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Volumn 1840, Issue 10, 2014, Pages 3006-3016

Cysteine deleted protegrin-1 (CDP-1): Anti-bacterial activity, outer-membrane disruption and selectivity

Author keywords

Antibiotics; Antimicrobial peptides; Lipopolysaccharide; NMR; Protegrin 1

Indexed keywords

ANTIBIOTICS; ANTIMICROBIAL PEPTIDES; LIPOPOLYSACCHARIDE; NMR; PROTEGRIN-1;

EID: 84905843048     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.06.018     Document Type: Article
Times cited : (34)

References (64)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 2005 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 3
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: General overview and clinical implications in human health and disease
    • E. Guani-Guerra, T. Santos-Mendoza, S.O. Lugo-Reyes, and L.M. Teran Antimicrobial peptides: general overview and clinical implications in human health and disease Clin. Immunol. 135 2010 1 11
    • (2010) Clin. Immunol. , vol.135 , pp. 1-11
    • Guani-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Teran, L.M.4
  • 6
    • 84877318780 scopus 로고    scopus 로고
    • Antimicrobial peptides stage a comeback
    • J.L. Fox Antimicrobial peptides stage a comeback Nat. Biotechnol. 31 2013 379 382
    • (2013) Nat. Biotechnol. , vol.31 , pp. 379-382
    • Fox, J.L.1
  • 7
    • 84878419915 scopus 로고    scopus 로고
    • Database guided discovery of potent peptides to combat HIV-1 or superbugs
    • G. Wang Database guided discovery of potent peptides to combat HIV-1 or superbugs Pharmaceuticals 6 2013 728 758
    • (2013) Pharmaceuticals , vol.6 , pp. 728-758
    • Wang, G.1
  • 9
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • L.T. Nguyen, E.F. Haney, and H.J. Vogel The expanding scope of antimicrobial peptide structures and their modes of action Trends Biotechnol. 29 2011 464 472
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 10
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • DOI 10.1002/bip.10260
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248 (Pubitemid 36098316)
    • (2002) Biopolymers - Peptide Science Section , vol.66 , Issue.4 , pp. 236-248
    • Shai, Y.1
  • 11
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • W.C. Wimley Describing the mechanism of antimicrobial peptide action with the interfacial activity model ACS Chem. Biol. 5 2010 905 917
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 12
    • 0034718563 scopus 로고    scopus 로고
    • The lipopolysaccharide barrier: Correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics
    • D.S. Snyder, and T.J. McIntosh The lipopolysaccharide barrier: correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics Biochemistry 39 2000 11777 11787
    • (2000) Biochemistry , vol.39 , pp. 11777-11787
    • Snyder, D.S.1    McIntosh, T.J.2
  • 13
    • 70350450689 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Functional and mechanistic insights from NMR structures of potent antimicrobial peptides
    • S. Bhattacharjya, and A. Ramamoorthy Multifunctional host defense peptides: functional and mechanistic insights from NMR structures of potent antimicrobial peptides FEBS J. 276 2009 6465 6473
    • (2009) FEBS J. , vol.276 , pp. 6465-6473
    • Bhattacharjya, S.1    Ramamoorthy, A.2
  • 14
    • 0142031491 scopus 로고    scopus 로고
    • Interaction of Antimicrobial Peptides with Lipopolysaccharides
    • DOI 10.1021/bi035130+
    • L. Ding, L. Yang, T.M. Weiss, A.J. Waring, R.I. Lehrer, and H.W. Huang Interaction of antimicrobial peptides with lipopolysaccharides Biochemistry 42 2003 12251 12259 (Pubitemid 37296502)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12251-12259
