuir. 21:9091-9097.
    • (2005) Langmuir , vol.21 , pp. 9091-9097
    • Liu, J.1    Conboy, J.C.2
  • 10
    • 25844515222 scopus 로고    scopus 로고
    • 1,2-diacyl-phosphatidylcholine flip-flop measured directly by sum-frequency vibrational spectroscopy
    • Liu, J., and J. C. Conboy. 2005. 1,2-diacyl-phosphatidylcholine flip-flop measured directly by sum-frequency vibrational spectroscopy. Biophys. J. 89:2522-2532.
    • (2005) Biophys. J , vol.89 , pp. 2522-2532
    • Liu, J.1    Conboy, J.C.2
  • 11
    • 3242816081 scopus 로고    scopus 로고
    • Phase transition of a single lipid bilayer measured by sum-frequency vibrational spectroscopy
    • Liu, J., and J. C. Conboy. 2004. Phase transition of a single lipid bilayer measured by sum-frequency vibrational spectroscopy. J. Am. Chem. Soc. 126:8894-8895.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8894-8895
    • Liu, J.1    Conboy, J.C.2
  • 12
    • 3142763239 scopus 로고    scopus 로고
    • Direct measurement of the transbilayer movement of phospholipids by sum-frequency vibrational spectroscopy
    • Liu, J., and J. C. Conboy. 2004. Direct measurement of the transbilayer movement of phospholipids by sum-frequency vibrational spectroscopy. J. Am. Chem. Soc. 126:8376-8377.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8376-8377
    • Liu, J.1    Conboy, J.C.2
  • 13
    • 9944237389 scopus 로고    scopus 로고
    • Investigations of polymyxin B-phospholipid interactions by vibrational sum frequency generation spectroscopy
    • Ohe, C., Y. Ida, S. Matsumoto, T. Sasaki, Y. Goto, A. Noi, T. Tsurumaru, and K. Itoh. 2004. Investigations of polymyxin B-phospholipid interactions by vibrational sum frequency generation spectroscopy. J. Phys. Chem. B. 108:18081-18087.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 18081-18087
    • Ohe, C.1    Ida, Y.2    Matsumoto, S.3    Sasaki, T.4    Goto, Y.5    Noi, A.6    Tsurumaru, T.7    Itoh, K.8
  • 14
    • 33745486388 scopus 로고    scopus 로고
    • DPPC Langmuir monolayer at the airwater interface: Probing the tail and head groups by vibrational sum frequency generation spectroscopy
    • Ma, G., and H. C. Allen. 2006. DPPC Langmuir monolayer at the airwater interface: probing the tail and head groups by vibrational sum frequency generation spectroscopy. Langmuir. 22:5341-5349.
    • (2006) Langmuir , vol.22 , pp. 5341-5349
    • Ma, G.1    Allen, H.C.2
  • 15
    • 0037433596 scopus 로고    scopus 로고
    • Molecular packing of lysozyme, fibrinogen, and bovine serum albumin on hydrophilic and hydrophobic surfaces studied by infrared-visible sum frequency generation and fluorescence microscopy
    • Kim, J., and G. A. Somorjai. 2003. Molecular packing of lysozyme, fibrinogen, and bovine serum albumin on hydrophilic and hydrophobic surfaces studied by infrared-visible sum frequency generation and fluorescence microscopy. J. Am. Chem. Soc. 125:3150-3158.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 3150-3158
    • Kim, J.1    Somorjai, G.A.2
  • 16
    • 33645420002 scopus 로고    scopus 로고
    • In situ adsorption studies of a 14-amino acid leucine-lysine peptide onto hydrophobic polystyrene and hydrophilic silica surfaces using quartz crystal microbalance, atomic force microscopy, and sum frequency generation vibrational spectroscopy
    • Mermut, O., D. C. Phillips, R. L. York, K. R. McCrea, R. S. Ward, and G. A. Somorjai. 2006. In situ adsorption studies of a 14-amino acid leucine-lysine peptide onto hydrophobic polystyrene and hydrophilic silica surfaces using quartz crystal microbalance, atomic force microscopy, and sum frequency generation vibrational spectroscopy. J. Am. Chem. Soc. 128:3598-3607.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 3598-3607
    • Mermut, O.1    Phillips, D.C.2    York, R.L.3    McCrea, K.R.4    Ward, R.S.5    Somorjai, G.A.6
  • 19
    • 0041520556 scopus 로고    scopus 로고
    • Detection of amide I signals of interfacial proteins in situ using SFG
    • Wang, J., M. A. Even, X. Chen, A. H. Schmaier, J. H. Waite, and Z. Chen. 2003. Detection of amide I signals of interfacial proteins in situ using SFG. J. Am. Chem. Soc. 125:9914-9915.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 9914-9915
    • Wang, J.1    Even, M.A.2    Chen, X.3    Schmaier, A.H.4    Waite, J.H.5    Chen, Z.6
  • 20
    • 0141843505 scopus 로고    scopus 로고
    • Using isotope-labeled proteins and sum frequency generation vibrational spectroscopy to study protein adsorption
    • Wang, J., M. L. Clarke, Y. B. Zhang, X. Chen, and Z. Chen. 2003. Using isotope-labeled proteins and sum frequency generation vibrational spectroscopy to study protein adsorption. Langmuir. 19:7862-7866.
