메뉴 건너뛰기




Volumn 165, Issue 4, 2012, Pages 365-373

Effect of head Group and curvature on binding of the antimicrobial peptide tritrpticin to lipid membranes

Author keywords

tritrpticin, antimicrobial peptide, micelles, bilayers, spectroscopic techniques, toroidal pore

Indexed keywords

LYSOPHOSPHOLIPID; POLYPEPTIDE ANTIBIOTIC AGENT; TRITRPTICIN; UNCLASSIFIED DRUG;

EID: 84860779822     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2011.12.005     Document Type: Conference Paper
Times cited : (41)

References (67)
  • 1
    • 33749076672 scopus 로고    scopus 로고
    • Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy
    • V.V. Andrushchenko, H.J. Vogel, and E.J. Prenner Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy Biochim. Biophys. Acta 1758 2006 1596 1608
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1596-1608
    • Andrushchenko, V.V.1    Vogel, H.J.2    Prenner, E.J.3
  • 2
    • 34948879131 scopus 로고    scopus 로고
    • Interactions of trypthophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry
    • V.V. Andrushchenko, H.J. Vogel, and E.J. Prenner Interactions of trypthophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry Biochim. Biophys. Acta 1768 2007 2447 2458
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2447-2458
    • Andrushchenko, V.V.1    Vogel, H.J.2    Prenner, E.J.3
  • 3
    • 40949131305 scopus 로고    scopus 로고
    • Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes
    • V.V. Andrushchenko, M.H. Aarabi, L.T. Nguyen, E.J. Prenner, and H.J. Vogel Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes Biochim. Biophys. Acta 1778 2008 1004 1014
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1004-1014
    • Andrushchenko, V.V.1    Aarabi, M.H.2    Nguyen, L.T.3    Prenner, E.J.4    Vogel, H.J.5
  • 4
    • 79953805263 scopus 로고    scopus 로고
    • Insights into the mechanism of action of host defence peptides from biophysical and structural investigations
    • B. Bechinger Insights into the mechanism of action of host defence peptides from biophysical and structural investigations J. Peptide Sci. 17 2011 306 314
    • (2011) J. Peptide Sci. , vol.17 , pp. 306-314
    • Bechinger, B.1
  • 5
    • 0032738473 scopus 로고    scopus 로고
    • Lipid-induced conformation and lipid binding properties of cytolytic and antimicrobial peptides: Determination and biological specificity
    • S.E. Blondelle, K. Lohner, and M.I. Aguilar Lipid-induced conformation and lipid binding properties of cytolytic and antimicrobial peptides: determination and biological specificity Biochim. Biophys. Acta 1462 1999 89 108
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 89-108
    • Blondelle, S.E.1    Lohner, K.2    Aguilar, M.I.3
  • 6
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nature Rev
    • K. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nature Rev Microbiol. 3 2005 238 250
    • (2005) Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.1
  • 7
    • 33748988741 scopus 로고    scopus 로고
    • Tryphtophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • D.I. Chan, E.J. Prenner, and H.J. Vogel Tryphtophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action Biochim. Biophys. Acta 1758 2006 1184 1202
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 9
    • 33847798446 scopus 로고
    • Fluorescence quenching of indole and model micelle systems
    • M.R. Eftink, and C.A. Ghiron Fluorescence quenching of indole and model micelle systems J. Phys. Chem 80 1976 486 493
    • (1976) J. Phys. Chem , vol.80 , pp. 486-493
    • Eftink, M.R.1    Ghiron, C.A.2
  • 10
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • G. Ehrenstein, and H. Lecar Electrically gated ionic channels in lipid bilayers Q. Rev. Biophys. 10 1977 1 34
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 11
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • R.M. Epand, and R.F. Epand Lipid domains in bacterial membranes and the action of antimicrobial agents Biochim. Biophys. Acta 1788 2009 289 294
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 12
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 14
    • 0021764821 scopus 로고
    • Bacterial membranes and lipid packing theory
    • H. Goldfine Bacterial membranes and lipid packing theory J. Lipid Res. 25 1984 1501 1507
    • (1984) J. Lipid Res. , vol.25 , pp. 1501-1507
    • Goldfine, H.1
  • 15
    • 0028716614 scopus 로고
    • Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators
    • I.B. Grishina, and R.W. Woody Contributions of tryptophan side chains to the circular dichroism of globular proteins: exciton couplets and coupled oscillators Faraday Discuss. 99 1994 245 262
    • (1994) Faraday Discuss. , vol.99 , pp. 245-262
    • Grishina, I.B.1    Woody, R.W.2
  • 16
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • Huang, H.W.; Chen, F.-Y.; Lee, M.-T.; 2004. Molecular mechanism of peptide-induced pores in membranes. Phys. Rev. Lett. 92, 198304/1-198304/4.