    • Ding, L.1    Yang, L.2    Weiss, T.M.3    Waring, A.J.4    Lehrer, R.I.5    Huang, H.W.6
  • 15
    • 15444370838 scopus 로고    scopus 로고
    • A molecular mechanism for lipopolysaccharide protection of gram-negative bacteria from antimicrobial peptides
    • DOI 10.1074/jbc.M412865200
    • 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 (Pubitemid 40395894)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10378-10387
    • Papo, N.1    Shai, Y.2
  • 16
    • 33749376461 scopus 로고    scopus 로고
    • A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer
    • DOI 10.1074/jbc.M606031200
    • 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 (Pubitemid 44506999)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28565-28574
    • Rosenfeld, Y.1    Barra, D.2    Simmaco, M.3    Shai, Y.4    Mangoni, M.L.5
  • 17
    • 84883622438 scopus 로고    scopus 로고
    • NMR structure of temporin-1 Ta in lipopolysaccharide micelles: Mechanistic insight into inactivation by outer membrane
    • R. Saravanan, M. Joshi, H. Mohanram, A. Bhunia, M.L. Mangoni, and S. Bhattacharjya NMR structure of temporin-1 Ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane PLoS ONE 8 2013 e72718
    • (2013) PLoS ONE , vol.8 , pp. 72718
    • Saravanan, R.1    Joshi, M.2    Mohanram, H.3    Bhunia, A.4    Mangoni, M.L.5    Bhattacharjya, S.6
  • 19
    • 0037180768 scopus 로고    scopus 로고
    • The immunopathogenesis of sepsis
    • DOI 10.1038/nature01326
    • J. Cohen The immunopathogenesis of sepsis Nature 420 2002 885 891 (Pubitemid 36019643)
    • (2002) Nature , vol.420 , Issue.6917 , pp. 885-891
    • Cohen, J.1
  • 20
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • DOI 10.1056/NEJMoa022139
    • G.S. Martin, D.M. Mannino, S. Eaton, and M. Moss The epidemiology of sepsis in the United States from 1979 through 2000 N. Engl. J. Med. 348 2003 1546 1554 (Pubitemid 36437931)
    • (2003) New England Journal of Medicine , vol.348 , Issue.16 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 21
    • 77955600292 scopus 로고    scopus 로고
    • De novo designed lipopolysaccharide binding peptides: Structure based development of antiendotoxic and antimicrobial drugs
    • S. Bhattacharjya De novo designed lipopolysaccharide binding peptides: structure based development of antiendotoxic and antimicrobial drugs Curr. Med. Chem. 17 2010 3080 3093
    • (2010) Curr. Med. Chem. , vol.17 , pp. 3080-3093
    • Bhattacharjya, S.1
  • 22
    • 84872856945 scopus 로고    scopus 로고
    • Peptide antimicrobials: Cell wall as a bacterial target
    • N.Y. Yount, and M.R. Yeaman Peptide antimicrobials: cell wall as a bacterial target Ann. N. Y. Acad. Sci. 1277 2013 127 138
    • (2013) Ann. N. Y. Acad. Sci. , vol.1277 , pp. 127-138
    • Yount, N.Y.1    Yeaman, M.R.2
  • 23
    • 0034650823 scopus 로고    scopus 로고
    • Cutting edge: Cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein
    • M.G. Scott, A.C. Vreugdenhil, W.A. Buurman, R.E. Hancock, and M.R. Gold Cutting edge: cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein J. Immunol. 164 2000 549 553 (Pubitemid 30043670)
    • (2000) Journal of Immunology , vol.164 , Issue.2 , pp. 549-553
    • Scott, M.G.1    Vreugdenhil, A.C.E.2    Buurman, W.A.3    Hancock, R.E.W.4    Gold, M.R.5
  • 25
    • 84875974241 scopus 로고    scopus 로고
    • Bacterial membrane disrupting dodecapeptide SC4 improves survival of mice challenged with Pseudomonas aeruginosa
