메뉴 건너뛰기




Volumn 1768, Issue 2, 2007, Pages 236-245

Defect formation of lytic peptides in lipid membranes and their influence on the thermodynamic properties of the pore environment

Author keywords

Alamethicin; Atomic force microscopy; Differential scanning calorimetry; Lipid membranes; Melittin; Peptide pores

Indexed keywords

1,2 DILAUROYLGLYCERO 3 PHOSPHOCHOLINE; 1,2 DIPALMITOYLGLYCERO 3 PHOSPHATIDYLCHOLINE; ALAMETHICIN; MELITTIN; PHOSPHOLIPID DERIVATIVE; PHOSPHORYLCHOLINE; UNCLASSIFIED DRUG;

EID: 33846406880     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.10.007     Document Type: Article
Times cited : (26)

References (50)
  • 1
    • 0024555637 scopus 로고
    • Structure and supramolecular architecture of membrane channel-forming peptides
    • Spach G., Duclohier H., Molle G., and Valleton J.M. Structure and supramolecular architecture of membrane channel-forming peptides. Biochimie 71 1 (1989) 11-21
    • (1989) Biochimie , vol.71 , Issue.1 , pp. 11-21
    • Spach, G.1    Duclohier, H.2    Molle, G.3    Valleton, J.M.4
  • 2
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by k-helical antimicrobial and cell non-selective membrane lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by k-helical antimicrobial and cell non-selective membrane lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 4
    • 0028226051 scopus 로고
    • Alamethicin: a peptide model for voltage gating and protein-membrane interactions
    • Cafiso D.S. Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 141-165
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 5
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey C.E. The actions of melittin on membranes. Biochim. Biophys. Acta 1031 2 (1990) 143-161
    • (1990) Biochim. Biophys. Acta , vol.1031 , Issue.2 , pp. 143-161
    • Dempsey, C.E.1
  • 6
    • 0020360086 scopus 로고
    • A voltage gated ion channel inferred from the crystal structure of alamethicin at 1.5 å resolution
    • Fox R.O., and Richards F.M. A voltage gated ion channel inferred from the crystal structure of alamethicin at 1.5 å resolution. Nature 300 (1982) 325-330
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox, R.O.1    Richards, F.M.2
  • 8
    • 0020079526 scopus 로고
    • The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities
    • Terwilliger T., Weissman L., and Eisenberg D. The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities. Biophys. J. 37 1 (1982) 353-361
    • (1982) Biophys. J. , vol.37 , Issue.1 , pp. 353-361
    • Terwilliger, T.1    Weissman, L.2    Eisenberg, D.3
  • 9
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He K., Ludtke S., Heller W., and Huang H. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71 5 (1996) 2669-2679
    • (1996) Biophys. J. , vol.71 , Issue.5 , pp. 2669-2679
    • He, K.1    Ludtke, S.2    Heller, W.3    Huang, H.4
  • 10
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: structure of alamethicin pores
    • He K., Ludtke S., Worcester D., and Huang H. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70 6 (1996) 2659-2666
    • (1996) Biophys. J. , vol.70 , Issue.6 , pp. 2659-2666
    • He, K.1    Ludtke, S.2    Worcester, D.3    Huang, H.4
  • 11
    • 0034753275 scopus 로고    scopus 로고
    • Insertion and pore formation driven by adsorption of proteins onto lipid bilayer membrane-water interfaces
    • Zuckermann M.J., and Heimburg T. Insertion and pore formation driven by adsorption of proteins onto lipid bilayer membrane-water interfaces. Biophys. J. 81 5 (2001) 2458-2472
    • (2001) Biophys. J. , vol.81 , Issue.5 , pp. 2458-2472
    • Zuckermann, M.J.1    Heimburg, T.2
  • 12
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin
    • Chen F.-Y., Lee M.-T., and Huang H.W. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82 2 (2002) 908-914
    • (2002) Biophys. J. , vol.82 , Issue.2 , pp. 908-914
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 14
