메뉴 건너뛰기




Volumn 1808, Issue 1, 2011, Pages 171-182

A plausible mode of action of pseudin-2, an antimicrobial peptide from Pseudis paradoxa

Author keywords

Antimicrobial peptide; Depolarization; Giant unilamellar vesicle; Penetration; pseudin 2; RNA binding; Toroidal pore

Indexed keywords

LIPOPOLYSACCHARIDE; MONOMER; POLYPEPTIDE ANTIBIOTIC AGENT; PSEUDIN 2; RNA; UNCLASSIFIED DRUG;

EID: 78649774177     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.08.023     Document Type: Article
Times cited : (58)

References (51)
  • 1
    • 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
  • 2
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • M.R. Yeaman, and N.Y. Yount Mechanisms of antimicrobial peptide action and resistance Pharmacol. Rev. 55 2003 27 55
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 2005 238 250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 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
    • Y. Shai 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
  • 5
    • 33748919831 scopus 로고    scopus 로고
    • Membrane interactions of antimicrobial peptides from Australian tree frogs
    • M.P. Boland, and F. Separovic Membrane interactions of antimicrobial peptides from Australian tree frogs Biochim. Biophys. Acta 1758 2006 1178 1183
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1178-1183
    • Boland, M.P.1    Separovic, F.2
  • 6
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • J.D. Hale, and R.E. Hancock Alternative mechanisms of action of cationic antimicrobial peptides on bacteria Expert Rev. Anti Infect. Ther. 5 2007 951 959
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 7
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: An expanding scenario
    • A.C. Rinaldi Antimicrobial peptides from amphibian skin: an expanding scenario Curr. Opin. Chem. Biol. 6 2002 799 804
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 799-804
    • Rinaldi, A.C.1
  • 8
    • 0035834573 scopus 로고    scopus 로고
    • Pseudin-2: An antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog
    • L. Olson, A. Soto, F.C. Knoop, and J.M. Conlon Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog Biochem. Biophys. Res. Commun. 288 2001 1001 1005
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1001-1005
    • Olson, L.1    Soto, A.2    Knoop, F.C.3    Conlon, J.M.4
  • 9
    • 38649103176 scopus 로고    scopus 로고
    • Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue
    • Y.H. Abdel-Wahab, G.J. Power, M.T. Ng, P.R. Flatt, and J.M. Conlon Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue Biol. Chem. 389 2008 143 148
    • (2008) Biol. Chem. , vol.389 , pp. 143-148
    • Abdel-Wahab, Y.H.1    Power, G.J.2    Ng, M.T.3    Flatt, P.R.4    Conlon, J.M.5
  • 10
    • 0031465747 scopus 로고    scopus 로고
    • Selective sytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis
    • J.K. Ghosh, D. Shaool, P. Guillaud, L. Ciceron, D. Mazier, I. Kustanovich, Y. Shai, and A. Mor Selective sytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis J. Biol. Chem. 272 1997 31609 31616
    • (1997) J. Biol. Chem. , vol.272 , pp. 31609-31616
    • Ghosh, J.K.1    Shaool, D.2    Guillaud, P.3    Ciceron, L.4    Mazier, D.5    Kustanovich, I.6    Shai, Y.7    Mor, A.8
  • 11
    • 0026758174 scopus 로고
    • Aggregation and organization of pardaxin in phospholipid membranes
    • D. Rapaport, and Y. Shai Aggregation and organization of pardaxin in phospholipid membranes J. Biol. Chem. 267 1992 6502 6509
    • (1992) J. Biol. Chem. , vol.267 , pp. 6502-6509
    • Rapaport, D.1    Shai, Y.2
  • 12
    • 38149030149 scopus 로고    scopus 로고
    • Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: Pore formation mechanism in various lipid compositions
