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Volumn 41, Issue 9, 2012, Pages 769-776

Effect of salt on the interaction of Hal18 with lipid membranes

Author keywords

A Helical; Antimicrobial peptide; Hydrophobic groove; Membrane interactive; Salt resistance

Indexed keywords

ANTIINFECTIVE AGENT; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLSERINE; HALOCIDIN; LIPOSOME; PEPTIDE; PHOSPHATIDYLSERINE; SODIUM CHLORIDE;

EID: 84866527609     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-012-0840-6     Document Type: Article
Times cited : (8)

References (28)
  • 1
    • 34047222991 scopus 로고    scopus 로고
    • Review Comparison of multidrug resistant efflux pumps of cancer and bacterial cells with respect to the same inhibitory agents
    • Amaral L, Engi H, Viveiros M, Molnar J (2007) Review Comparison of multidrug resistant efflux pumps of cancer and bacterial cells with respect to the same inhibitory agents In Vivo (Athens, Greece) 21:237-244
    • (2007) Vivo (Athens, Greece) , vol.21 , pp. 237-244
    • Amaral, L.1    Engi, H.2    Viveiros, M.3    Molnar, J.4
  • 2
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger B, Lohner K (2006) Detergent-like actions of linear amphipathic cationic antimicrobial peptides Biochim Biophys Acta 1758:1529-1539
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 3
    • 0016369116 scopus 로고
    • Monolayers-description of use and interaction
    • Demel RA (1974) Monolayers-description of use and interaction Methods Enzymol 32:539-544
    • (1974) Methods Enzymol , vol.32 , pp. 539-544
    • Demel, R.A.1
  • 4
    • 79952120584 scopus 로고    scopus 로고
    • Influence of c-terminal amidation on the efficacy of modelin-5
    • Dennison SR, Phoenix DA (2011) Influence of C-terminal amidation on the efficacy of modelin-5 Biochemistry 50:1514-1523
    • (2011) Biochemistry , vol.50 , pp. 1514-1523
    • Dennison, S.R.1    Phoenix, D.A.2
  • 5
    • 11244352103 scopus 로고    scopus 로고
    • Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?
    • Dennison SR, Harris F, Phoenix DA (2005) Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion? Protein Pept Lett 12:27-29
    • (2005) Protein Pept Lett , vol.12 , pp. 27-29
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 6
    • 55349119857 scopus 로고    scopus 로고
    • Investigations into the ability of the peptide, hal18, to interact with bacterial membranes
    • Dennison SR, Kim YS, Cha HJ, Phoenix DA (2008) Investigations into the ability of the peptide, HAL18, to interact with bacterial membranes Eur Biophys J 38:37-43
    • (2008) Eur Biophys J , vol.38 , pp. 37-43
    • Dennison, S.R.1    Kim, Y.S.2    Cha, H.J.3    Phoenix, D.A.4
  • 7
    • 73449105110 scopus 로고    scopus 로고
    • A study on the importance of phenylalanine for aurein functionality
    • Dennison SR, Harris F, Phoenix DA (2009) A study on the importance of phenylalanine for aurein functionality Protein Pept Lett 16:1455-1458
    • (2009) Protein Pept Lett , vol.16 , pp. 1455-1458
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 8
    • 58349116453 scopus 로고    scopus 로고
    • Cystic fibrosis and innate immunity: How chloride channel mutations provoke lung disease
    • Dooring G, Gulbins E (2009) Cystic fibrosis and innate immunity: how chloride channel mutations provoke lung disease Cell Microbiol 11:208-216
    • (2009) Cell Microbiol , vol.11 , pp. 208-216
    • Dooring, G.1    Gulbins, E.2
  • 10
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg D, Schwarz E, Komaromy M, Wall R (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot J Mol Biol 179:125-142
    • (1984) J Mol Biol , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 11
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman MJ, Anderson GM, Stolzenberg ED, Kari UP, Zasloff M, Wilson JM (1997) Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis Cell 88: 553-560
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 12
    • 33644543069 scopus 로고    scopus 로고
    • The forgotten gram-negative bacilli: What genetic determinants are telling us about the spread of antibiotic resistance
    • Gootz TD (2006) The forgotten Gram-negative bacilli: what genetic determinants are telling us about the spread of antibiotic resistance Biochem Pharmacol 71:1073-1084
    • (2006) Biochem Pharmacol , vol.71 , pp. 1073-1084
    • Gootz, T.D.1
  • 13
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure Nat Protoc 6:2876-2890
    • (2006) Nat Protoc , vol.6 , pp. 2876-2890
    • Greenfield, N.J.1
  • 14
