메뉴 건너뛰기




Volumn 1778, Issue 10, 2008, Pages 2325-2333

Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases

Author keywords

Differential scanning calorimetry; Lipid peptide interaction; Membrane electrostatics; Phase transition; Pore formation; X ray diffraction

Indexed keywords

GLYCYLLEUCINE; GRAMICIDIN S; LIPID; MELITTIN; PALMITOYLOLEOYL PHOSPHATIDYLETHANOLAMINE; PEPTIDYL GLYCYLLEUCINE CARBOXYAMIDE; PHOSPHATIDYLETHANOLAMINE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; PROTEGRIN 1; UNCLASSIFIED DRUG;

EID: 52049111366     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.05.014     Document Type: Article
Times cited : (45)

References (74)
  • 1
    • 47049098589 scopus 로고    scopus 로고
    • Liposome-based biomembrane mimetic systems: implications for lipid-peptide interactions
    • Leitmannova-Liu A. (Ed), Elsevier, Amsterdam
    • Lohner K., Sevcsik E., and Pabst G. Liposome-based biomembrane mimetic systems: implications for lipid-peptide interactions. In: Leitmannova-Liu A. (Ed). Advances in Planar Lipid Bilayers and Liposomes Vol. 6 (2008), Elsevier, Amsterdam 103-137
    • (2008) Advances in Planar Lipid Bilayers and Liposomes , vol.6 , pp. 103-137
    • Lohner, K.1    Sevcsik, E.2    Pabst, G.3
  • 2
    • 34948829603 scopus 로고    scopus 로고
    • How lipids influence the mode of action of membrane-active peptides
    • Sevcsik E., Pabst G., Jilek A., and Lohner K. How lipids influence the mode of action of membrane-active peptides. Biochim.Biophys.Acta 1768 (2007) 2568-2595
    • (2007) Biochim.Biophys.Acta , vol.1768 , pp. 2568-2595
    • Sevcsik, E.1    Pabst, G.2    Jilek, A.3    Lohner, K.4
  • 3
    • 45849085763 scopus 로고    scopus 로고
    • Interaction of LL-37 with model membrane systems of different complexity-influence of the lipid matrix
    • Sevcsik E., Pabst G., Richter W., Danner S., Amenitsch H., and Lohner K. Interaction of LL-37 with model membrane systems of different complexity-influence of the lipid matrix. Biophys.J. 94 (2008) 4688-4699
    • (2008) Biophys.J. , vol.94 , pp. 4688-4699
    • Sevcsik, E.1    Pabst, G.2    Richter, W.3    Danner, S.4    Amenitsch, H.5    Lohner, K.6
  • 4
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and transition of melittin
    • Matsuzaki K., Yoneyama S., and Miyajima K. Pore formation and transition of melittin. Biophys.J. 73 (1997) 831-838
    • (1997) Biophys.J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 6
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: the origin of cooperativity
    • Huang H.W. Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim.Biophys.Acta 1758 (2006) 1292-1302
    • (2006) Biochim.Biophys.Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 7
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-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
  • 8
    • 16844362681 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics
    • Lohner K., and Blondelle S.E. Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics. Comb.Chem.High Throughput.Screen. 8 (2005) 241-256
    • (2005) Comb.Chem.High Throughput.Screen. , vol.8 , pp. 241-256
    • Lohner, K.1    Blondelle, S.E.2
  • 9
    • 0030048521 scopus 로고    scopus 로고
    • Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures
    • Keller S.L., Gruner S.M., and Gawrisch K. Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures. Biochim.Biophys.Acta 1278 (1996) 241-246
    • (1996) Biochim.Biophys.Acta , vol.1278 , pp. 241-246
    • Keller, S.L.1    Gruner, S.M.2    Gawrisch, K.3
  • 10
    • 0030853508 scopus 로고    scopus 로고
    • Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity
    • Prenner E.J., Lewis R.N., Neuman K.C., Gruner S.M., Kondejewski L.H., Hodges R.S., and McElhaney R.N. Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity. Biochemistry 36 (1997) 7906-7916