    • R. Dings, J.R. Haseman, D.B. Leslie, M. Luong, D.L. Dunn, and K.H. Mayo Bacterial membrane disrupting dodecapeptide SC4 improves survival of mice challenged with Pseudomonas aeruginosa Biochim. Biophys. Acta 1830 2013 3454 3457
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3454-3457
    • Dings, R.1    Haseman, J.R.2    Leslie, D.B.3    Luong, M.4    Dunn, D.L.5    Mayo, K.H.6
  • 26
    • 79959903251 scopus 로고    scopus 로고
    • NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: Mechanistic insights into outer membrane permeabilization and synergistic activity
    • A. Bhunia, R. Saravanan, H. Mohanram, M.L. Mangoni, and S. Bhattacharjya NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity J. Biol. Chem. 286 2011 24394 24406
    • (2011) J. Biol. Chem. , vol.286 , pp. 24394-24406
    • Bhunia, A.1    Saravanan, R.2    Mohanram, H.3    Mangoni, M.L.4    Bhattacharjya, S.5
  • 27
    • 20444505207 scopus 로고    scopus 로고
    • Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide
    • DOI 10.1074/jbc.M500266200
    • B. Japelj, P. Pristovsek, A. Majerle, and R. Jerala Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide J. Biol. Chem. 280 2005 16955 16961 (Pubitemid 41389156)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16955-16961
    • Japelj, B.1    Pristovsek, P.2    Majerle, A.3    Jerala, R.4
  • 28
    • 60749118629 scopus 로고    scopus 로고
    • Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy
    • A. Bhunia, A. Ramamoorthy, and S. Bhattacharjya Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy Chemistry 15 2009 2036 2040
    • (2009) Chemistry , vol.15 , pp. 2036-2040
    • Bhunia, A.1    Ramamoorthy, A.2    Bhattacharjya, S.3
  • 29
    • 78650599747 scopus 로고    scopus 로고
    • Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: Role of the helical hairpin conformation in outer-membrane permeabilization
    • P.N. Domadia, A. Bhunia, A. Ramamoorthy, and S. Bhattacharjya Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: role of the helical hairpin conformation in outer-membrane permeabilization J. Am. Chem. Soc. 132 2010 18417 18428
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 18417-18428
    • Domadia, P.N.1    Bhunia, A.2    Ramamoorthy, A.3    Bhattacharjya, S.4
  • 30
    • 34248995513 scopus 로고    scopus 로고
    • High-resolution solution structure of a designed peptide bound to lipopolysaccharide: Transferred nuclear overhauser effects, micelle selectivity, and anti-endotoxic activity
    • DOI 10.1021/bi6025159
    • S. Bhattacharjya, P. Domadia, A. Bhunia, S. Malladi, and S. David High resolution solution structure of a designed peptide bound to lipopolysaccharide: transferred nuclear Overhauser effects, micelle selectivity and anti-endotoxic activity Biochemistry 46 2007 5864 5874 (Pubitemid 46799149)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 5864-5874
    • Bhattacharjya, S.1    Domadia, P.N.2    Bhunia, A.3    Malladi, S.4    David, S.A.5
  • 36
    • 11144242839 scopus 로고    scopus 로고
    • Protegrin structure-activity relationships: Using homology models of synthetic sequences to determine structural characteristics important for activity
    • DOI 10.1016/j.peptides.2004.09.020, PII S0196978104004437
    • N. Ostberg, and Y. Kaznessis Protegrin structure-activity relationships: using homology models of synthetic sequences to determine structural characteristics important for activity Peptides 26 2005 197 206 (Pubitemid 40051415)
    • (2005) Peptides , vol.26 , Issue.2 , pp. 197-206
    • Ostberg, N.1    Kaznessis, Y.2
  • 37
    • 50849120027 scopus 로고    scopus 로고
    • Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1