    • (2004) Phys. Rev. Lett. , vol.92
    • Huang H., .W.1    Chen F., .-Y.2    Lee M., .-T.3
  • 17
    • 13844308071 scopus 로고    scopus 로고
    • Membrane interactions of host-defense peptides studied in model systems
    • R. Jelinek, and S. Kolusheva Membrane interactions of host-defense peptides studied in model systems Curr. Opin. Protein Pept. Sci. 6 2005 103 114
    • (2005) Curr. Opin. Protein Pept. Sci. , vol.6 , pp. 103-114
    • Jelinek, R.1    Kolusheva, S.2
  • 20
    • 0030586288 scopus 로고    scopus 로고
    • Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides
    • C. Lawyer, S. Pai, M. Watabe, P. Borgia, T. Mashimo, L. Eagleton, and K. Watabe Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides FEBS Lett. 390 1996 95 98
    • (1996) FEBS Lett. , vol.390 , pp. 95-98
    • Lawyer, C.1    Pai, S.2    Watabe, M.3    Borgia, P.4    Mashimo, T.5    Eagleton, L.6    Watabe, K.7
  • 21
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • M.-T. Lee, F.-T. Chen, and H.W. Huang Energetics of pore formation induced by membrane active peptides Biochemistry 43 2004 3590 3599
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.-T.1    Chen, F.-T.2    Huang, H.W.3
  • 22
  • 23
    • 0002336563 scopus 로고    scopus 로고
    • The role of the membrane lipid composition in cell targeting of antimicrobial peptides
    • K. Lohner (Ed.) Horizon Scientific Press, Wymondham, Norfolk, U.K.
    • Lohner, K.; 2001. The role of the membrane lipid composition in cell targeting of antimicrobial peptides, in: K. Lohner (Ed.) Development of novel antimicrobial agents: emerging strategies, Horizon Scientific Press, Wymondham, Norfolk, U.K.; pp. 149-165.
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 149-165
    • Lohner, K.1
  • 24
    • 67650957816 scopus 로고    scopus 로고
    • New strategies for novel antibiotics: Peptides targeting bacterial cell membranes
    • K. Lohner New strategies for novel antibiotics: peptides targeting bacterial cell membranes Gen. Physiol. Biophys. 28 2009 105 116
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 105-116
    • Lohner, K.1
  • 25
    • 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
    • K. Lohner, and S.E. Blondelle 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 Screening 8 2005 241 256
    • (2005) Comb. Chem. High Throughput Screening , vol.8 , pp. 241-256
    • Lohner, K.1    Blondelle, S.E.2
  • 27
    • 0037181999 scopus 로고    scopus 로고
    • Solvation of polymers as model for solvent effect investigation: Proposition of a novel polarity scale
    • L. Malavolta, E. Oliveira, E. Cilli, and C.R. Nakaie Solvation of polymers as model for solvent effect investigation: proposition of a novel polarity scale Tetrahedron 58 2002 4383 4394
    • (2002) Tetrahedron , vol.58 , pp. 4383-4394
    • Malavolta, L.1    Oliveira, E.2    Cilli, E.3    Nakaie, C.R.4
  • 28
    • 0034866366 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self defense?