    • (2003) Langmuir , vol.19 , pp. 7862-7866
    • Wang, J.1    Clarke, M.L.2    Zhang, Y.B.3    Chen, X.4    Chen, Z.5
  • 21
    • 0038460630 scopus 로고    scopus 로고
    • The effect of surface coverage on conformation changes of bovine serum albumin molecules at the air-solution interface detected by sum frequency generation vibrational spectroscopy
    • Wang, J., S. M. Buck, and Z. Chen. 2003. The effect of surface coverage on conformation changes of bovine serum albumin molecules at the air-solution interface detected by sum frequency generation vibrational spectroscopy. Analyst. 128:773-778.
    • (2003) Analyst , vol.128 , pp. 773-778
    • Wang, J.1    Buck, S.M.2    Chen, Z.3
  • 22
    • 17044433851 scopus 로고    scopus 로고
    • Detection of chiral sum frequency generation vibrational spectra of proteins and peptides at interfaces in situ
    • Wang, J., X. Chen, M. L. Clarke, and Z. Chen. 2005. Detection of chiral sum frequency generation vibrational spectra of proteins and peptides at interfaces in situ. Proc. Natl. Acad. Sci. USA. 102:4978-4983.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4978-4983
    • Wang, J.1    Chen, X.2    Clarke, M.L.3    Chen, Z.4
  • 23
    • 33645520999 scopus 로고    scopus 로고
    • Vibrational spectroscopic studies on fibrinogen adsorption at polystyrene/protein solution interfaces: Hydrophobic side chain and secondary structure changes
    • Wang, J., X. Chen, M. L. Clarke, and Z. Chen. 2006. Vibrational spectroscopic studies on fibrinogen adsorption at polystyrene/protein solution interfaces: hydrophobic side chain and secondary structure changes. J. Phys. Chem. B. 110:5017-5024.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 5017-5024
    • Wang, J.1    Chen, X.2    Clarke, M.L.3    Chen, Z.4
  • 24
    • 16244408339 scopus 로고    scopus 로고
    • Probing α-helical and β-sheet structures of peptides at solid/liquid interfaces with SFG
    • Chen, X., J. Wang, J. J. Sniadecki, M. A. Even, and Z. Chen. 2005. Probing α-helical and β-sheet structures of peptides at solid/liquid interfaces with SFG. Langmuir. 21:2662-2664.
    • (2005) Langmuir , vol.21 , pp. 2662-2664
    • Chen, X.1    Wang, J.2    Sniadecki, J.J.3    Even, M.A.4    Chen, Z.5
  • 25
    • 28944449298 scopus 로고    scopus 로고
    • Conformational changes of fibrinogen after adsorption
    • Clarke, M. L., J. Wang, and Z. Chen. 2005. Conformational changes of fibrinogen after adsorption. J. Phys. Chem. B. 109:22027-22035.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 22027-22035
    • Clarke, M.L.1    Wang, J.2    Chen, Z.3
  • 26
    • 33748940617 scopus 로고    scopus 로고
    • SFG studies on interactions between antimicrobial peptides and supported lipid bilayers
    • Chen, X., and Z. Chen. 2006. SFG studies on interactions between antimicrobial peptides and supported lipid bilayers. Biochim. Biophys. Acta. 1758:1257-1273.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1257-1273
    • Chen, X.1    Chen, Z.2
  • 27
    • 17444400457 scopus 로고    scopus 로고
    • Sum frequency generation vibrational spectroscopy studies on molecular conformation and orientation of biological molecules at interfaces
    • Chen, X., M. L. Clarke, J. Wang, and Z. Chen. 2005. Sum frequency generation vibrational spectroscopy studies on molecular conformation and orientation of biological molecules at interfaces. Int. J. Mod. Phys. B. 19:691-713.
