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Volumn 96, Issue 5, 2009, Pages 1815-1827

Synergistic effects of the membrane actions of cecropin-melittin antimicrobial hybrid peptide BP100

Author keywords

[No Author keywords available]

Indexed keywords

BP 100; LIPID; PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; LYSYL LYSYL LEUCYL PHENYLALANYL LYSYL LYSYL ISOLEUCYL LEUCYL LYSYL TYROSYL LEUCINAMIDE; LYSYL-LYSYL-LEUCYL-PHENYLALANYL-LYSYL-LYSYL-ISOLEUCYL-LEUCYL-LYSYL-TYROSYL-LEUCINAMIDE; OLIGOPEPTIDE;

EID: 65549119292     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.11.053     Document Type: Article
Times cited : (80)

References (79)
  • 2
    • 1642545489 scopus 로고    scopus 로고
    • Antimicrobial peptides: From invertebrates to vertebrates
    • Bulet, P., R. Stocklin, and L. Menin. 2004. Antimicrobial peptides: from invertebrates to vertebrates. Immunol. Rev. 198:169-184.
    • (2004) Immunol. Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 3
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • Ganz, T., and R. I. Lehrer. 1998. Antimicrobial peptides of vertebrates. Curr. Opin. Immunol. 10:41-44.
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 41-44
    • Ganz, T.1    Lehrer, R.I.2
  • 5
    • 0033754189 scopus 로고    scopus 로고
    • Antibacterial peptides isolated from insects
    • Otvos, L., Jr. 2000. Antibacterial peptides isolated from insects. J. Pept. Sci. 6:497-511.
    • (2000) J. Pept. Sci , vol.6 , pp. 497-511
    • Otvos Jr., L.1
  • 6
    • 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
  • 8
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic antimicrobial peptides: From natural to novel antibiotics
    • Hancock, R. E., and A. Patrzykat. 2002. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr. Drug Targets Infect. Disord. 2:79-83.
    • (2002) Curr. Drug Targets Infect. Disord , vol.2 , pp. 79-83
    • Hancock, R.E.1    Patrzykat, A.2
  • 9
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E., and H. G. Sahl. 2006. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24:1551-1557.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 10
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman, H. G. 2003. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254:197-215.
    • (2003) J. Intern. Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 11
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock, R. E. 2001. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1:156-164.
    • (2001) Lancet Infect. Dis , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 13
    • 34247137266 scopus 로고    scopus 로고
    • Antimicrobial peptides and plant disease control
    • Montesinos, E. 2007. Antimicrobial peptides and plant disease control. FEMS Microbiol. Lett. 270:1-11.
    • (2007) FEMS Microbiol. Lett , vol.270 , pp. 1-11
    • Montesinos, E.1
  • 14
    • 33645803815 scopus 로고    scopus 로고
    • Antimicrobial peptides: Therapeutic potential
    • Zhang, L., and T. J. Falla. 2006. Antimicrobial peptides: therapeutic potential. Expert Opin. Pharmacother. 7:653-663.
    • (2006) Expert Opin. Pharmacother , vol.7 , pp. 653-663
    • Zhang, L.1    Falla, T.J.2
  • 15
    • 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
  • 16
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R., and N. Y. Yount. 2003. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55:27-55.
    • (2003) Pharmacol. Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 17
    • 33645834508 scopus 로고    scopus 로고
    • Experimental evolution of resistance to an antimicrobial peptide
    • Perron, G. G., M. Zasloff, and G. Bell. 2006. Experimental evolution of resistance to an antimicrobial peptide. Proc. Biol. Sci. 273:251-256.
    • (2006) Proc. Biol. Sci , vol.273 , pp. 251-256
    • Perron, G.G.1    Zasloff, M.2    Bell, G.3
  • 18
    • 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
  • 19
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi, A., L. Sandri, and A. Giangaspero. 2000. Amphipathic, α-helical antimicrobial peptides. Biopolymers. 55:4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 20
    • 3042620560 scopus 로고    scopus 로고
    • Structure and function of membrane-lytic peptides
    • Bechinger, B. 2004. Structure and function of membrane-lytic peptides. Crit. Rev. Plant Sci. 23:271-292.