    • L.M. Gottler, R. Salud Bea, C.E. Shelburne, A. Ramamoorthy, and E.N. Marsh Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1 Biochemistry 47 2008 9243 9250
    • (2008) Biochemistry , vol.47 , pp. 9243-9250
    • Gottler, L.M.1    Salud Bea, R.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.5
  • 38
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • DOI 10.1016/S1074-5521(96)90145-3
    • R.L. Fahrner, T. Dieckmann, S.S.L. Harwig, R.I. Lehrer, D. Eisenberg, and J. Feigon Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes Chem. Biol. 3 1996 543 550 (Pubitemid 26324167)
    • (1996) Chemistry and Biology , vol.3 , Issue.7 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.L.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 41
    • 0032536098 scopus 로고    scopus 로고
    • Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study
    • DOI 10.1016/S0014-5793(97)01579-2, PII S0014579397015792
    • C. Roumestand, V. Louis, A. Aumelas, G. Grassy, B. Calas, and A. Chavanieu Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study FEBS Lett. 421 1999 263 267 (Pubitemid 28045767)
    • (1998) FEBS Letters , vol.421 , Issue.3 , pp. 263-267
    • Roumestand, C.1    Louis, V.2    Aumelas, A.3    Grassy, G.4    Calas, B.5    Chavanieu, A.6
  • 42
    • 41549125949 scopus 로고    scopus 로고
    • On the nature of antimicrobial activity: A model for protegrin-1 pores
    • A.A. Langham, A.S. Ahmad, and Y.N. Kaznessis On the nature of antimicrobial activity: a model for protegrin-1 pores J. Am. Chem. Soc. 130 2008 338 346
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 338-346
    • Langham, A.A.1    Ahmad, A.S.2    Kaznessis, Y.N.3
  • 43
    • 84873328552 scopus 로고    scopus 로고
    • Membrane interactions and pore formation by the antimicrobial peptide protegrin
    • T. Lazaridis, Y. He, and L. Prieto Membrane interactions and pore formation by the antimicrobial peptide protegrin Biophys. J. 104 2013 633 642
    • (2013) Biophys. J. , vol.104 , pp. 633-642
    • Lazaridis, T.1    He, Y.2    Prieto, L.3
  • 44
    • 0029831079 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations
    • S.S. Harwig, A. Waring, H.J. Yang, Y. Cho, L. Tan, and R.I. Lehrer Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations Eur. J. Biochem. 240 1996 352 357 (Pubitemid 26292741)
    • (1996) European Journal of Biochemistry , vol.240 , Issue.2 , pp. 352-357
    • Harwig, S.S.L.1
  • 46
    • 0034113230 scopus 로고    scopus 로고
    • Membranolytic selectivity of cystine-stabilized cyclic protegrins
    • DOI 10.1046/j.1432-1327.2000.01359.x
    • J.P. Tam, C. Wu, and J.L. Yang Membranolytic selectivity of cystine-stabilized cyclic protegrins Eur. J. Biochem. 267 2000 3289 3300 (Pubitemid 30341157)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.11 , pp. 3289-3300
    • Tam, J.P.1    Wu, C.2    Yang, J.-L.3
  • 47
    • 0037159195 scopus 로고    scopus 로고
    • Design of non-cysteine-containing antimicrobial β-hairpins: Structure-activity relationship studies with linear protegrin-1 analogues
    • DOI 10.1021/bi026127d
    • J.R. Lai, B.R. Huck, B. Weisblum, and S.H. Gellman Design of non-cysteine-containing antimicrobial beta-hairpins: structure-activity relationship studies with linear protegrin-1 analogues Biochemistry 41 2002 12835 12842 (Pubitemid 35192512)
    • (2002) Biochemistry , vol.41 , Issue.42 , pp. 12835-12842
    • Lai, J.R.1    Huck, B.R.2    Weisblum, B.3    Gellman, S.H.4
  • 48
    • 33845945985 scopus 로고    scopus 로고
    • Roles of salt and conformation in the biological and physicochemical behavior of protegrin-1 and designed analogues: Correlation of antimicrobial, hemolytic, and lipid bilayer-perturbing activities