    • (1997) Biochemistry , vol.36 , pp. 7906-7916
    • Prenner, E.J.1    Lewis, R.N.2    Neuman, K.C.3    Gruner, S.M.4    Kondejewski, L.H.5    Hodges, R.S.6    McElhaney, R.N.7
  • 11
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner E.J., Lewis R.N., and McElhaney R.N. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim.Biophys.Acta 1462 (1999) 201-221
    • (1999) Biochim.Biophys.Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.2    McElhaney, R.N.3
  • 12
    • 0032929807 scopus 로고    scopus 로고
    • Nisin promotes the formation of non-lamellar inverted phases in unsaturated phosphatidylethanolamines
    • El Jastimi R., and Lafleur M. Nisin promotes the formation of non-lamellar inverted phases in unsaturated phosphatidylethanolamines. Biochim.Biophys Acta 1418 (1999) 97-105
    • (1999) Biochim.Biophys Acta , vol.1418 , pp. 97-105
    • El Jastimi, R.1    Lafleur, M.2
  • 13
    • 0034214104 scopus 로고    scopus 로고
    • Interaction of the peptide antibiotic alamethicin with bilayer-and non-bilayer-forming lipids: influence of increasing alamethicin concentration on the lipids supramolecular structures
    • Angelova A., Ionov R., Koch M.H., and Rapp G. Interaction of the peptide antibiotic alamethicin with bilayer-and non-bilayer-forming lipids: influence of increasing alamethicin concentration on the lipids supramolecular structures. Arch.Biochem.Biophys. 378 (2000) 93-106
    • (2000) Arch.Biochem.Biophys. , vol.378 , pp. 93-106
    • Angelova, A.1    Ionov, R.2    Koch, M.H.3    Rapp, G.4
  • 14
    • 0034730576 scopus 로고    scopus 로고
    • X-ray studies on the interaction of the antimicrobial peptide gramicidin S with microbial lipid extracts: evidence for cubic phase formation
    • Staudegger E., Prenner E.J., Kriechbaum M., Degovics G., Lewis R.N., McElhaney R.N., and Lohner K. X-ray studies on the interaction of the antimicrobial peptide gramicidin S with microbial lipid extracts: evidence for cubic phase formation. Biochim.Biophys.Acta 1468 (2000) 213-230
    • (2000) Biochim.Biophys.Acta , vol.1468 , pp. 213-230
    • Staudegger, E.1    Prenner, E.J.2    Kriechbaum, M.3    Degovics, G.4    Lewis, R.N.5    McElhaney, R.N.6    Lohner, K.7
  • 15
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock K.J., Lee D.K., and Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys.J. 84 (2003) 3052-3060
    • (2003) Biophys.J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 16
    • 0041821476 scopus 로고    scopus 로고
    • The effects of gramicidin on the structure of phospholipid assemblies
    • Szule J.A., and Rand R.P. The effects of gramicidin on the structure of phospholipid assemblies. Biophys.J. 85 (2003) 1702-1712
    • (2003) Biophys.J. , vol.85 , pp. 1702-1712
    • Szule, J.A.1    Rand, R.P.2
  • 18
    • 40849102416 scopus 로고    scopus 로고
    • Membrane curvature stress and antibacterial activity of lactoferricin derivatives
    • Zweytick D., Tumer S., Blondelle S.E., and Lohner K. Membrane curvature stress and antibacterial activity of lactoferricin derivatives. Biochem.Biophys.Res.Commun. 369 (2008) 395-400
    • (2008) Biochem.Biophys.Res.Commun. , vol.369 , pp. 395-400
    • Zweytick, D.1    Tumer, S.2    Blondelle, S.E.3    Lohner, K.4
  • 19
    • 77957054958 scopus 로고
    • Polymorphism of lipid water systems
    • Lipowsky R., and Sackmann E. (Eds), North-Holland, Amsterdam
    • Seddon J.M., and Templer R.H. Polymorphism of lipid water systems. In: Lipowsky R., and Sackmann E. (Eds). Structure and Dynamics of Membranes (1995), North-Holland, Amsterdam 97-160
    • (1995) Structure and Dynamics of Membranes , pp. 97-160
    • Seddon, J.M.1    Templer, R.H.2
  • 20
    • 0004485421 scopus 로고    scopus 로고
    • Liposome phase systems as membrane activity sensors for peptides