    • (2004) Crit. Rev. Plant Sci , vol.23 , pp. 271-292
    • Bechinger, B.1
  • 21
    • 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
  • 22
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. 1999. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta. 1462:55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 23
    • 10644260444 scopus 로고    scopus 로고
    • Membrane translocation mechanism of the antimicrobial peptide buforin 2
    • Kobayashi, S., A. Chikushi, S. Tougu, Y. Imura, M. Nishida, et al. 2004. Membrane translocation mechanism of the antimicrobial peptide buforin 2. Biochemistry. 43:15610-15616.
    • (2004) Biochemistry , vol.43 , pp. 15610-15616
    • Kobayashi, S.1    Chikushi, A.2    Tougu, S.3    Imura, Y.4    Nishida, M.5
  • 24
    • 0020366780 scopus 로고
    • Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae
    • Hultmark, D., A. Engstrom, H. Bennich, R. Kapur, and H. G. Boman. 1982. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur. J. Biochem. 127:207-217.
    • (1982) Eur. J. Biochem , vol.127 , pp. 207-217
    • Hultmark, D.1    Engstrom, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 25
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark, D., H. Steiner, T. Rasmuson, and H. G. Boman. 1980. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 106:7-16.
    • (1980) Eur. J. Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 26
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides
    • Sato, H., and J. B. Feix. 2006. Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides. Biochim. Biophys. Acta. 1758:1245-1256.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 28
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H., D. Hultmark, A. Engstrom, H. Bennich, and H. G. Boman. 1981. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature. 292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 29
    • 0942301299 scopus 로고    scopus 로고
    • Safety and efficacy of antimicrobial peptides against naturally acquired Leishmaniasis
    • Alberola, J., A. Rodriguez, O. Francino, X. Roura, L. Rivas, et al. 2004. Safety and efficacy of antimicrobial peptides against naturally acquired Leishmaniasis. Antimicrob. Agents Chemother. 48:641-643.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 641-643
    • Alberola, J.1    Rodriguez, A.2    Francino, O.3    Roura, X.4    Rivas, L.5
  • 30
    • 0026570489 scopus 로고
    • Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity
    • Andreu, D., J. Ubach, A. Boman, B. Wahlin, D. Wade, et al. 1992. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. FEBS Lett. 296:190-194.
    • (1992) FEBS Lett , vol.296 , pp. 190-194
    • Andreu, D.1    Ubach, J.2    Boman, A.3    Wahlin, B.4    Wade, D.5
  • 31
    • 0024841875 scopus 로고
    • Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids
    • Boman, H. G., D. Wade, I. A. Boman, B. Wahlin, and R. B. Merrifield. 1989. Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259:103-106.
    • (1989) FEBS Lett , vol.259 , pp. 103-106
    • Boman, H.G.1    Wade, D.2    Boman, I.A.3    Wahlin, B.4    Merrifield, R.B.5
  • 32
    • 0032031617 scopus 로고    scopus 로고
    • Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens
    • Cavallarin, L., D. Andreu, and B. San Segundo. 1998. Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens. Mol. Plant Microbe Interact. 11:218-227.
    • (1998) Mol. Plant Microbe Interact , vol.11 , pp. 218-227
    • Cavallarin, L.1    Andreu, D.2    San Segundo, B.3
  • 33
    • 0034862968 scopus 로고    scopus 로고
    • N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide
    • Chicharro, C., C. Granata, R. Lozano, D. Andreu, and L. Rivas. 2001. N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide. Antimicrob. Agents Chemother. 45:2441-2449.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 2441-2449
    • Chicharro, C.1    Granata, C.2    Lozano, R.3    Andreu, D.4    Rivas, L.5
  • 35
    • 2342604971 scopus 로고    scopus 로고
    • Structure-antiviral activity relationships of cecropin A-magainin 2 hybrid peptide and its analogues
    • Lee, D. G., Y. Park, I. Jin, K. S. Hahm, H. H. Lee, et al. 2004. Structure-antiviral activity relationships of cecropin A-magainin 2 hybrid peptide and its analogues. J. Pept. Sci. 10:298-303.