    • DOI 10.1021/bi0617759
    • J.R. Lai, R.F. Epand, B. Weisblum, R.M. Epand, and S.H. Gellman Roles of salt and conformation in the biological and physicochemical behavior of protegrin-1 and designed analogues: correlation of antimicrobial, hemolytic, and lipid bilayer-perturbing activities Biochemistry 45 2006 15718 15730 (Pubitemid 46032492)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15718-15730
    • Lai, J.R.1    Epand, R.F.2    Weisblum, B.3    Epand, R.M.4    Gellman, S.H.5
  • 49
    • 33646891071 scopus 로고    scopus 로고
    • Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding
    • DOI 10.1021/bi052629q
    • A. Ramamoorthy, S. Thennarasu, A. Tan, K. Gottipati, S. Sreekumar, D.L. Heyl, F.Y. An, and C.E. Shelburne Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding Biochemistry 45 2006 6529 6540 (Pubitemid 43787817)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6529-6540
    • Ramamoorthy, A.1    Thennarasu, S.2    Tan, A.3    Gottipati, K.4    Sreekumar, S.5    Heyl, D.L.6    An, F.Y.P.7    Shelburne, C.E.8
  • 50
    • 84859912597 scopus 로고    scopus 로고
    • Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization
    • R. Saravanan, H. Mohanram, M. Joshi, P.N. Domadia, J. Torres, C. Ruedl, and S. Bhattacharjya Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: mechanistic insights into outer-membrane permeabilization and endotoxin neutralization Biochim. Biophys. Acta 1818 2012 1613 1624
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1613-1624
    • Saravanan, R.1    Mohanram, H.2    Joshi, M.3    Domadia, P.N.4    Torres, J.5    Ruedl, C.6    Bhattacharjya, S.7
  • 51
    • 0032501406 scopus 로고    scopus 로고
    • Critical aggregation concentrations of gram-negative bacterial lipopolysaccharides (LPS)
    • DOI 10.1006/bbrc.1998.9773
    • C.A. Aurell, and A.O. Wistrom Critical aggregation concentrations of gram-negative bacterial lipopolysaccharides (LPS) Biochem. Biophys. Res. Commun. 253 1998 119 123 (Pubitemid 29015610)
    • (1998) Biochemical and Biophysical Research Communications , vol.253 , Issue.1 , pp. 119-123
    • Aurell, C.A.1    Wistrom, A.O.2
  • 52
    • 29944441136 scopus 로고    scopus 로고
    • Determination of critical micelle concentrations and aggregation numbers by fluorescence correlation spectroscopy: Aggregation of a lipopolysaccharide
    • DOI 10.1016/j.aca.2005.09.008, PII S0003267005015382, Young Analytical Faculty in Asia
    • L. Yu, M. Tan, B. Hob, J.L. Ding, and T. Wohland Determination of critical micelle concentrations and aggregation numbers by fluorescence correlation spectroscopy: aggregation of a lipopolysaccharide Anal. Chim. Acta. 556 2006 216 225 (Pubitemid 43042597)
    • (2006) Analytica Chimica Acta , vol.556 , Issue.1 , pp. 216-225
    • Yu, L.1    Tan, M.2    Ho, B.3    Ding, J.L.4    Wohland, T.5
  • 53
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR protein structure calculation with CYANA
    • P. Guntert Automated NMR protein structure calculation with CYANA Methods Mol. Biol. 278 2004 353 378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 55
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides: Peptide properties and plausible mode of action
    • Y. Rosenfeld, N. Papo, and Y. Shai Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides: peptide properties and plausible mode of action J. Biol. Chem. 281 2006 1636 1643
    • (2006) J. Biol. Chem. , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 56
    • 0028924539 scopus 로고
    • Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD4