    • Katsaras J., and Gutberlet T. (Eds), Springer, Berlin
    • Laggner P., and Lohner K. Liposome phase systems as membrane activity sensors for peptides. In: Katsaras J., and Gutberlet T. (Eds). Lipid bilayers. Structure and Interactions (2000), Springer, Berlin 233-264
    • (2000) Lipid bilayers. Structure and Interactions , pp. 233-264
    • Laggner, P.1    Lohner, K.2
  • 21
    • 0002336563 scopus 로고    scopus 로고
    • The role of membrane lipid composition in cell targeting of antimicrobial peptides
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, Norfolk, UK
    • Lohner K. The role of membrane lipid composition in cell targeting of antimicrobial peptides. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, Norfolk, UK 149-165
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 149-165
    • Lohner, K.1
  • 22
    • 0038298731 scopus 로고    scopus 로고
    • Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution X-ray diffraction
    • Rappolt M., Hickel A., Bringezu F., and Lohner K. Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution X-ray diffraction. Biophys.J. 84 (2003) 3111-3122
    • (2003) Biophys.J. , vol.84 , pp. 3111-3122
    • Rappolt, M.1    Hickel, A.2    Bringezu, F.3    Lohner, K.4
  • 23
    • 0025311581 scopus 로고
    • Lamellar/inverted cubic (L alpha/QII) phase transition in N-methylated dioleoylphosphatidylethanolamine
    • Siegel D.P., and Banschbach J.L. Lamellar/inverted cubic (L alpha/QII) phase transition in N-methylated dioleoylphosphatidylethanolamine. Biochemistry 29 (1990) 5975-5981
    • (1990) Biochemistry , vol.29 , pp. 5975-5981
    • Siegel, D.P.1    Banschbach, J.L.2
  • 24
    • 3042776328 scopus 로고    scopus 로고
    • The Gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior
    • Siegel D.P., and Kozlov M.M. The Gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior. Biophys.J. 87 (2004) 366-374
    • (2004) Biophys.J. , vol.87 , pp. 366-374
    • Siegel, D.P.1    Kozlov, M.M.2
  • 25
    • 33745686034 scopus 로고    scopus 로고
    • Determining the ratio of the Gaussian curvature and bending elastic moduli of phospholipids from Q(II) phase unit cell dimensions
    • Siegel D.P. Determining the ratio of the Gaussian curvature and bending elastic moduli of phospholipids from Q(II) phase unit cell dimensions. Biophys.J. 91 (2006) 608-618
    • (2006) Biophys.J. , vol.91 , pp. 608-618
    • Siegel, D.P.1
  • 26
    • 0031848842 scopus 로고    scopus 로고
    • Accelerated formation of cubic phases in phosphatidylethanolamine dispersions
    • Tenchov B., Koynova R., and Rapp G. Accelerated formation of cubic phases in phosphatidylethanolamine dispersions. Biophys.J. 75 (1998) 853-866
    • (1998) Biophys.J. , vol.75 , pp. 853-866
    • Tenchov, B.1    Koynova, R.2    Rapp, G.3
  • 27
    • 0024278433 scopus 로고
    • Observation of inverted cubic phase in hydrated dioleoylphosphatidylethanolamine membranes
    • Shyamsunder E., Gruner S.M., Tate M.W., Turner D.C., So P.T., and Tilcock C.P. Observation of inverted cubic phase in hydrated dioleoylphosphatidylethanolamine membranes. Biochemistry 27 (1988) 2332-2336
    • (1988) Biochemistry , vol.27 , pp. 2332-2336
    • Shyamsunder, E.1    Gruner, S.M.2    Tate, M.W.3    Turner, D.C.4    So, P.T.5    Tilcock, C.P.6
  • 28
    • 0028532391 scopus 로고    scopus 로고
    • On the existence of bicontinuous cubic phases in dioleoylphosphatidylethanolamine
    • Erbes J., Czeslik C., Hahn W., Winter R., Rappolt M., and Rapp G. On the existence of bicontinuous cubic phases in dioleoylphosphatidylethanolamine. Ber.Bunsenges.Phys.Chem. 98 (2006) 1287-1293
    • (2006) Ber.Bunsenges.Phys.Chem. , vol.98 , pp. 1287-1293
    • Erbes, J.1    Czeslik, C.2    Hahn, W.3    Winter, R.4    Rappolt, M.5    Rapp, G.6
  • 29
    • 0036224803 scopus 로고    scopus 로고