    • (2004) J. Pept. Sci , vol.10 , pp. 298-303
    • Lee, D.G.1    Park, Y.2    Jin, I.3    Hahm, K.S.4    Lee, H.H.5
  • 36
  • 37
    • 0033905698 scopus 로고    scopus 로고
    • Inhibition of fungal and bacterial plant pathogens by synthetic peptides: In vitro growth inhibition, interaction between peptides and inhibition of disease progression
    • Ali, G. S., and A. S. Reddy. 2000. Inhibition of fungal and bacterial plant pathogens by synthetic peptides: in vitro growth inhibition, interaction between peptides and inhibition of disease progression. Mol. Plant Microbe Interact. 13:847-859.
    • (2000) Mol. Plant Microbe Interact , vol.13 , pp. 847-859
    • Ali, G.S.1    Reddy, A.S.2
  • 38
    • 36148939499 scopus 로고    scopus 로고
    • A library of linear undecapeptides with bactericidal activity against phytopathogenic bacteria
    • Badosa, E., R. Ferre, M. Planas, L. Feliu, E. Besalu, et al. 2007. A library of linear undecapeptides with bactericidal activity against phytopathogenic bacteria. Peptides. 28:2276-2285.
    • (2007) Peptides , vol.28 , pp. 2276-2285
    • Badosa, E.1    Ferre, R.2    Planas, M.3    Feliu, L.4    Besalu, E.5
  • 39
    • 85031356043 scopus 로고    scopus 로고
    • Bardají, E., E. Montesinos, E. Badosa, L. Feliu, M. Planas, et al. 2006. Antimicrobial linear peptides. P200601098; priority date: April 28th, 2006; Oficina Española de Patentes y Marcas, Spain.
    • Bardají, E., E. Montesinos, E. Badosa, L. Feliu, M. Planas, et al. 2006. Antimicrobial linear peptides. P200601098; priority date: April 28th, 2006; Oficina Española de Patentes y Marcas, Spain.
  • 40
    • 33646576163 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides
    • Ferre, R., E. Badosa, L. Feliu, M. Planas, E. Montesinos, et al. 2006. Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides. Appl. Environ. Microbiol. 72:3302-3308.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 3302-3308
    • Ferre, R.1    Badosa, E.2    Feliu, L.3    Planas, M.4    Montesinos, E.5
  • 41
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., J. Fink, R. B. Merrifield, and D. Mauzerall. 1988. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA. 85:5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 42
    • 0030971376 scopus 로고    scopus 로고
    • Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: Pore formation by melittin
    • Ladokhin, A. S., M. E. Selsted, and S. H. White. 1997. Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin. Biophys. J. 72:1762-1766.
    • (1997) Biophys. J , vol.72 , pp. 1762-1766
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 43
    • 0035479424 scopus 로고    scopus 로고
    • Detergent-like permeabilization of anionic lipid vesicles by melittin
    • Ladokhin, A. S., and S. H. White. 2001. "Detergent-like" permeabilization of anionic lipid vesicles by melittin. Biochim. Biophys. Acta. 1514:253-260.
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 44
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • Silvestro, L., K. Gupta, J. N. Weiser, and P. H. Axelsen. 1997. The concentration-dependent membrane activity of cecropin A. Biochemistry. 36:11452-11460.
    • (1997) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 45
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • Steiner, H., D. Andreu, and R. B. Merrifield. 1988. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta. 939:260-266.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 46
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • Mayer, L. D., M. J. Hope, and P. R. Cullis. 1986. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta. 858:161-168.
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 47
    • 4043134641 scopus 로고    scopus 로고
    • Fluorescence spectroscopy methodologies on the study of proteins and peptides. On the 150th anniversary of protein fluorescence
    • Santos, N. C., and M. A. Castanho. 2002. Fluorescence spectroscopy methodologies on the study of proteins and peptides. On the 150th anniversary of protein fluorescence. Trends Appl. Spectrosc. 4:113-125.
    • (2002) Trends Appl. Spectrosc , vol.4 , pp. 113-125
    • Santos, N.C.1    Castanho, M.A.2
  • 48
    • 0001336544 scopus 로고
    • 1 and alcohol-dehydrogenase fluorescence quenching by acrylamide - a laboratory experiment for undergraduate students
    • 1 and alcohol-dehydrogenase fluorescence quenching by acrylamide - a laboratory experiment for undergraduate students. J. Chem. Educ. 70:425-428.
