메뉴 건너뛰기




Volumn 14, Issue 4, 2008, Pages 407-415

Interaction of peptides with biomembranes assessed by potential-sensitive fluorescent probes

Author keywords

Bioactive peptides; Biomembranes; Dipole potential; Fluorescent probes; Surface potential; Transmembrane potential

Indexed keywords

4 [2 [6 (DIOCTYLAMINO) 2 NAPHTHALENYL]ETHENYL] 1 (3 SULFOPROPYL)PYRIDINIUM; BACITRACIN; FLUORESCENT DYE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; PEPTIDE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PROTEIN P25; UNCLASSIFIED DRUG;

EID: 42149117742     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1005     Document Type: Review
Times cited : (27)

References (57)
  • 2
    • 24644453083 scopus 로고    scopus 로고
    • Transfer of lipophilic drugs between liposomal membranes and biological interfaces: Consequences for drug delivery
    • Fahr A, van Hoogevest P, May S, Bergstrand N, Leigh MLS. 'Transfer of lipophilic drugs between liposomal membranes and biological interfaces: consequences for drug delivery. Eur. J. Pharm. Sci. 2005; 26: 251-265.
    • (2005) Eur. J. Pharm. Sci , vol.26 , pp. 251-265
    • Fahr, A.1    van Hoogevest, P.2    May, S.3    Bergstrand, N.4    Leigh, M.L.S.5
  • 3
    • 30044436650 scopus 로고    scopus 로고
    • Lipid membrane-induced optimization for ligand-receptor docking: Recent tools and insights for the "membrane catalysis" model
    • Castanho MA, Fernandes MX. Lipid membrane-induced optimization for ligand-receptor docking: recent tools and insights for the "membrane catalysis" model. Eur. Biophys. J. 2006: 35: 92-103.
    • (2006) Eur. Biophys. J , vol.35 , pp. 92-103
    • Castanho, M.A.1    Fernandes, M.X.2
  • 4
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • Killian JA, Nyholm, TK. Peptides in lipid bilayers: the power of simple models. Curr. Opin. Struct. Biol. 2006; 16: 473-479.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.2
  • 5
    • 0038392423 scopus 로고    scopus 로고
    • Quantifying molecular partition into model systems of biomembranes: An emphasis on optical spectroscopic methods
    • Santos NC, Prieto M, Castanho MA. Quantifying molecular partition into model systems of biomembranes: an emphasis on optical spectroscopic methods. Biochim. Biophys. Acta 2003; 1612: 123-135.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 123-135
    • Santos, N.C.1    Prieto, M.2    Castanho, M.A.3
  • 6
    • 0024553457 scopus 로고
    • The electrostatic properties of membranes
    • McLaughlin S. The electrostatic properties of membranes. Annu. Rev. Biophys. Biophys. Chem. 1989; 18: 113-136.
    • (1989) Annu. Rev. Biophys. Biophys. Chem , vol.18 , pp. 113-136
    • McLaughlin, S.1
  • 7
    • 0032821480 scopus 로고    scopus 로고
    • The electrostatics of lipid surfaces
    • Langner M, Kubica K. The electrostatics of lipid surfaces. Chem. Phys. Lipids 1999; 101: 3-35.
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 3-35
    • Langner, M.1    Kubica, K.2
  • 8
    • 0025052304 scopus 로고
    • Membrane electrostatics
    • Cevc G. Membrane electrostatics. Biochim. Biophys. Acta 1990; 1031: 311-382.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 311-382
    • Cevc, G.1
  • 9
    • 0029283976 scopus 로고
    • The use of fluorescein phosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions
    • Wall J, Golding CA, Van Veen M, O'Shea P. The use of fluorescein phosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions. Mol. Membr. Biol. 1995; 12: 183-192.