    • S.C. Park, M.H. Kim, M.A. Hossain, S.Y. Shin, Y. Kim, L. Stella, J.D. Wade, Y. Park, and K.S. Hahm Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions Biochim. Biophys. Acta 1778 2008 229 241
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 229-241
    • Park, S.C.1    Kim, M.H.2    Hossain, M.A.3    Shin, S.Y.4    Kim, Y.5    Stella, L.6    Wade, J.D.7    Park, Y.8    Hahm, K.S.9
  • 13
    • 34548446295 scopus 로고    scopus 로고
    • Characterization of a heat-stable protein with antimicrobial activity from Arabidopsis thaliana
    • S.C. Park, J.R. Lee, S.O. Shin, Y. Park, S.Y. Lee, and K.S. Hahm Characterization of a heat-stable protein with antimicrobial activity from Arabidopsis thaliana Biochem. Biophys. Res. Commun. 362 2007 562 567
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 562-567
    • Park, S.C.1    Lee, J.R.2    Shin, S.O.3    Park, Y.4    Lee, S.Y.5    Hahm, K.S.6
  • 14
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Y.H. Chen, J.T. Yang, and K.H. Chau Determination of the helix and beta form of proteins in aqueous solution by circular dichroism Biochemistry 13 1974 3350 3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 15
    • 37849047198 scopus 로고    scopus 로고
    • Antimicrobial activity and protease stability of peptides containing fluorinated amino acids
    • H. Meng, and K. Kumar Antimicrobial activity and protease stability of peptides containing fluorinated amino acids J. Am. Chem. Soc. 129 2007 15615 15622
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15615-15622
    • Meng, H.1    Kumar, K.2
  • 16
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Z. Oren, J.C. Lerman, G.H. Gudmundsson, B. Agerberth, and Y. Shai Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity Biochem. J. 341 1999 501 513
    • (1999) Biochem. J. , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 17
    • 0037072808 scopus 로고    scopus 로고
    • The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers
    • N. Papo, Z. Oren, U. Pag, H.G. Sahl, and Y. Shai The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers J. Biol. Chem. 277 2002 33913 33921
    • (2002) J. Biol. Chem. , vol.277 , pp. 33913-33921
    • Papo, N.1    Oren, Z.2    Pag, U.3    Sahl, H.G.4    Shai, Y.5
  • 18
    • 3042743487 scopus 로고    scopus 로고
    • Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli
    • M.L. Mangoni, N. Papo, D. Barra, M. Simmaco, A. Bozzi, A. Di Giulio, and A.C. Rinaldi Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli Biochem. J. 380 2004 2004 859 865
    • (2004) Biochem. J. , vol.380 , Issue.2004 , pp. 859-865
    • Mangoni, M.L.1    Papo, N.2    Barra, D.3    Simmaco, M.4    Bozzi, A.5    Di Giulio, A.6    Rinaldi, A.C.7
  • 19
    • 33846397753 scopus 로고    scopus 로고
    • In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin S4 derivatives
    • K. Marynka, S. Rotem, I. Portnaya, U. Cogan, and A. Mor In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin S4 derivatives Chem. Biol. 14 2007 75 85
    • (2007) Chem. Biol. , vol.14 , pp. 75-85
    • Marynka, K.1    Rotem, S.2    Portnaya, I.3    Cogan, U.4    Mor, A.5
  • 21
    • 33749376461 scopus 로고    scopus 로고
    • A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer
    • Y. Rosenfeld, D. Barra, M. Simmaco, Y. Shai, and M.L. Mangoni A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer J. Biol. Chem. 281 2006 28565 28574
    • (2006) J. Biol. Chem. , vol.281 , pp. 28565-28574
    • Rosenfeld, Y.1    Barra, D.2    Simmaco, M.3    Shai, Y.4    Mangoni, M.L.5
  • 23
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin
    • N. Asthana, S.P. Yadav, and J.K. Ghosh Dissection of antibacterial and toxic activity of melittin J. Biol. Chem. 279 2004 55042 55050
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 26
    • 17044400144 scopus 로고    scopus 로고
    • Electroformation of giant liposomes from spin-coated films of lipids