    • 0026673421 scopus 로고
    • Prolines are not essential residues in the "barrel-stave" model for ion channels induced by alamethicin analogues
    • Duclohier H., Molle G., Dugast J., and Spach G. Prolines are not essential residues in the "barrel-stave" model for ion channels induced by alamethicin analogues. Biophys. J. 63 3 (1992) 868-873
    • (1992) Biophys. J. , vol.63 , Issue.3 , pp. 868-873
    • Duclohier, H.1    Molle, G.2    Dugast, J.3    Spach, G.4
  • 15
    • 0028010959 scopus 로고
    • The barrel-stave model as applied to alamethicin and its analogs reevaluated
    • Laver D. The barrel-stave model as applied to alamethicin and its analogs reevaluated. Biophys. J. 66 2 Pt. 1 (1994) 355-359
    • (1994) Biophys. J. , vol.66 , Issue.2 PART 1 , pp. 355-359
    • Laver, D.1
  • 16
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile
    • Cantor R. Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile. Biophys. J. 82 5 (2002) 2520-2525
    • (2002) Biophys. J. , vol.82 , Issue.5 , pp. 2520-2525
    • Cantor, R.1
  • 17
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • Duclohier H., and Wróblewski H. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184 1 (2001) 1-12
    • (2001) J. Membr. Biol. , vol.184 , Issue.1 , pp. 1-12
    • Duclohier, H.1    Wróblewski, H.2
  • 18
    • 0015760624 scopus 로고
    • The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes
    • Eisenberg M., Hal J., and Mead C. The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes. J. Membr. Biol. 14 1 (1973) 143-176
    • (1973) J. Membr. Biol. , vol.14 , Issue.1 , pp. 143-176
    • Eisenberg, M.1    Hal, J.2    Mead, C.3
  • 19
    • 0019323459 scopus 로고
    • The lowest conductance state of the alamethicin pore
    • Hanke W., and Boheim G. The lowest conductance state of the alamethicin pore. Biochim. Biophys. Acta 596 3 (1980) 456-462
    • (1980) Biochim. Biophys. Acta , vol.596 , Issue.3 , pp. 456-462
    • Hanke, W.1    Boheim, G.2
  • 20
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • Keller S.L., Bezrukov S.M., Gruner S.M., Tate M.W., Vodyanoy I., and Parsegian V.A. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys. J. 65 (1993) 23-27
    • (1993) Biophys. J. , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 21
    • 0025897469 scopus 로고
    • "Reversed" alamethicin conductance in lipid bilayers
    • Taylor R., and de Levie R. "Reversed" alamethicin conductance in lipid bilayers. Biophys. J. 59 4 (1991) 873-879
    • (1991) Biophys. J. , vol.59 , Issue.4 , pp. 873-879
    • Taylor, R.1    de Levie, R.2
  • 22
    • 0035306147 scopus 로고    scopus 로고
    • Histogram method to obtain heat capacities in lipid monolayers, curved bilayers, and membranes containing peptides
    • Ivanova V.P., and Heimburg T. Histogram method to obtain heat capacities in lipid monolayers, curved bilayers, and membranes containing peptides. Phys. Rev., E 63 (2001) 1914-1925
    • (2001) Phys. Rev., E , vol.63 , pp. 1914-1925
    • Ivanova, V.P.1    Heimburg, T.2
  • 23
    • 0037379826 scopus 로고    scopus 로고
    • Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A
    • Ivanova V.P., Makarov I.M., Schäffer T.E., and Heimburg T. Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A. Biophys. J. 84 (2003) 2427-2439
    • (2003) Biophys. J. , vol.84 , pp. 2427-2439
    • Ivanova, V.P.1    Makarov, I.M.2    Schäffer, T.E.3    Heimburg, T.4
  • 24
    • 26044439375 scopus 로고    scopus 로고
    • Phase behavior and nanoscale structure of phospholipid membranes incorporated with acylated C14-peptides
    • Pedersen T.B., Kaasgaard T., Jensen M., Frokjaer S., Mouritsen O.G., and Jørgensen K. Phase behavior and nanoscale structure of phospholipid membranes incorporated with acylated C14-peptides. Biophys. J. 89 4 (2005) 2494-2503
    • (2005) Biophys. J. , vol.89 , Issue.4 , pp. 2494-2503
    • Pedersen, T.B.1    Kaasgaard, T.2    Jensen, M.3    Frokjaer, S.4    Mouritsen, O.G.5    Jørgensen, K.6