    • (1995) Mol. Membr. Biol , vol.12 , pp. 183-192
    • Wall, J.1    Golding, C.A.2    Van Veen, M.3    O'Shea, P.4
  • 10
    • 0021771793 scopus 로고
    • The use of fluorescein-dipalmitoylphosphatidylethanolamine for measuring pH-changes in the internal compartment of phospholipid vesicles
    • Thelen M, Petrone G, O'Shea PS, Azzi A. The use of fluorescein-dipalmitoylphosphatidylethanolamine for measuring pH-changes in the internal compartment of phospholipid vesicles. Biochim. Biophys. Acta 1984; 766: 161-168.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 161-168
    • Thelen, M.1    Petrone, G.2    O'Shea, P.S.3    Azzi, A.4
  • 11
    • 0023839487 scopus 로고
    • Use of a fluorescein derivative of phosphatidylethanolamine as a pH probe at water/lipid interfaces
    • Soucaille P, Prats M, Tocanne JF, Teissie J. Use of a fluorescein derivative of phosphatidylethanolamine as a pH probe at water/lipid interfaces. Biochim. Biophys. Acta 1988: 939: 289-294.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 289-294
    • Soucaille, P.1    Prats, M.2    Tocanne, J.F.3    Teissie, J.4
  • 12
    • 27644468368 scopus 로고    scopus 로고
    • 1-ATPase using N-(fluorescein-5-thiocarbamoyl)-1,2-dihexadecanoyl- sn-glycero-3-phosphoethano lamine, triethylammonium salt
    • 1-ATPase using N-(fluorescein-5-thiocarbamoyl)-1,2-dihexadecanoyl- sn-glycero-3-phosphoethano lamine, triethylammonium salt. Anal. Biochem. 2005; 344: 102-107.
    • (2005) Anal. Biochem , vol.344 , pp. 102-107
    • Yuanbo, C.1    Fan, Z.2    Jiachang, Y.3
  • 13
    • 0021918058 scopus 로고    scopus 로고
    • ThelenM, O'Shea PS, Petrone G, Azzi A. Proton translocation by a native and subunit III-depleted cytochrome c oxidase reconstituted into phospholipid vesicles. Use of fluorescein-phosphatidylethanolamine as an intravesicular pH indicator. J. Biol. Chem. 1985; 260: 3626-3631.
    • ThelenM, O'Shea PS, Petrone G, Azzi A. Proton translocation by a native and subunit III-depleted cytochrome c oxidase reconstituted into phospholipid vesicles. Use of fluorescein-phosphatidylethanolamine as an intravesicular pH indicator. J. Biol. Chem. 1985; 260: 3626-3631.
  • 14
    • 0142154784 scopus 로고    scopus 로고
    • Intermolecular interactions with/within cell membranes and the trinity of membrane potentials: Kinetics and imaging
    • O'Shea P. Intermolecular interactions with/within cell membranes and the trinity of membrane potentials: kinetics and imaging. Biochem. Soc. Trans. 2003: 31: 990-996.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 990-996
    • O'Shea, P.1
  • 15
    • 0029134105 scopus 로고
    • Interactions of macromolecules with the mammalian cell surface
    • Wall J, Ayoub F, O'Shea P. Interactions of macromolecules with the mammalian cell surface. J. Cell Sci. 1995; 108: 2673-2682.
    • (1995) J. Cell Sci , vol.108 , pp. 2673-2682
    • Wall, J.1    Ayoub, F.2    O'Shea, P.3
  • 16
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 1997; 156: 197-211.
    • (1997) J. Membr. Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 17
    • 0028838445 scopus 로고
    • Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase, subunit IV: A 2D 1H-NMR study
    • Chupin V, Leenhouts JM, de Kroon AI, de Kruijff B. Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase, subunit IV: a 2D 1H-NMR study. FEBS Lett. 1995; 373: 239-244.
    • (1995) FEBS Lett , vol.373 , pp. 239-244
    • Chupin, V.1    Leenhouts, J.M.2    de Kroon, A.I.3    de Kruijff, B.4
  • 18
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki K, Yoneyama S, Miyajima K. Pore formation and translocation of melittin. Biophys. J. 1997: 73: 831-838.