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption
    • Hallock KJ, Lee DK, Omnaas J, Mosberg HI, Ramamoorthy I (2002) Membrane composition determines pardaxin's mechanism of lipid bilayer disruption Biophys J 83:1004-1013
    • (2002) Biophys J , vol.83 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, I.5
  • 15
    • 0034456592 scopus 로고    scopus 로고
    • Use of hydrophobic moment plot methodology to aid the identification of oblique orientated alpha-helices
    • Harris F, Wallace J, Phoenix DA (2000) Use of hydrophobic moment plot methodology to aid the identification of oblique orientated alpha-helices Mol Membr Biol 17:201-207
    • (2000) Mol Membr Biol , vol.17 , pp. 201-207
    • Harris, F.1    Wallace, J.2    Phoenix, D.A.3
  • 16
  • 17
    • 0037134853 scopus 로고    scopus 로고
    • Halocidin: A new antimicrobial peptide from hemocytes of the solitary tunicate, halocynthia aurantium
    • Jang WS, Kim KN, Lee YS, Nam MH, Lee IH (2002) Halocidin: a new antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium FEBS Lett 521:81-86
    • (2002) FEBS Lett , vol.521 , pp. 81-86
    • Jang, W.S.1    Kim, K.N.2    Lee, Y.S.3    Nam, M.H.4    Lee, I.H.5
  • 18
    • 0043270583 scopus 로고    scopus 로고
    • Biological activities of synthetic analogs of halocidin, an antimicrobial peptide from the tunicate halocynthia aurantium
    • Jang WS, Kim CH, Kim KN, Park SY, Lee JH, Son SM, Lee IH (2003) Biological activities of synthetic analogs of halocidin, an antimicrobial peptide from the tunicate Halocynthia aurantium Antimicrob Agents Chemother 47:2481-2486
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2481-2486
    • Jang, W.S.1    Kim, C.H.2    Kim, K.N.3    Park, S.Y.4    Lee, J.H.5    Son, S.M.6    Lee, I.H.7
  • 19
    • 9444251086 scopus 로고    scopus 로고
    • A new type of antimicrobial protein with multiple histidines from the hard tick, amblyomma hebraeum
    • Lai R, Takeuchi H, Lomas LO, Jonczy J, Rigden DJ, Rees HH, Turner PC (2004) A new type of antimicrobial protein with multiple histidines from the hard tick, Amblyomma hebraeum FASEB J 18:1447-1449
    • (2004) FASEB J , vol.18 , pp. 1447-1449
    • Lai, R.1    Takeuchi, H.2    Lomas, L.O.3    Jonczy, J.4    Rigden, D.J.5    Rees, H.H.6    Turner, P.C.7
  • 22
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen LT, Haney EF, Vogel HJ (2011) The expanding scope of antimicrobial peptide structures and their modes of action Trends Biotechnol 29:464-472
    • (2011) Trends Biotechnol , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.Z.2    Vogel, H.J.3
  • 23
    • 26044458858 scopus 로고    scopus 로고
    • Nosocomial infections due to multidrug-resistant pseudomonas aeruginosa: Epidemiology and treatment options
    • Obritsch MD, Fish DN, MacLaren R, Jung R (2005) Nosocomial infections due to multidrug-resistant Pseudomonas aeruginosa: epidemiology and treatment options Pharmacotherapy 25:1353-1364
    • (2005) Pharmacotherapy , vol.25 , pp. 1353-1364
    • Obritsch, M.D.1    Fish, D.N.2    MacLaren, R.3    Jung, R.4
  • 24
    • 1842639632 scopus 로고    scopus 로고
    • Helix stability confers salt resistance upon helical antimicrobial peptides
    • Park IY, Cho JH, Kim KS, Kim YB, Kim MS, Kim SC (2004) Helix stability confers salt resistance upon helical antimicrobial peptides J Biol Chem 279:13896-13901
    • (2004) J Biol Chem , vol.279 , pp. 13896-13901
    • Park, I.Y.1    Cho, J.H.2    Kim, K.S.3    Kim, Y.B.4    Kim, M.S.5    Kim, S.C.6
  • 25
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides
    • Sato H, Feix JB (2006) Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-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
  • 26
    • 14044268292 scopus 로고    scopus 로고
    • Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor
    • Wang G, Li Y, Li X (2005) Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor J Biol Chem 280:5803-5811
    • (2005) J Biol Chem , vol.280 , pp. 5803-5811
    • Wang, G.1    Li, Y.2    Li, X.3
  • 27
    • 77957766588 scopus 로고    scopus 로고
    • The protein circular dichroism data bank, a web-based site for access to circular dichroism spectroscopic data
    • Whitmore L, Woollett B, Miles AJ, Janes RW, Wallace BA (2010) The protein circular dichroism data bank, a web-based site for access to circular dichroism spectroscopic data Structure 18: 1267-1269
    • (2010) Structure , vol.18 , pp. 1267-1269
    • Whitmore, L.1    Woollett, B.2    Miles, A.J.3    Janes, R.W.4    Wallace, B.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.