  • 25
    • 0030071247 scopus 로고    scopus 로고
    • A Monte Carlo simulation study of protein-induced heat capacity changes
    • Heimburg T., and Biltonen R.L. A Monte Carlo simulation study of protein-induced heat capacity changes. Biophys. J. 70 (1996) 84-96
    • (1996) Biophys. J. , vol.70 , pp. 84-96
    • Heimburg, T.1    Biltonen, R.L.2
  • 26
    • 0028950310 scopus 로고
    • Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers
    • Zhang Y.P., Lewis R.N., Hodges R.S., and McElhaney R.N. Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers. Biochemistry 34 7 (1995) 2362-2371
    • (1995) Biochemistry , vol.34 , Issue.7 , pp. 2362-2371
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 28
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function-the hydrophobic matching hypothesis revisited
    • Jensen M.Ø., and Mouritsen O.G. Lipids do influence protein function-the hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta 1666 (2004) 205-226
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.Ø.1    Mouritsen, O.G.2
  • 30
    • 12844255666 scopus 로고    scopus 로고
    • Scanning force microscopy of artificial membranes
    • Janshoff A., and Steinem C. Scanning force microscopy of artificial membranes. ChemBioChem 2 11 (2001) 798-808
    • (2001) ChemBioChem , vol.2 , Issue.11 , pp. 798-808
    • Janshoff, A.1    Steinem, C.2
  • 31
    • 33645287528 scopus 로고    scopus 로고
    • The atomic force microscope as a tool for studying phase separation in lipid membranes
    • Connell S.D., and Smith D.A. The atomic force microscope as a tool for studying phase separation in lipid membranes. Mol. Membr. Biol. 23 1 (2006) 17-28
    • (2006) Mol. Membr. Biol. , vol.23 , Issue.1 , pp. 17-28
    • Connell, S.D.1    Smith, D.A.2
  • 32
    • 33645028968 scopus 로고    scopus 로고
    • Striated domains: self-organizing ordered assemblies of transmembrane alpha-helical peptides and lipids in bilayers
    • (doi.org/10.1515/BC.2006.031)
    • de Kruijff B., Killian J.A., Ganchev D.N., Rinia H.A., and Sparr E. Striated domains: self-organizing ordered assemblies of transmembrane alpha-helical peptides and lipids in bilayers. Biol. Chem. 387 3 (2006) 235-241. http://dx.doi.org/10.1515/BC.2006.031 (doi.org/10.1515/BC.2006.031)
    • (2006) Biol. Chem. , vol.387 , Issue.3 , pp. 235-241
    • de Kruijff, B.1    Killian, J.A.2    Ganchev, D.N.3    Rinia, H.A.4    Sparr, E.5
  • 34
    • 0037379711 scopus 로고    scopus 로고
    • Nanoscopic lipid domain dynamics revealed by atomic force microscopy
    • Tokumasu F., Jin A.J., Feigenson G.W., and Dvorak J.A. Nanoscopic lipid domain dynamics revealed by atomic force microscopy. Biophys. J. 84 (2003) 2609-2618
    • (2003) Biophys. J. , vol.84 , pp. 2609-2618
    • Tokumasu, F.1    Jin, A.J.2    Feigenson, G.W.3    Dvorak, J.A.4
  • 35
    • 0036840109 scopus 로고    scopus 로고
    • Ripples and the formation of anisotropic lipid domains: imaging two-component supported double bilayers by atomic force microscopy
    • Leidy C., Kaasgaard T., Crowe J.H., Mouritsen O.G., and Jørgensen K. Ripples and the formation of anisotropic lipid domains: imaging two-component supported double bilayers by atomic force microscopy. Biophys. J. 83 (2002) 2625-2633
    • (2002) Biophys. J. , vol.83 , pp. 2625-2633
    • Leidy, C.1    Kaasgaard, T.2    Crowe, J.H.3    Mouritsen, O.G.4    Jørgensen, K.5
  • 36
    • 0035979795 scopus 로고    scopus 로고
    • Imaging domains in model membranes with atomic force microscopy
    • Rinia H.A., and de Kruiji B. Imaging domains in model membranes with atomic force microscopy. FEBS Lett. 504 (2001) 194-199
    • (2001) FEBS Lett. , vol.504 , pp. 194-199
    • Rinia, H.A.1    de Kruiji, B.2
  • 37
    • 0037636128 scopus 로고    scopus 로고
    • Temperature-controlled structure and kinetics of ripple phases in one- and two-component supported lipid bilayers