    • D.J. Estes, and M. Mayer Electroformation of giant liposomes from spin-coated films of lipids Colloids Surf. B Biointerfaces 42 2005 115 123
    • (2005) Colloids Surf. B Biointerfaces , vol.42 , pp. 115-123
    • Estes, D.J.1    Mayer, M.2
  • 27
    • 58749085926 scopus 로고    scopus 로고
    • Magainin 2 in action: Distinct modes of membrane permeabilization in living bacterial and mammalian cells
    • Y. Imura, N. Choda, and K. Matsuzaki Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells Biophys. J. 95 2008 5757 5765
    • (2008) Biophys. J. , vol.95 , pp. 5757-5765
    • Imura, Y.1    Choda, N.2    Matsuzaki, K.3
  • 29
    • 0019304939 scopus 로고
    • Colorimetric determination of phospholipids with ammonium ferrothiocyanate
    • J.C.M. Stewart, Colorimetric determination of phospholipids with ammonium ferrothiocyanate, Anal. Biochem. 104 (1080) 10-14.
    • (1080) Anal. Biochem. , vol.104 , pp. 10-14
    • Stewart, J.C.M.1
  • 30
    • 23044452974 scopus 로고    scopus 로고
    • Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: Evidence for multiple conformations involved in binding to membranes and DNA
    • C.H. Hsu, C. Chen, M.L. Jou, A.Y.L. Lee, Y.C. Lin, Y.P. Yu, W.T. Huang, and S.H. Wu Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA Nucleic Acids Res. 33 2005 4053 4064
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4053-4064
    • Hsu, C.H.1    Chen, C.2    Jou, M.L.3    Lee, A.Y.L.4    Lin, Y.C.5    Yu, Y.P.6    Huang, W.T.7    Wu, S.H.8
  • 31
    • 20144376875 scopus 로고    scopus 로고
    • Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2
    • T. Pál, A. Sonnevend, S. Galadari, and J.M. Conlon Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2 Regul. Pept. 129 2005 85 91
    • (2005) Regul. Pept. , vol.129 , pp. 85-91
    • Pál, T.1    Sonnevend, A.2    Galadari, S.3    Conlon, J.M.4
  • 32
    • 54849407971 scopus 로고    scopus 로고
    • Bacterial membranes as predictors of antimicrobial potency
    • R.M. Epand, S. Rotem, A. Mor, B. Berno, and R.F. Epand Bacterial membranes as predictors of antimicrobial potency J. Am. Chem. Soc. 130 2008 14346 14352
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14346-14352
    • Epand, R.M.1    Rotem, S.2    Mor, A.3    Berno, B.4    Epand, R.F.5
  • 33
    • 35048882380 scopus 로고    scopus 로고
    • Synthetic antimicrobial oligomers induce a composition-dependent topological transition in membranes
    • L. Yang, V.D. Gordon, A. Mishra, A. Som, K.R. Purdy, M.A. Davis, G.N. Tew, and G.C. Wong Synthetic antimicrobial oligomers induce a composition-dependent topological transition in membranes J. Am. Chem. Soc. 129 2007 12141 12147
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12141-12147
    • Yang, L.1    Gordon, V.D.2    Mishra, A.3    Som, A.4    Purdy, K.R.5    Davis, M.A.6    Tew, G.N.7    Wong, G.C.8
  • 34
    • 33748929313 scopus 로고    scopus 로고
    • Role of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides
    • R.F. Epand, M.A. Schmitt, S.H. Gellman, and R.M. Epand Role of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1343 1350
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1343-1350
    • Epand, R.F.1    Schmitt, M.A.2    Gellman, S.H.3    Epand, R.M.4
  • 35
    • 0031017699 scopus 로고    scopus 로고
    • Main chain and side chain dynamics of peptides in liquid solution from 13C NMR: Melittin as a model peptide
    • M.D. Kemple, P. Buckley, P. Yuan, and F.G. Prendergast Main chain and side chain dynamics of peptides in liquid solution from 13C NMR: melittin as a model peptide Biochemistry 36 1997 1678 1688
    • (1997) Biochemistry , vol.36 , pp. 1678-1688
    • Kemple, M.D.1    Buckley, P.2    Yuan, P.3    Prendergast, F.G.4
  • 36
    • 0032532218 scopus 로고    scopus 로고
    • The structure of the melittin tetramer at different temperatures: An NOE-based calculation with chemical shift refinement