    • (2005) Int. J. Mod. Phys. B , vol.19 , pp. 691-713
    • Chen, X.1    Clarke, M.L.2    Wang, J.3    Chen, Z.4
  • 28
    • 6744248168 scopus 로고
    • Surface-properties probed by 2nd-harmonic and sum-frequency generation
    • Shen, Y. R. 1989. Surface-properties probed by 2nd-harmonic and sum-frequency generation. Nature. 337:519-525.
    • (1989) Nature , vol.337 , pp. 519-525
    • Shen, Y.R.1
  • 29
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey, C. E. 1990. The actions of melittin on membranes. Biochim. Biophys. Acta. 1031:143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 30
    • 0027254408 scopus 로고
    • Possible mechanisms of action of cobra snake venom cardiotoxins and bee venom melittin
    • Fletcher, J. E., and M. S. Jiang. 1993. Possible mechanisms of action of cobra snake venom cardiotoxins and bee venom melittin. Toxicon. 31:669-695.
    • (1993) Toxicon , vol.31 , pp. 669-695
    • Fletcher, J.E.1    Jiang, M.S.2
  • 31
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. 1997. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:197-211.
    • (1997) J. Membr. Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 32
    • 0020479083 scopus 로고
    • The structure of melittin. I. Structure determination and partial refinement
    • Terwilliger, T. C., and D. Eisenberg. 1982. The structure of melittin. I. Structure determination and partial refinement. J. Biol. Chem. 257:6010-6015.
    • (1982) J. Biol. Chem , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 33
    • 0020479123 scopus 로고
    • The structure of melittin. II. interpretation of the structure
    • Terwilliger, T. C., and D. Eisenberg. 1982. The structure of melittin. II. interpretation of the structure. J. Biol. Chem. 257:6016-6022.
    • (1982) J. Biol. Chem , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 34
    • 16344384943 scopus 로고    scopus 로고
    • Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR
    • Toraya, S., K. Nishimura, and A. Naito. 2004. Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR. Biophys. J. 87:3323-3335.
    • (2004) Biophys. J , vol.87 , pp. 3323-3335
    • Toraya, S.1    Nishimura, K.2    Naito, A.3
  • 35
    • 0034763782 scopus 로고    scopus 로고
    • Solid-state NMR structure determination of melittin in a lipid environment
    • Lam, Y., S. R. Wassall, C. J. Morton, R. Smith, and F. Separovic. 2001. Solid-state NMR structure determination of melittin in a lipid environment. Biophys. J. 81:2752-2761.
    • (2001) Biophys. J , vol.81 , pp. 2752-2761
    • Lam, Y.1    Wassall, S.R.2    Morton, C.J.3    Smith, R.4    Separovic, F.5
  • 38
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L., T. A. Harroun, T. M. Weiss, L. Ding, and H. W. Huang. 2001. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81:1475-1485.
    • (2001) Biophys. J , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 39
    • 0346850624 scopus 로고    scopus 로고
    • Conformational analysis of melittin in solution phase: Vibrational circular dichroism study
    • Wang, F., and P. L. Polavarapu. 2003. Conformational analysis of melittin in solution phase: vibrational circular dichroism study. Biopolymers. 70:614-619.
    • (2003) Biopolymers , vol.70 , pp. 614-619
    • Wang, F.1    Polavarapu, P.L.2
  • 40
    • 7744240086 scopus 로고    scopus 로고
    • Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers
    • Constantinescu, I., and M. Lafleur. 2004. Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers. Biochim. Biophys. Acta. 1667:26-37.
    • (2004) Biochim. Biophys. Acta , vol.1667 , pp. 26-37
    • Constantinescu, I.1    Lafleur, M.2
  • 41
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • Frey, S., and L. K. Tamm. 1991. Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys. J. 60:922-930.
    • (1991) Biophys. J , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 42
    • 0037419793 scopus 로고    scopus 로고
    • Label-free chiral detection of melittin binding to a membrane
    • Kriech, M. A., and J. C. Conboy. 2003. Label-free chiral detection of melittin binding to a membrane. J. Am. Chem. Soc. 125:1148-1149.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1148-1149
    • Kriech, M.A.1    Conboy, J.C.2
  • 43
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. 2000. Action of antimicrobial peptides: two-state model. Biochemistry. 39:8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 44
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. 2002. Mode of action of membrane active antimicrobial peptides. Biopolymers. 66:236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 45
    • 3042620560 scopus 로고    scopus 로고
    • Structure and function of membrane-lytic peptides
    • Bechinger, B. 2004. Structure and function of membrane-lytic peptides. CRC Crit. Rev. Plant Sci. 23:271-292.