    • K. Matsuzaki Why and how are peptide-lipid interactions utilized for self defense? Biochem. Soc. Trans. 29 2001 598 601
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 598-601
    • Matsuzaki, K.1
  • 29
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobal peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • K. Matsuzaki, O. Murase, N. Fujii, and K. Miyajima An antimicrobal peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation Biochemistry 35 1996 11361 11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 30
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • R.B. Merrifield Solid phase peptide synthesis. I. The synthesis of a tetrapeptide J. Am. Chem. Soc 85 1963 2149 2154
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 31
    • 0033551685 scopus 로고    scopus 로고
    • Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin
    • S. Nagpal, V. Gupta, K.J. Kaur, and D.M. Salunke Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin J. Biol. Chem. 274 1999 23296 23304
    • (1999) J. Biol. Chem. , vol.274 , pp. 23296-23304
    • Nagpal, S.1    Gupta, V.2    Kaur, K.J.3    Salunke, D.M.4
  • 32
    • 0036707998 scopus 로고    scopus 로고
    • Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin
    • S. Nagpal, K.J. Kaur, D. Jain, and D.M. Salunke Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin Protein Sci. 11 2002 2158 2167
    • (2002) Protein Sci. , vol.11 , pp. 2158-2167
    • Nagpal, S.1    Kaur, K.J.2    Jain, D.3    Salunke, D.M.4
  • 33
    • 79959936150 scopus 로고    scopus 로고
    • Investigating the cationic side chains of the antimicrobial peptide tritrpticin: Hydrogen bonding properties govern its membrane-disruptive activities
    • L.T. Nguyen, L. deBoer, S.A.J. Zaat, and H.J. Vogel Investigating the cationic side chains of the antimicrobial peptide tritrpticin: hydrogen bonding properties govern its membrane-disruptive activities Biochim. Biophys Acta 1808 2011 2297 2303
    • (2011) Biochim. Biophys Acta , vol.1808 , pp. 2297-2303
    • Nguyen, L.T.1    Deboer, L.2    Zaat, S.A.J.3    Vogel, H.J.4
  • 34
    • 0028856941 scopus 로고
    • Conformational changes upon binding of a receptor loop to lipid structures: Possible role in signal transduction
    • T.A. Pertinhez, C.R. Nakaie, R.S. Carvalho, A.C.M. Paiva, M. Tabak, F. Toma, and S. Schreier Conformational changes upon binding of a receptor loop to lipid structures: possible role in signal transduction FEBS Lett. 375 1995 239 242
    • (1995) FEBS Lett. , vol.375 , pp. 239-242
    • Pertinhez, T.A.1    Nakaie, C.R.2    Carvalho, R.S.3    Paiva, A.C.M.4    Tabak, M.5    Toma, F.6    Schreier, S.7
  • 35
    • 0031541028 scopus 로고    scopus 로고
    • Spin-labeled extracellular loop from a seven-transmembrane helix receptor: Studies in solution and interaction with model membranes
    • T.A. Pertinhez, C.R. Nakaie, A.C.M. Paiva, and S. Schreier Spin-labeled extracellular loop from a seven-transmembrane helix receptor: studies in solution and interaction with model membranes Biopolymers 42 1997 821 829
    • (1997) Biopolymers , vol.42 , pp. 821-829
    • Pertinhez, T.A.1    Nakaie, C.R.2    Paiva, A.C.M.3    Schreier, S.4
  • 36
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Y. Pouny, D. Rapaport, A. Mor, P. Nicolas, and Y. Shai Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes Biochemistry 31 1992 12416 12423
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 37
    • 0017356323 scopus 로고
    • Membrane asymmetry
    • J.E. Rothman, and J. Leonard Membrane asymmetry Science 195 1977 743 753
    • (1977) Science , vol.195 , pp. 743-753
    • Rothman, J.E.1    Leonard, J.2
  • 38
    • 0014779155 scopus 로고
    • Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorous analysis of spots
    • G. Rouser, S. Fleisher, and A. Yamamoto Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorous analysis of spots Lipids 5 1970 494 496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleisher, S.2    Yamamoto, A.3
  • 39
    • 2342501360 scopus 로고    scopus 로고
    • Ion channel-like activity of the antimicrobial peptide tritrpticin in planar lipid bilayers