    • Determination of L(alpha)-H(II) phase transition temperature for 1,2-dioleoyl-sn-glycero-3-phosphatidylethanolamine
    • Toombes G.E., Finnefrock A.C., Tate M.W., and Gruner S.M. Determination of L(alpha)-H(II) phase transition temperature for 1,2-dioleoyl-sn-glycero-3-phosphatidylethanolamine. Biophys.J. 82 (2002) 2504-2510
    • (2002) Biophys.J. , vol.82 , pp. 2504-2510
    • Toombes, G.E.1    Finnefrock, A.C.2    Tate, M.W.3    Gruner, S.M.4
  • 30
    • 0028044781 scopus 로고
    • Phases and phase transitions of the hydrated phosphatidylethanolamines
    • Koynova R., and Caffrey M. Phases and phase transitions of the hydrated phosphatidylethanolamines. Chem.Phys.Lipids 69 (1994) 1-34
    • (1994) Chem.Phys.Lipids , vol.69 , pp. 1-34
    • Koynova, R.1    Caffrey, M.2
  • 31
    • 0242301629 scopus 로고    scopus 로고
    • The kinetics of non-lamellar phase formation in DOPE-Me: relevance to biomembrane fusion
    • Cherezov V., Siegel D.P., Shaw W., Burgess S.W., and Caffrey M. The kinetics of non-lamellar phase formation in DOPE-Me: relevance to biomembrane fusion. J.Membr.Biol. 195 (2003) 165-182
    • (2003) J.Membr.Biol. , vol.195 , pp. 165-182
    • Cherezov, V.1    Siegel, D.P.2    Shaw, W.3    Burgess, S.W.4    Caffrey, M.5
  • 32
    • 0037136054 scopus 로고    scopus 로고
    • Cubic phase is induced by cholesterol in the dispersion of 1-palmitoyl-2-oleoyl-phosphatidylethanolamine
    • Wang X., and Quinn P.J. Cubic phase is induced by cholesterol in the dispersion of 1-palmitoyl-2-oleoyl-phosphatidylethanolamine. Biochim.Biophys.Acta 1564 (2002) 66-72
    • (2002) Biochim.Biophys.Acta , vol.1564 , pp. 66-72
    • Wang, X.1    Quinn, P.J.2
  • 33
    • 0034730436 scopus 로고    scopus 로고
    • Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms
    • Siegel D.P., and Epand R.M. Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms. Biochim.Biophys.Acta 1468 (2000) 87-98
    • (2000) Biochim.Biophys.Acta , vol.1468 , pp. 87-98
    • Siegel, D.P.1    Epand, R.M.2
  • 34
    • 33646143773 scopus 로고    scopus 로고
    • Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion
    • Siegel D.P., Cherezov V., Greathouse D.V., Koeppe R.E., Killian J.A., and Caffrey M. Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion. Biophys.J. 90 (2006) 200-211
    • (2006) Biophys.J. , vol.90 , pp. 200-211
    • Siegel, D.P.1    Cherezov, V.2    Greathouse, D.V.3    Koeppe, R.E.4    Killian, J.A.5    Caffrey, M.6
  • 35
    • 0028122480 scopus 로고
    • Bending, hydration and interstitial energies quantitatively account for the hexagonal-lamellar-hexagonal reentrant phase transition in dioleoylphosphatidylethanolamine
    • Kozlov M.M., Leikin S., and Rand R.P. Bending, hydration and interstitial energies quantitatively account for the hexagonal-lamellar-hexagonal reentrant phase transition in dioleoylphosphatidylethanolamine. Biophys.J. 67 (1994) 1603-1611
    • (1994) Biophys.J. , vol.67 , pp. 1603-1611
    • Kozlov, M.M.1    Leikin, S.2    Rand, R.P.3
  • 36
    • 43849106474 scopus 로고    scopus 로고
    • Influence of the lamellar phase unbinding energy on the relative stability of lamellar and inverted cubic phases
    • Siegel D.P., and Tenchov B.G. Influence of the lamellar phase unbinding energy on the relative stability of lamellar and inverted cubic phases. Biophys.J. 94 (2008) 3987-3995
    • (2008) Biophys.J. , vol.94 , pp. 3987-3995
    • Siegel, D.P.1    Tenchov, B.G.2
  • 37
    • 0021099105 scopus 로고
    • Cooperative effects in the interaction between melittin and phosphatidylcholine model membranes. Studies by temperature scanning densitometry
    • Posch M., Rakusch U., Mollay C., and Laggner P. Cooperative effects in the interaction between melittin and phosphatidylcholine model membranes. Studies by temperature scanning densitometry. J.Biol.Chem. 258 (1983) 1761-1766