    • M. Iwadate, T. Asakura, and M.P. Williamson The structure of the melittin tetramer at different temperatures: an NOE-based calculation with chemical shift refinement Eur. J. Biochem. 257 1998 479 487
    • (1998) Eur. J. Biochem. , vol.257 , pp. 479-487
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 37
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • S. Frey, and L.K. Tamm Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study Biophys. J. 60 1991 922 930
    • (1991) Biophys. J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 38
    • 0031465747 scopus 로고    scopus 로고
    • Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis
    • J.K. Ghosh, D. Shaool, P. Guillaud, L. Ciceron, D. Mazier, I. Kustanovich, Y. Shai, and A. Mor Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis J. Biol. Chem. 272 1997 31609 31616
    • (1997) J. Biol. Chem. , vol.272 , pp. 31609-31616
    • Ghosh, J.K.1    Shaool, D.2    Guillaud, P.3    Ciceron, L.4    Mazier, D.5    Kustanovich, I.6    Shai, Y.7    Mor, A.8
  • 40
    • 0029824838 scopus 로고    scopus 로고
    • Antiendotoxin activity of cationic peptide antimicrobial agents
    • M. Gough, R.E. Hancock, and N.M. Kelly Antiendotoxin activity of cationic peptide antimicrobial agents Infect. Immun. 64 1996 4922 4927
    • (1996) Infect. Immun. , vol.64 , pp. 4922-4927
    • Gough, M.1    Hancock, R.E.2    Kelly, N.M.3
  • 41
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • R.E. Hancock, and M.G. Scott The role of antimicrobial peptides in animal defenses Proc. Natl. Acad. Sci. USA 97 2000 8856 8861
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 42
    • 9644252819 scopus 로고    scopus 로고
    • Perturbation of lipopolysaccharide (LPS) micelles by Sushi 3 (S3) antimicrobial peptide
    • P. Li, T. Wohland, B. Ho, and J.L. Ding Perturbation of lipopolysaccharide (LPS) micelles by Sushi 3 (S3) antimicrobial peptide J. Biol. Chem. 279 2004 50150 50156
    • (2004) J. Biol. Chem. , vol.279 , pp. 50150-50156
    • Li, P.1    Wohland, T.2    Ho, B.3    Ding, J.L.4
  • 43
    • 15444370838 scopus 로고    scopus 로고
    • A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides
    • N. Papo, and Y. Shai A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides J. Biol. Chem. 280 2005 10378 10387
    • (2005) J. Biol. Chem. , vol.280 , pp. 10378-10387
    • Papo, N.1    Shai, Y.2
  • 44
    • 0031740520 scopus 로고    scopus 로고
    • Magainin as paradigm for the mode of action of pore forming polypeptides
    • K. Matsuzaki Magainin as paradigm for the mode of action of pore forming polypeptides Biochim. Biophys. Acta 1376 1998 391 400
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 45
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • T.J. Falla, D.N. Karunaratne, and R.E. Hancock Mode of action of the antimicrobial peptide indolicidin J. Biol. Chem. 271 1996 19298 19303
    • (1996) J. Biol. Chem. , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.3
  • 48
    • 33750446295 scopus 로고    scopus 로고
    • Ultrashort antibacterial and antifungal lipopeptides
    • A. Makovitzki, D. Avrahami, and Y. Shai Ultrashort antibacterial and antifungal lipopeptides Proc. Natl. Acad. Sci. USA 103 2006 15997 16002
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15997-16002
    • Makovitzki, A.1    Avrahami, D.2    Shai, Y.3
  • 50
    • 34447252557 scopus 로고    scopus 로고
    • The lipid dependence of melittin action investigated by dual-color fluorescence burst analysis
    • G. van den Bogaart, J.T. Mika, V. Krasnikov, and B. Poolman The lipid dependence of melittin action investigated by dual-color fluorescence burst analysis Biophys. J. 93 2007 154 163
    • (2007) Biophys. J. , vol.93 , pp. 154-163
    • Van Den Bogaart, G.1    Mika, J.T.2    Krasnikov, V.3    Poolman, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.