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Volumn 1818, Issue 5, 2012, Pages 1386-1394

Binding of peptides corresponding to the carboxy-terminal region of human-β-defensins-1-3 with model membranes investigated by isothermal titration calorimetry

Author keywords

Electrostatic interaction; Human defensin analog; Membrane destabilization; Peptide conformation; Peptide membrane interaction; Surface partition equilibrium model

Indexed keywords

1 PALMITOYL 2 OLEOYL SN GLYCEROPHOSPHOGLYCEROL; 1 PHENYL 6 [4 (TRIMETHYLAMMONIO)PHENYL] 1,3,5 HEXATRIENE; 1,6 DIPHENYL 1,3,5 HEXATRIENE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; ALKENE DERIVATIVE; AMPHOLYTE; BETA DEFENSIN 1; BETA DEFENSIN 2; BETA DEFENSIN 3; GLYCEROPHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 84858726977     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.02.016     Document Type: Article
Times cited : (11)

References (64)
  • 2
    • 3242778563 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of vertebrates
    • T. Ganz Defensins: antimicrobial peptides of vertebrates C. R. Biol. 327 2004 539 549
    • (2004) C. R. Biol. , vol.327 , pp. 539-549
    • Ganz, T.1
  • 3
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • R.I. Lehrer, and T. Ganz Defensins of vertebrate animals Curr. Opin. Immunol. 14 2002 96 102
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 4
    • 0142218765 scopus 로고    scopus 로고
    • Roles of antimicrobial peptides such as defensins in innate and adaptive immunity
    • J.J. Oppenheim, A. Biragyn, L.W. Kwak, and D. Yang Roles of antimicrobial peptides such as defensins in innate and adaptive immunity Ann. Rheum. Dis. 62 2003 17 21
    • (2003) Ann. Rheum. Dis. , vol.62 , pp. 17-21
    • Oppenheim, J.J.1    Biragyn, A.2    Kwak, L.W.3    Yang, D.4
  • 7
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • M.E. Selsted, and A.J. Ouellette Mammalian defensins in the antimicrobial immune response Nat. Immunol. 6 2005 551 557
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 8
    • 0035914442 scopus 로고    scopus 로고
    • The structure of human beta-defensin-1: New insights into structural properties of beta-defensins
    • D.M. Hoover, O. Chertov, and J. Lubkowski The structure of human beta-defensin-1: new insights into structural properties of beta-defensins J. Biol. Chem. 276 2001 39021 39026
    • (2001) J. Biol. Chem. , vol.276 , pp. 39021-39026
    • Hoover, D.M.1    Chertov, O.2    Lubkowski, J.3
  • 12
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • D.J. Schibli, H.N. Hunter, V. Aseyev, T.D. Starner, J.M. Wiencek, P.B. McCray Jr., B.F. Tack, and H.J. Vogel The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus J. Biol. Chem. 277 2002 8279 8289
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray, Jr.P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 13
    • 0032169557 scopus 로고    scopus 로고
    • Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung
    • R. Bals, X. Wang, Z. Wu, T. Freeman, V. Bafna, M. Zasloff, and J.M. Wilson Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung J. Clin. Invest. 102 1998 874 880
    • (1998) J. Clin. Invest. , vol.102 , pp. 874-880
    • Bals, R.1    Wang, X.2    Wu, Z.3    Freeman, T.4    Bafna, V.5    Zasloff, M.6    Wilson, J.M.7
  • 14
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • M.J. Goldman, G.M. Anderson, E.D. Stolzenberg, U.P. Kari, M. Zasloff, and J.M. Wilson Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis Cell 88 1997 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
  • 16
    • 33749525670 scopus 로고    scopus 로고
    • Human beta-defensin-3: A promising antimicrobial peptide
    • G. Batoni, G. Maisetta, S. Esin, and M. Campa Human beta-defensin-3: a promising antimicrobial peptide Mini Rev. Med. Chem. 6 2006 1063 1073
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 1063-1073
    • Batoni, G.1    Maisetta, G.2    Esin, S.3    Campa, M.4
  • 17
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic
    • J. Harder, J. Bartels, E. Christophers, and J.M. Schroder Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic J. Biol. Chem. 276 2001 5707 5713
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 18
    • 33750083071 scopus 로고    scopus 로고
    • Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human beta-defensins 1-3