    • (1997) Biophys. J , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 19
    • 0029764221 scopus 로고    scopus 로고
    • Time resolution of binding and membrane insertion of a mitochondrial signal peptide: Correlation with structural changes and evidence for cooperativity
    • Golding C, Senior S, Wilson MT, O'Shea P. Time resolution of binding and membrane insertion of a mitochondrial signal peptide: correlation with structural changes and evidence for cooperativity. Biochemistry 1996; 35: 10931-10937.
    • (1996) Biochemistry , vol.35 , pp. 10931-10937
    • Golding, C.1    Senior, S.2    Wilson, M.T.3    O'Shea, P.4
  • 20
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS. HIV entry and its inhibition. Cell 1998; 93: 681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 21
    • 0035862949 scopus 로고    scopus 로고
    • The fusion domain of HIV gp41 interacts specifically with heparan sulfate on the T-lymphocyte cell surface
    • Cladera J, Martin I, O'Shea P. The fusion domain of HIV gp41 interacts specifically with heparan sulfate on the T-lymphocyte cell surface. EMBO J. 2001; 20: 19-26.
    • (2001) EMBO J , vol.20 , pp. 19-26
    • Cladera, J.1    Martin, I.2    O'Shea, P.3
  • 22
    • 1942517459 scopus 로고    scopus 로고
    • 171bronectin interactions with osteoblasts: Identification of a non-integrin-mediated binding mechanism using a real-time fluorescence binding assay
    • Sim B, Cladera J, O'Shea P. 171bronectin interactions with osteoblasts: identification of a non-integrin-mediated binding mechanism using a real-time fluorescence binding assay. J. Biomed. Mater. Res. A 2004; 68: 352-359.
    • (2004) J. Biomed. Mater. Res. A , vol.68 , pp. 352-359
    • Sim, B.1    Cladera, J.2    O'Shea, P.3
  • 23
    • 0141884337 scopus 로고    scopus 로고
    • Electrostatic sensor for identifying interactions between peptides and bacterial membranes
    • Fitchen N, O'Shea P, Williams P, Hardie KR. Electrostatic sensor for identifying interactions between peptides and bacterial membranes. Mol. Immunol. 2003; 40: 407-411.
    • (2003) Mol. Immunol , vol.40 , pp. 407-411
    • Fitchen, N.1    O'Shea, P.2    Williams, P.3    Hardie, K.R.4
  • 24
    • 0026635481 scopus 로고
    • Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces
    • Gawrisch K, Ruston D, Zimmerberg J, Parsegian VA, Rand RP, Fuller N. Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces. Biophys. J. 1992; 61: 1213-1223.
    • (1992) Biophys. J , vol.61 , pp. 1213-1223
    • Gawrisch, K.1    Ruston, D.2    Zimmerberg, J.3    Parsegian, V.A.4    Rand, R.P.5    Fuller, N.6
  • 25
    • 0026699999 scopus 로고
    • Molecular origin of the internal dipole potential in lipid bilayers: Calculation of the electrostatic potential
    • Zheng C, Vanderkooi G. Molecular origin of the internal dipole potential in lipid bilayers: calculation of the electrostatic potential. Biophys. J. 1992; 63: 935-941.
    • (1992) Biophys. J , vol.63 , pp. 935-941
    • Zheng, C.1    Vanderkooi, G.2
  • 26
    • 0034746677 scopus 로고    scopus 로고
    • The dipole potential of phospholipid membranes and methods for its detection
    • Clarke P.J. The dipole potential of phospholipid membranes and methods for its detection. Adv. Colloid Interface Sci. 2001; 89-90: 263-281.
    • (2001) Adv. Colloid Interface Sci , vol.89-90 , pp. 263-281
    • Clarke, P.J.1
  • 27
    • 0028284842 scopus 로고
    • Dual-wavelength ratiometric fluorescence measurement of the membrane dipole potential
    • Gross E, Bedlack RS, Loew LM. Dual-wavelength ratiometric fluorescence measurement of the membrane dipole potential. Biophys. J. 1994; 67: 208-216.