    • (2004) CRC Crit. Rev. Plant Sci , vol.23 , pp. 271-292
    • Bechinger, B.1
  • 46
    • 0034667493 scopus 로고    scopus 로고
    • Interaction of melittin with solid supported membranes
    • Steinem, C., H. Galla, and A. Janshoff. 2000. Interaction of melittin with solid supported membranes. Phys. Chem. Chem. Phys. 2:4580-4585.
    • (2000) Phys. Chem. Chem. Phys , vol.2 , pp. 4580-4585
    • Steinem, C.1    Galla, H.2    Janshoff, A.3
  • 47
    • 15244349709 scopus 로고    scopus 로고
    • Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores
    • Allende, D., S. A. Simon, and T. J. McIntosh. 2005. Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores. Biophys. J. 88:1828-1837.
    • (2005) Biophys. J , vol.88 , pp. 1828-1837
    • Allende, D.1    Simon, S.A.2    McIntosh, T.J.3
  • 48
    • 19644364144 scopus 로고    scopus 로고
    • Implementing the theory of sum frequency generation vibrational spectroscopy: A tutorial review
    • Lambert, A. G., P. B. Davies, and D. J. Neivandt. 2005. Implementing the theory of sum frequency generation vibrational spectroscopy: a tutorial review. Appl. Spectrosc. Rev. 40:103-145.
    • (2005) Appl. Spectrosc. Rev , vol.40 , pp. 103-145
    • Lambert, A.G.1    Davies, P.B.2    Neivandt, D.J.3
  • 49
    • 0035507359 scopus 로고    scopus 로고
    • Vibrational spectroscopy of interfaces by infrared-visible sum frequency generation
    • Buck, M., and M. Himmelhaus. 2001. Vibrational spectroscopy of interfaces by infrared-visible sum frequency generation. J. Vac. Sci. Technol. A. 19:2717-2736.
    • (2001) J. Vac. Sci. Technol. A , vol.19 , pp. 2717-2736
    • Buck, M.1    Himmelhaus, M.2
  • 50
    • 0036420639 scopus 로고    scopus 로고
    • Studies of polymer surfaces by sum frequency generation vibrational spectroscopy
    • Chen, Z., Y. R. Shen, and G. A. Somorjai. 2002. Studies of polymer surfaces by sum frequency generation vibrational spectroscopy. Annu. Rev. Phys. Chem. 53:437-465.
    • (2002) Annu. Rev. Phys. Chem , vol.53 , pp. 437-465
    • Chen, Z.1    Shen, Y.R.2    Somorjai, G.A.3
  • 52
    • 0001625429 scopus 로고    scopus 로고
    • Mapping molecular orientation and conformation at interfaces by surface nonlinear optics
    • Zhuang, X., P. B. Miranda, D. Kim, and Y. R. Shen. 1999. Mapping molecular orientation and conformation at interfaces by surface nonlinear optics. Phys. Rev. B. 59:12632-12640.
    • (1999) Phys. Rev. B , vol.59 , pp. 12632-12640
    • Zhuang, X.1    Miranda, P.B.2    Kim, D.3    Shen, Y.R.4
  • 53
    • 0035819187 scopus 로고    scopus 로고
    • Molecular chemical structure on poly(methyl methacrylate) (PMMA) surface studied by sum frequency generation (SFG) vibrational spectroscopy
    • Wang, J., C. Y. Chen, S. M. Buck, and Z. Chen. 2001. Molecular chemical structure on poly(methyl methacrylate) (PMMA) surface studied by sum frequency generation (SFG) vibrational spectroscopy. J. Phys. Chem. B. 105:12118-12125.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12118-12125
    • Wang, J.1    Chen, C.Y.2    Buck, S.M.3    Chen, Z.4
  • 54
    • 0037134882 scopus 로고    scopus 로고
    • Measuring polymer surface ordering differences in air and water by sum frequency generation vibrational spectroscopy
    • Wang, J., Z. Paszti, M. A. Even, and Z. Chen. 2002. Measuring polymer surface ordering differences in air and water by sum frequency generation vibrational spectroscopy. J. Am. Chem. Soc. 124:7016-7023.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 7016-7023
    • Wang, J.1    Paszti, Z.2    Even, M.A.3    Chen, Z.4
  • 55
    • 0000529857 scopus 로고
    • Formulas for the analysis of surface sum-frequency generation spectrum by CH stretching modes of methyl and methylene groups
    • Hirose, C., N. Akamatsu, and K. Domen. 1992. Formulas for the analysis of surface sum-frequency generation spectrum by CH stretching modes of methyl and methylene groups. J. Chem. Phys. 96:997-1004.