    • V. Krishnakumari, S. Singh, and R. Nagaraj Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human beta-defensins 1-3 Peptides 27 2006 2607 2613
    • (2006) Peptides , vol.27 , pp. 2607-2613
    • Krishnakumari, V.1    Singh, S.2    Nagaraj, R.3
  • 19
    • 50049096434 scopus 로고    scopus 로고
    • Mode of action of human beta-defensin 3 against Staphylococcus aureus and transcriptional analysis of responses to defensin challenge
    • V. Sass, U. Pag, A. Tossi, G. Bierbaum, and H.G. Sahl Mode of action of human beta-defensin 3 against Staphylococcus aureus and transcriptional analysis of responses to defensin challenge Int. J. Med. Microbiol. 298 2008 619 633
    • (2008) Int. J. Med. Microbiol. , vol.298 , pp. 619-633
    • Sass, V.1    Pag, U.2    Tossi, A.3    Bierbaum, G.4    Sahl, H.G.5
  • 20
    • 33645820597 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of beta-defensins, multi-functional peptides of the immune system
    • E. Kluver, K. Adermann, and A. Schulz Synthesis and structure-activity relationship of beta-defensins, multi-functional peptides of the immune system J. Pept. Sci. 12 2006 243 257
    • (2006) J. Pept. Sci. , vol.12 , pp. 243-257
    • Kluver, E.1    Adermann, K.2    Schulz, A.3
  • 21
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human beta-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • E. Kluver, S. Schulz-Maronde, S. Scheid, B. Meyer, W.G. Forssmann, and K. Adermann Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity Biochemistry 44 2005 9804 9816
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Kluver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 22
    • 59749096989 scopus 로고    scopus 로고
    • Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3
    • V. Krishnakumari, N. Rangaraj, and R. Nagaraj Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3 Antimicrob. Agents Chemother. 53 2009 256 260
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 256-260
    • Krishnakumari, V.1    Rangaraj, N.2    Nagaraj, R.3
  • 23
    • 0042072743 scopus 로고    scopus 로고
    • Single disulfide and linear analogues corresponding to the carboxy-terminal segment of bovine beta-defensin-2: Effects of introducing the beta-hairpin nucleating sequence d-pro-gly on antibacterial activity and biophysical properties
    • V. Krishnakumari, A. Sharadadevi, S. Singh, and R. Nagaraj Single disulfide and linear analogues corresponding to the carboxy-terminal segment of bovine beta-defensin-2: effects of introducing the beta-hairpin nucleating sequence d-pro-gly on antibacterial activity and biophysical properties Biochemistry 42 2003 9307 9315
    • (2003) Biochemistry , vol.42 , pp. 9307-9315
    • Krishnakumari, V.1    Sharadadevi, A.2    Singh, S.3    Nagaraj, R.4
  • 24
    • 0036171208 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: Structural and disulfide bridge requirements for activity
    • M. Mandal, M.V. Jagannadham, and R. Nagaraj Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity Peptides 23 2002 413 418
    • (2002) Peptides , vol.23 , pp. 413-418
    • Mandal, M.1    Jagannadham, M.V.2    Nagaraj, R.3
  • 25
    • 0036196119 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges
    • M. Mandal, and R. Nagaraj Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges J. Pept. Res. 59 2002 95 104
    • (2002) J. Pept. Res. , vol.59 , pp. 95-104
    • Mandal, M.1    Nagaraj, R.2
  • 26
    • 36248983841 scopus 로고    scopus 로고
    • Human defensins: Synthesis and structural properties
    • M. Pazgier, X. Li, W. Lu, and J. Lubkowski Human defensins: synthesis and structural properties Curr. Pharm. Des. 13 2007 3096 3118
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 3096-3118
    • Pazgier, M.1    Li, X.2    Lu, W.3    Lubkowski, J.4
  • 29
    • 34547120485 scopus 로고    scopus 로고
    • Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs
    • G. Zou, E. de Leeuw, C. Li, M. Pazgier, P. Zeng, W.Y. Lu, J. Lubkowski, and W. Lu Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs J. Biol. Chem. 282 2007 19653 19665
    • (2007) J. Biol. Chem. , vol.282 , pp. 19653-19665
    • Zou, G.1    De Leeuw, E.2    Li, C.3    Pazgier, M.4    Zeng, P.5    Lu, W.Y.6    Lubkowski, J.7    Lu, W.8
  • 30