    • (1983) J.Biol.Chem. , vol.258 , pp. 1761-1766
    • Posch, M.1    Rakusch, U.2    Mollay, C.3    Laggner, P.4
  • 38
    • 0024278460 scopus 로고
    • Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines
    • Batenburg A.M., van Esch J.H., and de Kruijff B. Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines. Biochemistry 27 (1988) 2324-2331
    • (1988) Biochemistry , vol.27 , pp. 2324-2331
    • Batenburg, A.M.1    van Esch, J.H.2    de Kruijff, B.3
  • 39
    • 0026242310 scopus 로고
    • Small-angle X-ray diffraction studies on the effects of melittin on lipid bilayer assemblies
    • Colotto A., Lohner K., and Laggner P. Small-angle X-ray diffraction studies on the effects of melittin on lipid bilayer assemblies. Journal of Applied Crystallography 24 (1991) 847-851
    • (1991) Journal of Applied Crystallography , vol.24 , pp. 847-851
    • Colotto, A.1    Lohner, K.2    Laggner, P.3
  • 40
    • 0027139908 scopus 로고
    • Ultrasonic study of melittin effects on phospholipid model membranes
    • Colotto A., Kharakoz D.P., Lohner K., and Laggner P. Ultrasonic study of melittin effects on phospholipid model membranes. Biophys.J. 65 (1993) 2360-2367
    • (1993) Biophys.J. , vol.65 , pp. 2360-2367
    • Colotto, A.1    Kharakoz, D.P.2    Lohner, K.3    Laggner, P.4
  • 41
    • 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 (2001) 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
  • 42
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • Hristova K., Dempsey C.E., and White S.H. Structure, location, and lipid perturbations of melittin at the membrane interface. Biophys.J. 80 (2001) 801-811
    • (2001) Biophys.J. , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 43
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • Fahrner R.L., Dieckmann T., Harwig S.S., Lehrer R.I., Eisenberg D., and Feigon J. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem.Biol. 3 (1996) 543-550
    • (1996) Chem.Biol. , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 45
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: magainin and protegrin
    • Yang L., Weiss T.M., Lehrer R.I., and Huang H.W. Crystallization of antimicrobial pores in membranes: magainin and protegrin. Biophys.J. 79 (2000) 2002-2009
    • (2000) Biophys.J. , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 46
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin
    • Yamaguchi S., Hong T., Waring A., Lehrer R.I., and Hong M. Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin. Biochemistry 41 (2002) 9852-9862
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 48
    • 7244257317 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1
    • Mani R., Buffy J.J., Waring A.J., Lehrer R.I., and Hong M. Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1. Biochemistry 43 (2004) 13839-13848
    • (2004) Biochemistry , vol.43 , pp. 13839-13848
    • Mani, R.1    Buffy, J.J.2    Waring, A.J.3    Lehrer, R.I.4    Hong, M.5
  • 49
    • 0030863833 scopus 로고    scopus 로고
    • Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids
    • Latal A., Degovics G., Epand R.F., Epand R.M., and Lohner K. Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids. Eur.J.Biochem. 248 (1997) 938-946
    • (1997) Eur.J.Biochem. , vol.248 , pp. 938-946
    • Latal, A.1    Degovics, G.2    Epand, R.F.3    Epand, R.M.4    Lohner, K.5
  • 50
    • 0031903306 scopus 로고    scopus 로고
    • Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
    • Bechinger B., Zasloff M., and Opella S.J. Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy. Biophys.J. 74 (1998) 981-987
    • (1998) Biophys.J. , vol.74 , pp. 981-987
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 51
    • 33646135796 scopus 로고    scopus 로고
    • Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR
    • Strandberg E., Wadhwani P., Tremouilhac P., Durr U.H., and Ulrich A.S. Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR. Biophys.J. 90 (2006) 1676-1686
    • (2006) Biophys.J. , vol.90 , pp. 1676-1686
    • Strandberg, E.1    Wadhwani, P.2    Tremouilhac, P.3    Durr, U.H.4    Ulrich, A.S.5
  • 52
    • 0035208239 scopus 로고    scopus 로고
    • Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state F-19-NMR
    • Salgado J., Grage S.L., Kondejewski L.H., Hodges R.S., McElhaney R.N., and Ulrich A.S. Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state F-19-NMR. J.Biomol.NMR 21 (2001) 191-208
    • (2001) J.Biomol.NMR , vol.21 , pp. 191-208
    • Salgado, J.1    Grage, S.L.2    Kondejewski, L.H.3    Hodges, R.S.4    McElhaney, R.N.5    Ulrich, A.S.6
  • 53
    • 52049119949 scopus 로고    scopus 로고
    • Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes: concentration-dependent re-alignment and self-assembly as a b-barrel
    • Peters T. (Ed), Springer
    • Afonin S., Dürr U.H.N., Wadhwani P., Salgado J.B., and Ulrich A.S. Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes: concentration-dependent re-alignment and self-assembly as a b-barrel. In: Peters T. (Ed). Bioactive Conformation II (2008), Springer
    • (2008) Bioactive Conformation II
    • Afonin, S.1    Dürr, U.H.N.2    Wadhwani, P.3    Salgado, J.B.4    Ulrich, A.S.5
  • 54
    • 0025880878 scopus 로고
    • The study of lipid-protein interactions: effect of melittin on phase transition of phosphatidylethanolamine and sensitivity of phospholipases to phase state
    • Nishiya T., and Chou H.L. The study of lipid-protein interactions: effect of melittin on phase transition of phosphatidylethanolamine and sensitivity of phospholipases to phase state. J.Biochem.(Tokyo) 110 (1991) 732-736
    • (1991) J.Biochem.(Tokyo) , vol.110 , pp. 732-736
    • Nishiya, T.1    Chou, H.L.2
  • 55
    • 0034257990 scopus 로고    scopus 로고
    • Structural information from multilamellar liposomes at full hydration: full q-range fitting with high quality X-ray data
    • Pabst G., Rappolt M., Amenitsch H., and Laggner P. Structural information from multilamellar liposomes at full hydration: full q-range fitting with high quality X-ray data. Phys.Rev.E 62 (2000) 4000-4009
    • (2000) Phys.Rev.E , vol.62 , pp. 4000-4009
    • Pabst, G.1    Rappolt, M.2    Amenitsch, H.3    Laggner, P.4
  • 57
    • 34247562641 scopus 로고    scopus 로고
    • Global properties of biomimetic membranes: perspectives on molecular features
    • Pabst G. Global properties of biomimetic membranes: perspectives on molecular features. Biophys.Rev.and Letters 1 (2006) 57-84
    • (2006) Biophys.Rev.and Letters , vol.1 , pp. 57-84
    • Pabst, G.1
  • 59
    • 0032222334 scopus 로고    scopus 로고
    • High-throughput asymmetric double-crystal monochromator of the SAXS beamline at ELETTRA
    • Bernstorff S., Amenitsch H., and Laggner P. High-throughput asymmetric double-crystal monochromator of the SAXS beamline at ELETTRA. J.Synchrotron Rad. 5 (1998) 1215-1221
    • (1998) J.Synchrotron Rad. , vol.5 , pp. 1215-1221
    • Bernstorff, S.1    Amenitsch, H.2    Laggner, P.3
  • 60
    • 0032119425 scopus 로고    scopus 로고
    • A beginners' guide to gas-filled proportional detectors with delay line readout
    • Petrascu A.M., Koch M.H.J., and Gabriel A. A beginners' guide to gas-filled proportional detectors with delay line readout. J.Macromol.Sci.B 37 (1998) 463-483
    • (1998) J.Macromol.Sci.B , vol.37 , pp. 463-483
    • Petrascu, A.M.1    Koch, M.H.J.2    Gabriel, A.3
  • 61
    • 45049083404 scopus 로고    scopus 로고
    • The biologically relevant lipid mesophases as "seen" by X-rays
    • Leitmannova-Liu A. (Ed), Elsevier, Amsterdam