    • (1992) J. Chem. Phys , vol.96 , pp. 997-1004
    • Hirose, C.1    Akamatsu, N.2    Domen, K.3
  • 56
    • 1642327373 scopus 로고    scopus 로고
    • A unified treatment of selection rules and symmetry relations for sum-frequency and second harmonic spectroscopies
    • Moad, A. J., and G. J. Simpson. 2004. A unified treatment of selection rules and symmetry relations for sum-frequency and second harmonic spectroscopies. J. Phys. Chem. B. 108:3548-3562.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3548-3562
    • Moad, A.J.1    Simpson, G.J.2
  • 57
    • 0021947327 scopus 로고
    • Supported phospholipid-bilayers
    • Tamm, L. K., and H. M. Mcconnell. 1985. Supported phospholipid-bilayers. Biophys. J. 47:105-113.
    • (1985) Biophys. J , vol.47 , pp. 105-113
    • Tamm, L.K.1    Mcconnell, H.M.2
  • 59
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Muller, D. J., M. Amrein, and A. Engel. 1997. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119:172-188.
    • (1997) J. Struct. Biol , vol.119 , pp. 172-188
    • Muller, D.J.1    Amrein, M.2    Engel, A.3
  • 60
    • 0035856674 scopus 로고    scopus 로고
    • Investigations of water structure at the solid/liquid interface in the presence of supported lipid bilayers by vibrational sum frequency spectroscopy
    • Kim, J., G. Kim, and P. S. Cremer. 2001. Investigations of water structure at the solid/liquid interface in the presence of supported lipid bilayers by vibrational sum frequency spectroscopy. Langmuir. 17:7255-7260.
    • (2001) Langmuir , vol.17 , pp. 7255-7260
    • Kim, J.1    Kim, G.2    Cremer, P.S.3
  • 61
    • 27144478607 scopus 로고    scopus 로고
    • Electrostatically driven spatial patterns in lipid membrane composition
    • 1-048101/4
    • Parthasarathy, R., P. A. Cripe, and J. T. Groves. 2005. Electrostatically driven spatial patterns in lipid membrane composition. Phys. Rev. Lett. 95:048101/1-048101/4.
    • (2005) Phys. Rev. Lett , vol.95 , pp. 048101
    • Parthasarathy, R.1    Cripe, P.A.2    Groves, J.T.3
  • 63
    • 0032558153 scopus 로고    scopus 로고
    • Phosphatidylcholine monolayer structure at a liquid-liquid interface
    • Walker, R. A., J. A. Gruetzmacher, and G. L. Richmond. 1998. Phosphatidylcholine monolayer structure at a liquid-liquid interface. J. Am. Chem. Soc. 120:6991-7003.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 6991-7003
    • Walker, R.A.1    Gruetzmacher, J.A.2    Richmond, G.L.3
  • 64
    • 0028178521 scopus 로고
    • Pore-forming peptides induce rapid phospholipid flip-flop in membranes
    • Fattal, E., S. Nir, R. A. Parente, and F. C. Szoka. 1994. Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry. 33:6721-6731.
    • (1994) Biochemistry , vol.33 , pp. 6721-6731
    • Fattal, E.1    Nir, S.2    Parente, R.A.3    Szoka, F.C.4
  • 65
    • 0038192455 scopus 로고    scopus 로고
    • The antibiotic activity of cationic linear amphipathic peptides: Lessons from the action of leucine/lysine copolymers on bacteria of the class mollicutes
    • Beven, L., S. Castano, J. Dufourcq, A. Wieslander, and H. Wroblewski. 2003. The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class mollicutes. Eur. J. Biochem. 270:2207-2217.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2207-2217
    • Beven, L.1    Castano, S.2    Dufourcq, J.3    Wieslander, A.4    Wroblewski, H.5
  • 66
    • 0346729747 scopus 로고    scopus 로고
    • Comparative activities of cecropin A, melittin, and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of acinetobacter baumannii
    • Giacometti, A., O. Cirioni, W. Kamysz, G. D'Amato, C. Silvestri, M. S. Del Prete, J. Lukasiak, and G. Scalise. 2003. Comparative activities of cecropin A, melittin, and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of acinetobacter baumannii. Peptides. 24:1315-1318.