    • L.C. Salay, J. Procopio, E. Oliveira, C.R. Nakaie, and S. Schreier Ion channel-like activity of the antimicrobial peptide tritrpticin in planar lipid bilayers FEBS Lett. 565 2004 171 175
    • (2004) FEBS Lett. , vol.565 , pp. 171-175
    • Salay, L.C.1    Procopio, J.2    Oliveira, E.3    Nakaie, C.R.4    Schreier, S.5
  • 40
    • 0037026868 scopus 로고    scopus 로고
    • Trifluoroethanol and binding to model membranes stabilize a predicted turn in a peptide corresponding to the first extracellular loop of the angiotensin II AT1A receptor
    • R.K. Salinas, C.S. Shida, T.A. Pertinhez, A. Spisni, C.R. Nakaie, A.C.M. Paiva, and S. Schreier Trifluoroethanol and binding to model membranes stabilize a predicted turn in a peptide corresponding to the first extracellular loop of the angiotensin II AT1A receptor Biopolymers 65 2002 21 31
    • (2002) Biopolymers , vol.65 , pp. 21-31
    • Salinas, R.K.1    Shida, C.S.2    Pertinhez, T.A.3    Spisni, A.4    Nakaie, C.R.5    Paiva, A.C.M.6    Schreier, S.7
  • 41
    • 0033592961 scopus 로고    scopus 로고
    • Structure of the antimicrobial peptide tritrpticin bound to micelles: A distinct membrane-bound peptide fold
    • D.J. Schibli, P.M. Hwang, and H.J. Vogel Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold Biochemistry 38 1999 16749 16755
    • (1999) Biochemistry , vol.38 , pp. 16749-16755
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 42
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: Comparative properties and membrane interactions
    • D.J. Schibli, R.F. Epand, H.J. Vogel, and R.M. Epand Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions Biochem. Cell. Biol. 80 2002 667 677
    • (2002) Biochem. Cell. Biol. , vol.80 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, H.J.3    Epand, R.M.4
  • 43
    • 33845461993 scopus 로고    scopus 로고
    • Structure-function analysis of tritrpticin analogs: Potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures
    • D.J. Schibli, L.Y. Nguyen, S.D. Kernaghan, O. Rekdal, and H.J. Vogel Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures Biophys. J. 91 2006 4413 4426
    • (2006) Biophys. J. , vol.91 , pp. 4413-4426
    • Schibli, D.J.1    Nguyen, L.Y.2    Kernaghan, S.D.3    Rekdal, O.4    Vogel, H.J.5
  • 44
    • 0034707095 scopus 로고    scopus 로고
    • Surface active drugs: Self-association and interaction with membranes and surfactants. Physicochemical and biological aspects
    • S. Schreier, S.V. Malheiros, and E. de Paula Surface active drugs: self-association and interaction with membranes and surfactants. Physicochemical and biological aspects Biochim. Biophys. Acta 1508 2000 210 234
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 210-234
    • Schreier, S.1    Malheiros, S.V.2    De Paula, E.3
  • 46
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 47
    • 33645960442 scopus 로고    scopus 로고
    • Antimicrobial peptides with unusual amino acid compositions and unusual structures
    • N. Sitaram Antimicrobial peptides with unusual amino acid compositions and unusual structures Curr. Med. Chem. 13 2006 679 696
    • (2006) Curr. Med. Chem. , vol.13 , pp. 679-696
    • Sitaram, N.1
  • 48
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • N. Sitaram, and R. Nagaraj Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity Biochim. Biophys. Acta 1462 1999 29 54
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 49
    • 0024713558 scopus 로고
    • Polymorphic phase behavior of lysophosphatidylethanoamine dispersions. A thermodynamic and spectroscopic characterization
    • J.L. Slater, C.-H. Huang, R.G. Adams, and I.W. Levin Polymorphic phase behavior of lysophosphatidylethanoamine dispersions. A thermodynamic and spectroscopic characterization Biophys. J 56 1989 243 252
    • (1989) Biophys. J , vol.56 , pp. 243-252
    • Slater, J.L.1    Huang, C.-H.2    Adams, R.G.3    Levin, I.W.4
  • 51
    • 79952980526 scopus 로고    scopus 로고
    • Structures of beta-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: Mechanism of Gram selectivity obtained from solid-state Nuclear Magnetic Resonance