    • 70350729306 scopus 로고    scopus 로고
    • Structure-dependent charge density as a determinant of antimicrobial activity of peptide analogues of defensin
    • Y. Bai, S. Liu, P. Jiang, L. Zhou, J. Li, C. Tang, C. Verma, Y. Mu, R.W. Beuerman, and K. Pervushin Structure-dependent charge density as a determinant of antimicrobial activity of peptide analogues of defensin Biochemistry 48 2009 7229 7239
    • (2009) Biochemistry , vol.48 , pp. 7229-7239
    • Bai, Y.1    Liu, S.2    Jiang, P.3    Zhou, L.4    Li, J.5    Tang, C.6    Verma, C.7    Mu, Y.8    Beuerman, R.W.9    Pervushin, K.10
  • 32
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • J. Seelig Titration calorimetry of lipid-peptide interactions Biochim. Biophys. Acta 1331 1997 103 116
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 33
    • 13544250497 scopus 로고    scopus 로고
    • Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes
    • T. Abraham, R.N. Lewis, R.S. Hodges, and R.N. McElhaney Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes Biochemistry 44 2005 2103 2112
    • (2005) Biochemistry , vol.44 , pp. 2103-2112
    • Abraham, T.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0034681140 scopus 로고    scopus 로고
    • Membrane binding and pore formation of the antibacterial peptide PGLa: Thermodynamic and mechanistic aspects
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects Biochemistry 39 2000 442 452
    • (2000) Biochemistry , vol.39 , pp. 442-452
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 37
    • 0033543167 scopus 로고    scopus 로고
    • Binding of antibacterial magainin peptides to electrically neutral membranes: Thermodynamics and structure
    • T. Wieprecht, M. Beyermann, and J. Seelig Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure Biochemistry 38 1999 10377 10387
    • (1999) Biochemistry , vol.38 , pp. 10377-10387
    • Wieprecht, T.1    Beyermann, M.2    Seelig, J.3
  • 38
    • 67650081577 scopus 로고    scopus 로고
    • Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue
    • K.B. Chandrababu, B. Ho, and D. Yang Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue Biochemistry 48 2009 6052 6061
    • (2009) Biochemistry , vol.48 , pp. 6052-6061
    • Chandrababu, K.B.1    Ho, B.2    Yang, D.3
  • 39
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • K. Lohner, A. Latal, R.I. Lehrer, and T. Ganz Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems Biochemistry 36 1997 1525 1531
    • (1997) Biochemistry , vol.36 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 40
    • 37249066994 scopus 로고    scopus 로고
    • Interaction of antibacterial peptides spanning the carboxy-terminal region of human beta-defensins 1-3 with phospholipids at the air-water interface and inner membrane of E. coli
    • V. Krishnakumari, and R. Nagaraj Interaction of antibacterial peptides spanning the carboxy-terminal region of human beta-defensins 1-3 with phospholipids at the air-water interface and inner membrane of E. coli Peptides 29 2008 7 14
    • (2008) Peptides , vol.29 , pp. 7-14
    • Krishnakumari, V.1    Nagaraj, R.2
  • 42
    • 0024553457 scopus 로고
    • The electrostatic properties of membranes
    • S. McLaughlin The electrostatic properties of membranes Annu. Rev. Biophys. Chem. 18 1989 113 136
    • (1989) Annu. Rev. Biophys. Chem. , vol.18 , pp. 113-136
    • McLaughlin, S.1
  • 43
  • 44
    • 0027525276 scopus 로고
    • Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = + 1 to z = + 3
    • J. Seelig, S. Nebel, P. Ganz, and C. Bruns Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = + 1 to z = + 3 Biochemistry 32 1993 9714 9721
    • (1993) Biochemistry , vol.32 , pp. 9714-9721
    • Seelig, J.1    Nebel, S.2    Ganz, P.3    Bruns, C.4
  • 45
    • 0034702860 scopus 로고    scopus 로고
    • Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry
    • E. Breukink, P. Ganz, B. de Kruijff, and J. Seelig Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry Biochemistry 39 2000 10247 10254
    • (2000) Biochemistry , vol.39 , pp. 10247-10254
    • Breukink, E.1    Ganz, P.2    De Kruijff, B.3    Seelig, J.4
  • 46
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation
    • G. Klocek, T. Schulthess, Y. Shai, and J. Seelig Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation Biochemistry 48 2009 2586 2596