    • P.S. Tobias, K. Soldau, J.A. Gegner, D. Mintz, and R.J. Ulevitch Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD4 J. Biol. Chem. 270 1995 10482 10488
    • (1995) J. Biol. Chem. , vol.270 , pp. 10482-10488
    • Tobias, P.S.1    Soldau, K.2    Gegner, J.A.3    Mintz, D.4    Ulevitch, R.J.5
  • 58
    • 0029870193 scopus 로고    scopus 로고
    • Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A
    • S. Srimal, N. Surolia, S. Balasubramanian, and A. Surolia Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A Biochem. J. 315 1996 679 686
    • (1996) Biochem. J. , vol.315 , pp. 679-686
    • Srimal, S.1    Surolia, N.2    Balasubramanian, S.3    Surolia, A.4
  • 59
    • 36849010657 scopus 로고    scopus 로고
    • Structural and thermodynamic analyses of the interaction between melittin and lipopolysaccharide
    • DOI 10.1016/j.bbamem.2007.07.017, PII S0005273607002817
    • A. Bhunia, P.N. Domadia, and S. Bhattacharjya Structural and thermodynamic analyses of the interaction between melittin and lipopolysaccharide Biochim. Biophys. Acta 1768 2007 3282 3291 (Pubitemid 350236077)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.12 , pp. 3282-3291
    • Bhunia, A.1    Domadia, P.N.2    Bhattacharjya, S.3
  • 60
    • 77950515754 scopus 로고    scopus 로고
    • NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: Mechanism of outer membrane permeabilization
    • A. Bhunia, P. Domadia, J. Torres, K.J. Hallock, A. Ramamoorthy, and S. Bhattacharjya NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization J. Biol. Chem. 285 2010 3883 3895
    • (2010) J. Biol. Chem. , vol.285 , pp. 3883-3895
    • Bhunia, A.1    Domadia, P.2    Torres, J.3    Hallock, K.J.4    Ramamoorthy, A.5    Bhattacharjya, S.6
  • 61
    • 69249119005 scopus 로고    scopus 로고
    • Designed beta-boomerang antiendotoxic and antimicrobial peptides: Structures and activities in lipopolysaccharide
    • A. Bhunia, H. Mohanram, P.N. Domadia, J. Torres, and S. Bhattacharjya Designed beta-boomerang antiendotoxic and antimicrobial peptides: structures and activities in lipopolysaccharide J. Biol. Chem. 284 2009 21991 22004
    • (2009) J. Biol. Chem. , vol.284 , pp. 21991-22004
    • Bhunia, A.1    Mohanram, H.2    Domadia, P.N.3    Torres, J.4    Bhattacharjya, S.5
  • 62
    • 34147162786 scopus 로고    scopus 로고
    • Thermodynamic analysis of the lipopolysaccharide-dependent resistance of Gram-negative bacteria against polymyxin B
    • DOI 10.1529/biophysj.106.095711
    • J. Howe, J. Andra, R. Conde, M. Iriarte, P. Garidel, M.H. Koch, T. Gutsmann, I. Moriyon, and K. Brandenburg Thermodynamic analysis of the lipopolysaccharide-dependent resistance of gram-negative bacteria against polymyxin B Biophys. J. 92 2007 2796 2805 (Pubitemid 46557854)
    • (2007) Biophysical Journal , vol.92 , Issue.8 , pp. 2796-2805
    • Howe, J.1    Andra, J.2    Conde, R.3    Iriarte, M.4    Garidel, P.5    Koch, M.H.J.6    Gutsmann, T.7    Moriyon, I.8    Brandenburg, K.9
  • 63
    • 21244432036 scopus 로고    scopus 로고
    • Temperature dependence of the binding of endotoxins to the polycationic peptides polymyxin B and its nonapeptide
    • DOI 10.1529/biophysj.104.047944
    • K. Brandenburg, A. David, J. Howe, M.H. Koch, J. Andra, and P. Garidel Temperature dependence of the binding of endotoxins to the polycationic peptides polymyxin B and its nonapeptide Biophys. J. 88 2005 1845 1858 (Pubitemid 40976198)
    • (2005) Biophysical Journal , vol.88 , Issue.3 , pp. 1845-1858
    • Brandenburg, K.1    David, A.2    Howe, J.3    Koch, M.H.J.4    Andra, J.5    Garidel, P.6


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