    • Y. Su, A.J. Waring, P. Ruchala, and M. Hong Structures of beta-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of Gram selectivity obtained from solid-state Nuclear Magnetic Resonance Biochemistry 50 2011 2072 2083
    • (2011) Biochemistry , vol.50 , pp. 2072-2083
    • Su, Y.1    Waring, A.J.2    Ruchala, P.3    Hong, M.4
  • 52
    • 0024653815 scopus 로고
    • Acrylamide quenching of tryptophan photochemistry and photophysics
    • D.H. Tallmadge, J.S. Huebner, and R.F. Borkman Acrylamide quenching of tryptophan photochemistry and photophysics Photochem. Photobiol. 49 1989 381 386
    • (1989) Photochem. Photobiol. , vol.49 , pp. 381-386
    • Tallmadge, D.H.1    Huebner, J.S.2    Borkman, R.F.3
  • 53
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptíde from solid-state NMR
    • M. Tang, A.J. Waring, and M. Hong Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptíde from solid-state NMR J. Am. Chem. Soc. 129 2007 11438 11446
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 54
    • 62949097134 scopus 로고    scopus 로고
    • Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy
    • M. Tang, and M. Hong Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy Mol. Biosyst. 5 2009 317 322
    • (2009) Mol. Biosyst. , vol.5 , pp. 317-322
    • Tang, M.1    Hong, M.2
  • 55
    • 32544456244 scopus 로고    scopus 로고
    • Antimicrobial peptides: New candidates in the fight against bacterial infections
    • O. Toke Antimicrobial peptides: new candidates in the fight against bacterial infections Biopolymers (Peptide Science) 80 2005 717 735
    • (2005) Biopolymers (Peptide Science) , vol.80 , pp. 717-735
    • Toke, O.1
  • 56
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • H.J. Vogel, D.J. Schibli, W.G. Jing, E.M. Lohmeier-Vogel, R.F. Epand, and R.M. Epand Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides Biochem. Cell Biol. 80 2002 49 63
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 49-63
    • Vogel, H.J.1    Schibli, D.J.2    Jing, W.G.3    Lohmeier-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 58
    • 0032539980 scopus 로고    scopus 로고
    • Magainin 2 amide interaction with lipid membranes: Calorimetric detection of peptide binding and pore formation
    • M.R. Wenk, and J. Seelig Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation Biochemistry 37 1998 3909 3916
    • (1998) Biochemistry , vol.37 , pp. 3909-3916
    • Wenk, M.R.1    Seelig, J.2
  • 60
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • W.C. Wimley, and S.H. White Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 3 1996 842 848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 63
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: Magainin and protegrin
    • L. Yang, T.M. Weiss, R.I. Leher, and H.W. Huang 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    Leher, R.I.3    Huang, H.W.4
  • 64
    • 0036389644 scopus 로고    scopus 로고
    • Conformational-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide
    • S.T. Yang, S.Y. Shin, Y.C. Kim, Y. Kim, K.S. Hahm, and J.I. Kim Conformational-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide Biochem. Biophys. Res. Commun. 296 2002 1044 1050
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1044-1050
    • Yang, S.T.1    Shin, S.Y.2    Kim, Y.C.3    Kim, Y.4    Hahm, K.S.5    Kim, J.I.6
  • 65
    • 0344838675 scopus 로고    scopus 로고
    • Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure
    • S.T. Yang, S.Y. Shin, C.W. Lee, Y.C. Kim, K.S. Hahm, and J.I. Kim Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure FEBS Lett. 540 2003 229 233
    • (2003) FEBS Lett. , vol.540 , pp. 229-233
    • Yang, S.T.1    Shin, S.Y.2    Lee, C.W.3    Kim, Y.C.4    Hahm, K.S.5    Kim, J.I.6
  • 66
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • W.-M. Yau, W.C. Wimley, K. Gawrisch, and S.H. White The preference of tryptophan for membrane interfaces Biochemistry 37 1998 14713 14718
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 67
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.