    • Rappolt M. The biologically relevant lipid mesophases as "seen" by X-rays. In: Leitmannova-Liu A. (Ed). Advances in Planar Lipid Bilayers and Liposomes Vol. 5 (2006), Elsevier, Amsterdam 253-283
    • (2006) Advances in Planar Lipid Bilayers and Liposomes , vol.5 , pp. 253-283
    • Rappolt, M.1
  • 62
    • 36248957675 scopus 로고    scopus 로고
    • Entropy-driven softening of fluid lipid bilayers by alamethicin
    • Pabst G., Danner S., Podgornik R., and Katsaras J. Entropy-driven softening of fluid lipid bilayers by alamethicin. Langmuir 23 (2007) 11705-11711
    • (2007) Langmuir , vol.23 , pp. 11705-11711
    • Pabst, G.1    Danner, S.2    Podgornik, R.3    Katsaras, J.4
  • 63
    • 84938081949 scopus 로고
    • Steric interaction of fluid membranes in multilayer systems
    • Helfrich W. Steric interaction of fluid membranes in multilayer systems. Z. Naturforsch. 33a (1978) 305-315
    • (1978) Z. Naturforsch. , vol.33 a , pp. 305-315
    • Helfrich, W.1
  • 64
    • 40149107726 scopus 로고    scopus 로고
    • A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A
    • Gregory S.M., Cavenaugh A., Journigan V., Pokorny A., and Almeida P.F. A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A. Biophys.J. 94 (2008) 1667-1680
    • (2008) Biophys.J. , vol.94 , pp. 1667-1680
    • Gregory, S.M.1    Cavenaugh, A.2    Journigan, V.3    Pokorny, A.4    Almeida, P.F.5
  • 65
    • 0032926928 scopus 로고    scopus 로고
    • The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion
    • Siegel D.P. The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion. Biophys.J. 76 (1999) 291-313
    • (1999) Biophys.J. , vol.76 , pp. 291-313
    • Siegel, D.P.1
  • 66
    • 0026731832 scopus 로고
    • Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
    • Jackson M., Mantsch H.H., and Spencer J.H. Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy. Biochemistry 31 (1992) 7289-7293
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Mantsch, H.H.2    Spencer, J.H.3
  • 67
    • 0025061113 scopus 로고
    • Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes
    • Beschiaschvili G., and Seelig J. Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes. Biochemistry 29 (1990) 52-58
    • (1990) Biochemistry , vol.29 , pp. 52-58
    • Beschiaschvili, G.1    Seelig, J.2
  • 68
    • 0034681140 scopus 로고    scopus 로고
    • Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects
    • Wieprecht T., Apostolov O., Beyermann M., and Seelig J. Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects. Biochemistry 39 (2000) 442-452
    • (2000) Biochemistry , vol.39 , pp. 442-452
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 71
    • 36949003906 scopus 로고    scopus 로고
    • Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence
    • Zhu W.L., Nan Y.H., Hahm K.S., and Shin S.Y. Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence. J.Biochem.Mol.Biol. 40 (2 0 07) 1090-1094
    • J.Biochem.Mol.Biol. , vol.40 , pp. 1090-1094
    • Zhu, W.L.1    Nan, Y.H.2    Hahm, K.S.3    Shin, S.Y.4
  • 72
    • 0024286949 scopus 로고
    • Antimicrobial properties of peptides from Xenopus granular gland secretions
    • Soravia E., Martini G., and Zasloff M. Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228 (1988) 337-340
    • (1988) FEBS Lett. , vol.228 , pp. 337-340
    • Soravia, E.1    Martini, G.2    Zasloff, M.3
  • 74
    • 0034424412 scopus 로고    scopus 로고
    • Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa
    • Zhang L., Dhillon P., Yan H., Farmer S., and Hancock R.E. Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa. Antimicrob.Agents Chemother. 44 (2000) 3317-3321
    • (2000) Antimicrob.Agents Chemother. , vol.44 , pp. 3317-3321
    • Zhang, L.1    Dhillon, P.2    Yan, H.3    Farmer, S.4    Hancock, R.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.