    • (1993) J. Chem. Educ , vol.70 , pp. 425-428
    • Coutinho, A.1    Prieto, M.2
  • 49
    • 0038392423 scopus 로고    scopus 로고
    • Quantifying molecular partition into model systems of biomembranes: An emphasis on optical spectroscopic methods
    • Santos, N. C., M. Prieto, and M. A. Castanho. 2003. Quantifying molecular partition into model systems of biomembranes: an emphasis on optical spectroscopic methods. Biochim. Biophys. Acta. 1612:123-135.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 123-135
    • Santos, N.C.1    Prieto, M.2    Castanho, M.A.3
  • 50
    • 0024280716 scopus 로고
    • Structure of fully hydrated bilayer dispersions
    • Nagle, J. F., and M. C. Wiener. 1988. Structure of fully hydrated bilayer dispersions. Biochim. Biophys. Acta. 942:1-10.
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 1-10
    • Nagle, J.F.1    Wiener, M.C.2
  • 51
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin, A. S., S. Jayasinghe, and S. H. White. 2000. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal. Biochem. 285:235-245.
    • (2000) Anal. Biochem , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 52
    • 0032539980 scopus 로고    scopus 로고
    • Magainin 2 amide interaction with lipid membranes: Calorimetric detection of peptide binding and pore formation
    • Wenk, M. R., and J. Seelig. 1998. Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation. Biochemistry. 37:3909-3916.
    • (1998) Biochemistry , vol.37 , pp. 3909-3916
    • Wenk, M.R.1    Seelig, J.2
  • 53
    • 34047249400 scopus 로고    scopus 로고
    • Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation
    • Melo, M. N., and M. A. Castanho. 2007. Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation. Biochim. Biophys. Acta. 1768:1277-1290.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1277-1290
    • Melo, M.N.1    Castanho, M.A.2
  • 54
    • 0001639244 scopus 로고
    • Interaction of fluorescence quenchers with the n-(9-anthroyloxy) fatty acid membrane probes
    • Chalpin, D. B., and A. M. Kleinfeld. 1983. Interaction of fluorescence quenchers with the n-(9-anthroyloxy) fatty acid membrane probes. Biochim. Biophys. Acta. 731:465-474.
    • (1983) Biochim. Biophys. Acta , vol.731 , pp. 465-474
    • Chalpin, D.B.1    Kleinfeld, A.M.2
  • 55
    • 0036667912 scopus 로고    scopus 로고
    • Joint determination by Brownian dynamics and fluorescence quenching of the in-depth location profile of biomolecules in membranes
    • Fernandes, M. X., J. Garcia de la Torre, and M. A. Castanho. 2002. Joint determination by Brownian dynamics and fluorescence quenching of the in-depth location profile of biomolecules in membranes. Anal. Biochem. 307:1-12.
    • (2002) Anal. Biochem , vol.307 , pp. 1-12
    • Fernandes, M.X.1    Garcia de la Torre, J.2    Castanho, M.A.3
  • 56
    • 0024281192 scopus 로고
    • Spectroscopic and ionization properties of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids in model membranes
    • Chattopadhyay, A., and E. London. 1988. Spectroscopic and ionization properties of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids in model membranes. Biochim. Biophys. Acta. 938:24-34.
    • (1988) Biochim. Biophys. Acta , vol.938 , pp. 24-34
    • Chattopadhyay, A.1    London, E.2
  • 57
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides
    • Pokorny, A., and P. F. Almeida. 2004. Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides. Biochemistry. 43:8846-8857.
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.2
  • 58
    • 40549089488 scopus 로고    scopus 로고
    • Quenching of fluorescence
    • 2nd Ed. Kluwer Academic/Plenum, New York; London
    • Lakowicz, J. R. 1999. Quenching of fluorescence. Principles of Fluorescence Spectroscopy, 2nd Ed. Kluwer Academic/Plenum, New York; London.
    • (1999) Principles of Fluorescence Spectroscopy
    • Lakowicz, J.R.1
  • 59
    • 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., A. Cavenaugh, V. Journigan, A. Pokorny, and P. F. Almeida. 2008. A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A. Biophys. J. 94:1667-1680.