    • (2003) Peptides , vol.24 , pp. 1315-1318
    • Giacometti, A.1    Cirioni, O.2    Kamysz, W.3    D'Amato, G.4    Silvestri, C.5    Del Prete, M.S.6    Lukasiak, J.7    Scalise, G.8
  • 67
    • 0022829127 scopus 로고
    • The action of various venoms on Escherichia coli
    • Stocker, J. F., and J. R. Traynor. 1986. The action of various venoms on Escherichia coli. J. Appl. Bacteriol. 61:383-388.
    • (1986) J. Appl. Bacteriol , vol.61 , pp. 383-388
    • Stocker, J.F.1    Traynor, J.R.2
  • 68
    • 0942287125 scopus 로고    scopus 로고
    • Demonstrating the feasibility of monitoring the molecular-level structures of moving polymer/silane interfaces during silane diffusion using SFG
    • Chen, C. Y., J. Wang, C. L. Loch, D. Ahn, and Z. Chen. 2004. Demonstrating the feasibility of monitoring the molecular-level structures of moving polymer/silane interfaces during silane diffusion using SFG. J. Am. Chem. Soc. 126:1174-1179.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 1174-1179
    • Chen, C.Y.1    Wang, J.2    Loch, C.L.3    Ahn, D.4    Chen, Z.5
  • 70
    • 33846818748 scopus 로고    scopus 로고
    • Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies
    • Chen, X., J. Wang, A. P. Boughton, C. B. Kristalyn, and Z. Chen. 2007. Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies. J. Am. Chem. Soc. 129:1420-1427.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 1420-1427
    • Chen, X.1    Wang, J.2    Boughton, A.P.3    Kristalyn, C.B.4    Chen, Z.5
  • 71
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • Hristova, K., C. E. Dempsey, and S. H. White. 2001. Structure, location, and lipid perturbations of melittin at the membrane interface. Biophys. J. 80:801-811.
    • (2001) Biophys. J , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 72
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R. E., and S. H. White. 1989. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry. 28:3421-3437.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 73
    • 0033066284 scopus 로고    scopus 로고
    • Interactions of a-helices with lipid bilayers: A review of simulation studies
    • Biggin, P. C., and M. S. P. Sansom. 1999. Interactions of a-helices with lipid bilayers: a review of simulation studies. Biophys. Chem. 76:161-183.
    • (1999) Biophys. Chem , vol.76 , pp. 161-183
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 74
    • 0041765833 scopus 로고    scopus 로고
    • Mechanisms of membrane deformation
    • Farsad, K., and P. De Camilli. 2003. Mechanisms of membrane deformation. Curr. Opin. Cell Biol. 15:372-381.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 372-381
    • Farsad, K.1    De Camilli, P.2
  • 75
    • 2042418996 scopus 로고    scopus 로고
    • The mechanisms of lipid-protein rearrangements during viral infection
    • Chizmadzhev, Y. A. 2004. The mechanisms of lipid-protein rearrangements during viral infection. Bioelectrochemistry. 63:129-136.
    • (2004) Bioelectrochemistry , vol.63 , pp. 129-136
    • Chizmadzhev, Y.A.1
  • 76
    • 11144340301 scopus 로고    scopus 로고
    • Class I and class II viral fusion protein structures reveal similar principles in membrane fusion
    • Schibli, D. J., and W. Weissenhorn. 2004. Class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol. Membr. Biol. 21:361-371.
    • (2004) Mol. Membr. Biol , vol.21 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 77
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., T. Lang, and T. C. Sudhof. 2003. Membrane fusion. Cell. 112:519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 78
    • 0032855980 scopus 로고    scopus 로고
    • Controlling cytoskeleton structure by phosphoinositide-protein interactions: Phosphoinositide binding protein domains and effects of lipid packing
    • Janmey, P. A., W. Xian, and L. A. Flanagan. 1999. Controlling cytoskeleton structure by phosphoinositide-protein interactions: phosphoinositide binding protein domains and effects of lipid packing. Chem. Phys. Lipids. 101:93-107.
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 93-107
    • Janmey, P.A.1    Xian, W.2    Flanagan, L.A.3
  • 79
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • Tanaka, M., and E. Sackmann. 2005. Polymer-supported membranes as models of the cell surface. Nature. 437:656-663.
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2


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