    • Kaasgaard T., Leidy C., Crowe H., Mouritsen O.G., and Jørgensen K. Temperature-controlled structure and kinetics of ripple phases in one- and two-component supported lipid bilayers. Biophys. J. 85 1 (2003) 350-360
    • (2003) Biophys. J. , vol.85 , Issue.1 , pp. 350-360
    • Kaasgaard, T.1    Leidy, C.2    Crowe, H.3    Mouritsen, O.G.4    Jørgensen, K.5
  • 38
    • 0030012156 scopus 로고    scopus 로고
    • Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers
    • Mou J., Czajkowsky D., and Shao Z. Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers. Biochemistry 35 10 (1996) 3222-3226
    • (1996) Biochemistry , vol.35 , Issue.10 , pp. 3222-3226
    • Mou, J.1    Czajkowsky, D.2    Shao, Z.3
  • 42
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao Z., and Yang J. Progress in high resolution atomic force microscopy in biology. Q. Rev. Biophys. 28 2 (1995) 195-251
    • (1995) Q. Rev. Biophys. , vol.28 , Issue.2 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 43
    • 0000914318 scopus 로고
    • Theory of the main lipid bilayer phase transition
    • Nagle J.F. Theory of the main lipid bilayer phase transition. Annu. Rev. Phys. Chem. 31 (1980) 157-195
    • (1980) Annu. Rev. Phys. Chem. , vol.31 , pp. 157-195
    • Nagle, J.F.1
  • 44
    • 33846422974 scopus 로고    scopus 로고
    • L. Makowski, J. Li, Topics in Molecular and structural Biology: Biomembrane Structure and Function., Weinheim, 1984, Ch. X-ray diffraction and electron microscope studies of the molecular structure of biological membranes., pp. 43-166.
  • 45
    • 0021947327 scopus 로고
    • Supported phospholipid bilayers
    • Tamm L.K., and McConnell H.M. Supported phospholipid bilayers. Biophys. J. 47 1 (1985) 105-113
    • (1985) Biophys. J. , vol.47 , Issue.1 , pp. 105-113
    • Tamm, L.K.1    McConnell, H.M.2
  • 46
    • 0028354421 scopus 로고
    • Tris(hydroxymethyl)aminomethane (C4H11NO3) induced a ripple phase in supported unilamellar phospholipid bilayers
    • Mou J., Yang J., and Shao Z. Tris(hydroxymethyl)aminomethane (C4H11NO3) induced a ripple phase in supported unilamellar phospholipid bilayers. Biochemistry 33 15 (1994) 4439-4443
    • (1994) Biochemistry , vol.33 , Issue.15 , pp. 4439-4443
    • Mou, J.1    Yang, J.2    Shao, Z.3
  • 47
    • 0032449839 scopus 로고    scopus 로고
    • Mechanical aspects of membrane thermodynamics. Estimation of the mechanical properties of lipid membranes close to the chain melting transition from calorimetry
    • Heimburg T. Mechanical aspects of membrane thermodynamics. Estimation of the mechanical properties of lipid membranes close to the chain melting transition from calorimetry. Biochim. Biophys. Acta 1415 (1998) 147-162
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 147-162
    • Heimburg, T.1
  • 48
    • 3042772810 scopus 로고    scopus 로고
    • Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering
    • Spaar A., Münster C., and Salditt T. Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering. Biophys. J. 87 (2004) 396-407
    • (2004) Biophys. J. , vol.87 , pp. 396-407
    • Spaar, A.1    Münster, C.2    Salditt, T.3
  • 49
    • 0033428891 scopus 로고    scopus 로고
    • Network formation of lipid membranes: triggering structural transitions by chain melting
    • Schneider M.F., Marsh D., Jahn W., Kloesgen B., and Heimburg T. Network formation of lipid membranes: triggering structural transitions by chain melting. Proc. Natl. Acad. Sci. U. S. A. 96 25 (1999) 14312-14317
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.25 , pp. 14312-14317
    • Schneider, M.F.1    Marsh, D.2    Jahn, W.3    Kloesgen, B.4    Heimburg, T.5
  • 50
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang L., Harroun T.A., Weiss T.M., Ding L., and Huang H.W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81 3 (2001) 1475-1485
    • (2001) Biophys. J. , vol.81 , Issue.3 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.