    • (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
  • 60
    • 0029941363 scopus 로고    scopus 로고
    • Development and validation of alternative metabolic systems for mutagenicity testing in short-term assays
    • Rueff, J., C. Chiapella, J. K. Chipman, F. Darroudi, I. D. Silva, et al. 1996. Development and validation of alternative metabolic systems for mutagenicity testing in short-term assays. Mutat. Res. 353:151-176.
    • (1996) Mutat. Res , vol.353 , pp. 151-176
    • Rueff, J.1    Chiapella, C.2    Chipman, J.K.3    Darroudi, F.4    Silva, I.D.5
  • 61
    • 0002774291 scopus 로고    scopus 로고
    • Cellular models for in vitro toxicity testing
    • M. Clynes, editor. Springer, Berlin; London
    • Zucco, F., I. De Angelis, and A. Stammati. 1998. Cellular models for in vitro toxicity testing. In Animal Cell Culture Techniques. M. Clynes, editor. Springer, Berlin; London.
    • (1998) Animal Cell Culture Techniques
    • Zucco, F.1    De Angelis, I.2    Stammati, A.3
  • 62
    • 3142610868 scopus 로고    scopus 로고
    • Experimental survey of non-clonogenic viability assays for adherent cells in vitro
    • Mickuviene, I., V. Kirveliene, and B. Juodka. 2004. Experimental survey of non-clonogenic viability assays for adherent cells in vitro. Toxicol. In Vitro. 18:639-648.
    • (2004) Toxicol. In Vitro , vol.18 , pp. 639-648
    • Mickuviene, I.1    Kirveliene, V.2    Juodka, B.3
  • 63
    • 0023932632 scopus 로고
    • Potential applicability of nonclonogenic measurements to clinical oncology
    • Mitchell, J. B. 1988. Potential applicability of nonclonogenic measurements to clinical oncology. Radiat. Res. 114:401-414.
    • (1988) Radiat. Res , vol.114 , pp. 401-414
    • Mitchell, J.B.1
  • 64
    • 41949094877 scopus 로고    scopus 로고
    • Studies on cellular resilience and adaptation following acute and repetitive exposure to ozone in cultured human epithelial (HeLa) cells
    • Brink, C. B., A. Pretorius, B. P. van Niekerk, D. W. Oliver, and D. P. Venter. 2008. Studies on cellular resilience and adaptation following acute and repetitive exposure to ozone in cultured human epithelial (HeLa) cells. Redox Rep. 13:87-100.
    • (2008) Redox Rep , vol.13 , pp. 87-100
    • Brink, C.B.1    Pretorius, A.2    van Niekerk, B.P.3    Oliver, D.W.4    Venter, D.P.5
  • 65
    • 0042430615 scopus 로고    scopus 로고
    • In vitro and in vivo activity of an antibacterial peptide analog against uropathogens
    • Cudic, M., C. V. Lockatell, D. E. Johnson, and L. Otvos, Jr. 2003. In vitro and in vivo activity of an antibacterial peptide analog against uropathogens. Peptides. 24:807-820.
    • (2003) Peptides , vol.24 , pp. 807-820
    • Cudic, M.1    Lockatell, C.V.2    Johnson, D.E.3    Otvos Jr., L.4
  • 66
    • 0035142541 scopus 로고    scopus 로고
    • A general best-fit method for concentration-response curves and the estimation of low-effect concentrations
    • Scholze, M., W. Boedeker, M. Faust, T. Backhaus, R. Altenburger, et al. 2001. A general best-fit method for concentration-response curves and the estimation of low-effect concentrations. Environ. Toxicol. Chem. 20:448-457.
    • (2001) Environ. Toxicol. Chem , vol.20 , pp. 448-457
    • Scholze, M.1    Boedeker, W.2    Faust, M.3    Backhaus, T.4    Altenburger, R.5
  • 67
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action
    • Zhao, H., R. Sood, A. Jutila, S. Bose, G. Fimland, et al. 2006. Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action. Biochim. Biophys. Acta. 1758:1461-1474.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5
  • 68
    • 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
  • 69
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • Huang, H. W. 2006. Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim. Biophys. Acta. 1758:1292-1302.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 71
    • 33646198955 scopus 로고    scopus 로고
    • Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: A systematic investigation of hydrophobic mismatch
    • Kandasamy, S. K., and R. G. Larson. 2006. Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophys. J. 90:2326-2343.