    • (1994) Biophys. J , vol.67 , pp. 208-216
    • Gross, E.1    Bedlack, R.S.2    Loew, L.M.3
  • 28
    • 0343731639 scopus 로고
    • Kinetics of the solubilization of styryl dye aggregates by lipid vesicles
    • Zouni A, Clarke RJ, Holzwarth JF. Kinetics of the solubilization of styryl dye aggregates by lipid vesicles. J. Phys. Chem. 1994: 98: 1732-1738.
    • (1994) J. Phys. Chem , vol.98 , pp. 1732-1738
    • Zouni, A.1    Clarke, R.J.2    Holzwarth, J.F.3
  • 29
    • 0022341014 scopus 로고
    • Spectra, membrane binding, and potentiometric responses of new charge shift probes
    • Fluhler E, Burnham VG, Loew LM. Spectra, membrane binding, and potentiometric responses of new charge shift probes. Biochemistry 1985; 24: 5749-5755.
    • (1985) Biochemistry , vol.24 , pp. 5749-5755
    • Fluhler, E.1    Burnham, V.G.2    Loew, L.M.3
  • 30
    • 0018186382 scopus 로고
    • Charge shift optical probes of membrane potential. theory
    • Loew LM, Bonneville GW, Surow J. Charge shift optical probes of membrane potential. theory. Biochemistry 1978; 17: 4065-4071.
    • (1978) Biochemistry , vol.17 , pp. 4065-4071
    • Loew, L.M.1    Bonneville, G.W.2    Surow, J.3
  • 31
    • 0030624708 scopus 로고    scopus 로고
    • Stark spectroscopy: Applications in chemistry, biology, and materials science
    • Bublitz GU, Boxer SG. Stark spectroscopy: applications in chemistry, biology, and materials science. Annu. Rev. Phys. Chem. 1997; 48: 213-242.
    • (1997) Annu. Rev. Phys. Chem , vol.48 , pp. 213-242
    • Bublitz, G.U.1    Boxer, S.G.2
  • 32
    • 0021895138 scopus 로고
    • A new generation of Ca2+ indicators with greatly improved fluorescence properties
    • Grynkiewicz G, Poenie M, Tsien RY. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 1985; 260: 3440-3450.
    • (1985) J. Biol. Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 33
    • 33845428514 scopus 로고    scopus 로고
    • Comparison of excitation and emission ratiometric fluorescence methods for quantifying the membrane dipole potential
    • Vitha MF, Clarke RJ. Comparison of excitation and emission ratiometric fluorescence methods for quantifying the membrane dipole potential. Biochim. Biophys. Acta 2007; 1768: 107-114.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 107-114
    • Vitha, M.F.1    Clarke, R.J.2
  • 34
    • 0031012421 scopus 로고    scopus 로고
    • Optical detection of membrane dipole potential: Avoidance of fluidity and dye-induced effects
    • Clarke RJ, Kane DJ. Optical detection of membrane dipole potential: avoidance of fluidity and dye-induced effects. Biochim. Biophys. Acta 1997; 1323: 223-239.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 223-239
    • Clarke, R.J.1    Kane, D.J.2
  • 35
    • 0030757379 scopus 로고    scopus 로고
    • Effect of lipid structure on the dipole potential of phosphatidylcholine bilayers
    • Clarke RJ. Effect of lipid structure on the dipole potential of phosphatidylcholine bilayers. Biochim. Biophys. Acta 1997; 1327: 269-278.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 269-278
    • Clarke, R.J.1
  • 36
    • 0031958516 scopus 로고    scopus 로고
    • Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide
    • Cladera J, O'Shea P. Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide. Biophys. J. 1998; 74: 2434-2442.
    • (1998) Biophys. J , vol.74 , pp. 2434-2442
    • Cladera, J.1    O'Shea, P.2
  • 37
    • 0027177939 scopus 로고
    • Internal electrostatic potentials in bilayers: Measuring and controlling dipole potentials in lipid vesicles
    • Franklin JC, Cafiso DS. Internal electrostatic potentials in bilayers: measuring and controlling dipole potentials in lipid vesicles. Biophys. J. 1993; 65: 289-299.
    • (1993) Biophys. J , vol.65 , pp. 289-299
    • Franklin, J.C.1    Cafiso, D.S.2
  • 38
    • 0033569892 scopus 로고    scopus 로고
    • Characterization of the sequence of interactions of the fusion domain of the simian immunodeficiency virus with membranes. Role of the membrane dipole potential
    • Cladera J, Martin I, Ruysschaert JM, O'Shea P. Characterization of the sequence of interactions of the fusion domain of the simian immunodeficiency virus with membranes. Role of the membrane dipole potential. J. Biol. Chem. 1999; 274: 29951-29959.
    • (1999) J. Biol. Chem , vol.274 , pp. 29951-29959
    • Cladera, J.1    Martin, I.2    Ruysschaert, J.M.3    O'Shea, P.4
  • 39
    • 33845929560 scopus 로고    scopus 로고
    • Effect of cholesterol on the interaction of the HIV GP41 fusion peptide with model membranes. Importance of the membrane dipole potential
    • Buzon V, Cladera J. Effect of cholesterol on the interaction of the HIV GP41 fusion peptide with model membranes. Importance of the membrane dipole potential. Biochemistry 2006; 45: 15768-15775.
    • (2006) Biochemistry , vol.45 , pp. 15768-15775
    • Buzon, V.1    Cladera, J.2
  • 41
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia RC, Tian H, Jensen FC. Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc. Natl. Acad. Sci. U.S.A. 1993; 90: 5181-5185.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 42
    • 0035914384 scopus 로고    scopus 로고
    • Effects of the membrane dipole potential on the interaction of saquinavir with phospholipid membranes and plasma membrane receptors of Caco-2 cells
    • Asawakarn T, Cladera J, O'Shea P. Effects of the membrane dipole potential on the interaction of saquinavir with phospholipid membranes and plasma membrane receptors of Caco-2 cells. J. Biol. Chem. 2001; 276: 38457-38463.
    • (2001) J. Biol. Chem , vol.276 , pp. 38457-38463
    • Asawakarn, T.1    Cladera, J.2    O'Shea, P.3
  • 43
    • 32344446760 scopus 로고    scopus 로고
    • Role of Caco-2 cell monolayers in prediction of intestinal drug absorption
    • Shah P, Jogani V, Bagchi T, Misra A. Role of Caco-2 cell monolayers in prediction of intestinal drug absorption. Biotechnol. Prog. 2006; 22: 186-198.
    • (2006) Biotechnol. Prog , vol.22 , pp. 186-198
    • Shah, P.1    Jogani, V.2    Bagchi, T.3    Misra, A.4
  • 45
    • 0037408151 scopus 로고    scopus 로고
    • Influence of molecular dipoles on human skin permeability: Use of 6-ketocholestanol to enhance the transdermal delivery of bacitracin
    • Cladera J, O'Shea P, Hadgraft J, Valenta C. Influence of molecular dipoles on human skin permeability: Use of 6-ketocholestanol to enhance the transdermal delivery of bacitracin. J. Pharm. Sci. 2003; 92: 1018-1027.
    • (2003) J. Pharm. Sci , vol.92 , pp. 1018-1027
    • Cladera, J.1    O'Shea, P.2    Hadgraft, J.3    Valenta, C.4
  • 46
    • 0141817700 scopus 로고    scopus 로고
    • Ultrasensitive two-color fluorescence probes for dipole potential in phospholipid membranes
    • Klymchenko AS, Duportail G, Mely Y, Demchenko AP. Ultrasensitive two-color fluorescence probes for dipole potential in phospholipid membranes. Proc. Natl. Acad. Sci. U.S.A. 2003; 100: 11219-11224.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 11219-11224
    • Klymchenko, A.S.1    Duportail, G.2    Mely, Y.3    Demchenko, A.P.4
  • 48
    • 33750504883 scopus 로고    scopus 로고
    • Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration
    • Deshayes S, Plenat T, Charnet P, Divita G, Molle G, Heitz F. Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration. Biochim. Biophys. Acta 2006; 1758: 1846-1851.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1846-1851
    • Deshayes, S.1    Plenat, T.2    Charnet, P.3    Divita, G.4    Molle, G.5    Heitz, F.6
  • 49
    • 0345275894 scopus 로고    scopus 로고
    • Penetrating and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential
    • Terrone D, Sang SL, Roudaia L, Silvius JR. Penetrating and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential. Biochemistry 2003; 42: 13787-13799.