    • (2006) Biophys. J , vol.90 , pp. 2326-2343
    • Kandasamy, S.K.1    Larson, R.G.2
  • 72
    • 25444466265 scopus 로고    scopus 로고
    • Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition
    • Abrunhosa, F., S. Faria, P. Gomes, I. Tomaz, J. C. Pessoa, et al. 2005. Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition. J. Phys. Chem. B. 109:17311-17319.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 17311-17319
    • Abrunhosa, F.1    Faria, S.2    Gomes, P.3    Tomaz, I.4    Pessoa, J.C.5
  • 73
    • 0030178188 scopus 로고    scopus 로고
    • Hydrophobic effects on antibacterial and channel-forming properties of cecropin A-melittin hybrids
    • Juvvadi, P., S. Vunnam, E. L. Merrifield, H. G. Boman, and R. B. Merrifield. 1996. Hydrophobic effects on antibacterial and channel-forming properties of cecropin A-melittin hybrids. J. Pept. Sci. 2:223-232.
    • (1996) J. Pept. Sci , vol.2 , pp. 223-232
    • Juvvadi, P.1    Vunnam, S.2    Merrifield, E.L.3    Boman, H.G.4    Merrifield, R.B.5
  • 74
    • 48249157851 scopus 로고    scopus 로고
    • Biomolecular engineering by combinatorial design and high-throughput screening: Small, soluble peptides that permeabilize membranes
    • Rathinakumar, R., and W. C. Wimley. 2008. Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes. J. Am. Chem. Soc. 130:9849-9858.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 9849-9858
    • Rathinakumar, R.1    Wimley, W.C.2
  • 75
    • 34249036121 scopus 로고    scopus 로고
    • How to address CPP and AMP translocation? Methods to detect and quantify peptide internalization in vitro and in vivo. (Review)
    • Henriques, S. T., M. N. Melo, and M. A. Castanho. 2007. How to address CPP and AMP translocation? Methods to detect and quantify peptide internalization in vitro and in vivo. (Review). Mol. Membr. Biol. 24:173-184.
    • (2007) Mol. Membr. Biol , vol.24 , pp. 173-184
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.3
  • 76
    • 0030037217 scopus 로고    scopus 로고
    • Transbilayer transport of ions and lipids coupled with mastoparan X translocation
    • Matsuzaki, K., S. Yoneyama, O. Murase, and K. Miyajima. 1996. Transbilayer transport of ions and lipids coupled with mastoparan X translocation. Biochemistry. 35:8450-8456.
    • (1996) Biochemistry , vol.35 , pp. 8450-8456
    • Matsuzaki, K.1    Yoneyama, S.2    Murase, O.3    Miyajima, K.4
  • 77
    • 0035860429 scopus 로고    scopus 로고
    • Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles
    • Persson, D., P. E. Thoren, and B. Norden. 2001. Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles. FEBS Lett. 505:307-312.
    • (2001) FEBS Lett , vol.505 , pp. 307-312
    • Persson, D.1    Thoren, P.E.2    Norden, B.3
  • 78
    • 0342264510 scopus 로고    scopus 로고
    • Insect peptides with improved protease-resistance protect mice against bacterial infection
    • Otvos, L., Jr., K. Bokonyi, I. Varga, B. I. Otvos, R. Hoffmann, et al. 2000. Insect peptides with improved protease-resistance protect mice against bacterial infection. Protein Sci. 9:742-749.
    • (2000) Protein Sci , vol.9 , pp. 742-749
    • Otvos Jr., L.1    Bokonyi, K.2    Varga, I.3    Otvos, B.I.4    Hoffmann, R.5
  • 79
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on Gram-positive bacteria
    • Friedrich, C. L., D. Moyles, T. J. Beveridge, and R. E. Hancock. 2000. Antibacterial action of structurally diverse cationic peptides on Gram-positive bacteria. Antimicrob. Agents Chemother. 44:2086-2092.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4


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