    • (2003) Biochemistry , vol.42 , pp. 13787-13799
    • Terrone, D.1    Sang, S.L.2    Roudaia, L.3    Silvius, J.R.4
  • 51
    • 0034601787 scopus 로고    scopus 로고
    • Comparison of the membrane interaction and permeabilization by the designed peptide Ac-MB21-NH2 and truncated dermaseptin S3
    • Moll GN, Brul S, Konings WN, Driessen AJ. Comparison of the membrane interaction and permeabilization by the designed peptide Ac-MB21-NH2 and truncated dermaseptin S3. Biochemistry 2000; 39: 11907-11912.
    • (2000) Biochemistry , vol.39 , pp. 11907-11912
    • Moll, G.N.1    Brul, S.2    Konings, W.N.3    Driessen, A.J.4
  • 52
    • 0034695129 scopus 로고    scopus 로고
    • Rintoul MR, de Arcuri BF, Morero RD. Effects of the antibiotic peptide microcin J25 on liposomes: role of acyl chain length and negatively charged phospholipid. Biochim. Biophys. Acta 2000; 11509: 65-72.
    • Rintoul MR, de Arcuri BF, Morero RD. Effects of the antibiotic peptide microcin J25 on liposomes: role of acyl chain length and negatively charged phospholipid. Biochim. Biophys. Acta 2000; 11509: 65-72.
  • 53
    • 0034684272 scopus 로고    scopus 로고
    • Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism
    • Ibrahim HR, Sugimoto Y, Aoki T. Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim. Biophys. Acta 2000; 1523: 196-205.
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 196-205
    • Ibrahim, H.R.1    Sugimoto, Y.2    Aoki, T.3
  • 54
    • 33947686656 scopus 로고    scopus 로고
    • A fluorescence spectroscopy study on the interactions of the TAT-PTD peptide with model lipid membranes
    • Tiriveedhi V, Butko P. A fluorescence spectroscopy study on the interactions of the TAT-PTD peptide with model lipid membranes. Biochemistry 2007; 46: 3888-3895.
    • (2007) Biochemistry , vol.46 , pp. 3888-3895
    • Tiriveedhi, V.1    Butko, P.2
  • 55
    • 33748416305 scopus 로고    scopus 로고
    • Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1
    • Zhu WL, Lan H, Park IS, Kim JI, Jin HZ, Hahm KS, Shin SY. Design and mechanism of action of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1. Biochem. Biophys. Res. Commun. 2006; 349: 769-774.
    • (2006) Biochem. Biophys. Res. Commun , vol.349 , pp. 769-774
    • Zhu, W.L.1    Lan, H.2    Park, I.S.3    Kim, J.I.4    Jin, H.Z.5    Hahm, K.S.6    Shin, S.Y.7
  • 56
    • 33646003271 scopus 로고    scopus 로고
    • A flow cytometric assay to monitor antimicrobial activity of defensins and cationic tissue extracts
    • Nuding S, Fellermann K, Wehkamp J, Mueller HA, Stange EF. A flow cytometric assay to monitor antimicrobial activity of defensins and cationic tissue extracts. J. Microbiol. Methods 2006; 65: 335-345.
    • (2006) J. Microbiol. Methods , vol.65 , pp. 335-345
    • Nuding, S.1    Fellermann, K.2    Wehkamp, J.3    Mueller, H.A.4    Stange, E.F.5
  • 57
    • 33845622939 scopus 로고    scopus 로고
    • Interaction mode of a symmetric Trp-rich undeca peptide PST11-RK with lipid bilayers
    • Yang ST, Shin SY, Kim JI. Interaction mode of a symmetric Trp-rich undeca peptide PST11-RK with lipid bilayers. FEBS Lett. 2007; 581: 157-163.
    • (2007) FEBS Lett , vol.581 , pp. 157-163
    • Yang, S.T.1    Shin, S.Y.2    Kim, J.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.