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1    Schulthess, T.2    Shai, Y.3    Seelig, J.4
  • 47
    • 77952541316 scopus 로고    scopus 로고
    • Microcalorimetric and zeta potential study on binding of drugs on liposomes
    • M. Ikonen, L. Murtomaki, and K. Kontturi Microcalorimetric and zeta potential study on binding of drugs on liposomes Colloids Surf. B 78 2010 275 282
    • (2010) Colloids Surf. B , vol.78 , pp. 275-282
    • Ikonen, M.1    Murtomaki, L.2    Kontturi, K.3
  • 48
    • 33749522506 scopus 로고    scopus 로고
    • Interaction of verapamil with lipid membranes and P-glycoprotein: Connecting thermodynamics and membrane structure with functional activity
    • M. Meier, X.L. Blatter, A. Seelig, and J. Seelig Interaction of verapamil with lipid membranes and P-glycoprotein: connecting thermodynamics and membrane structure with functional activity Biophys. J. 91 2006 2943 2955
    • (2006) Biophys. J. , vol.91 , pp. 2943-2955
    • Meier, M.1    Blatter, X.L.2    Seelig, A.3    Seelig, J.4
  • 50
    • 0016188814 scopus 로고
    • Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles
    • P.J. Sims, A.S. Waggoner, C.H. Wang, and J.F. Hoffman Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles Biochemistry 13 1974 3315 3330
    • (1974) Biochemistry , vol.13 , pp. 3315-3330
    • Sims, P.J.1    Waggoner, A.S.2    Wang, C.H.3    Hoffman, J.F.4
  • 51
    • 0024347619 scopus 로고
    • Membrane "fluidity" as detected by diphenylhexatriene probes
    • B.R. Lentz Membrane "fluidity" as detected by diphenylhexatriene probes Chem. Phys. Lipids 50 1989 171 190
    • (1989) Chem. Phys. Lipids , vol.50 , pp. 171-190
    • Lentz, B.R.1
  • 52
    • 0019886584 scopus 로고
    • 1-[4-(Trimethylamino)phenyl]-6-phenylhexa-1,3,5-triene: Synthesis, fluorescence properties, and use as a fluorescence probe of lipid bilayers
    • F.G. Prendergast, R.P. Haugland, and P.J. Callahan 1-[4-(Trimethylamino) phenyl]-6-phenylhexa-1,3,5-triene: synthesis, fluorescence properties, and use as a fluorescence probe of lipid bilayers Biochemistry 20 1981 7333 7338
    • (1981) Biochemistry , vol.20 , pp. 7333-7338
    • Prendergast, F.G.1    Haugland, R.P.2    Callahan, P.J.3
  • 53
    • 0032474434 scopus 로고    scopus 로고
    • Location of diphenylhexatriene (DPH) and its derivatives within membranes: Comparison of different fluorescence quenching analyses of membrane depth
    • R.D. Kaiser, and E. London Location of diphenylhexatriene (DPH) and its derivatives within membranes: comparison of different fluorescence quenching analyses of membrane depth Biochemistry 37 1998 8180 8190
    • (1998) Biochemistry , vol.37 , pp. 8180-8190
    • Kaiser, R.D.1    London, E.2
  • 54
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor
    • S. Kobayashi, K. Takeshima, C.B. Park, S.C. Kim, and K. Matsuzaki Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor Biochemistry 39 2000 8648 8654
    • (2000) Biochemistry , vol.39 , pp. 8648-8654
    • Kobayashi, S.1    Takeshima, K.2    Park, C.B.3    Kim, S.C.4    Matsuzaki, K.5
  • 55
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium J. Mol. Biol. 294 1999 785 794
    • (1999) J. Mol. Biol. , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 56
    • 34247368438 scopus 로고    scopus 로고
    • Thermodynamics of the coil <==> beta-sheet transition in a membrane environment
    • M. Meier, and J. Seelig Thermodynamics of the coil <==> beta-sheet transition in a membrane environment J. Mol. Biol. 369 2007 277 289
    • (2007) J. Mol. Biol. , vol.369 , pp. 277-289
    • Meier, M.1    Seelig, J.2
  • 57
    • 4444260314 scopus 로고    scopus 로고
    • Reversible unfolding of beta-sheets in membranes: A calorimetric study
    • W.C. Wimley, and S.H. White Reversible unfolding of beta-sheets in membranes: a calorimetric study J. Mol. Biol. 342 2004 703 711
    • (2004) J. Mol. Biol. , vol.342 , pp. 703-711
    • Wimley, W.C.1    White, S.H.2
  • 58
    • 0034910318 scopus 로고    scopus 로고
    • Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: Nucleation model of defect formation
    • I.V. Polozov, G.M. Anantharamaiah, J.P. Segrest, and R.M. Epand Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: nucleation model of defect formation Biophys. J. 81 2001 949 959
    • (2001) Biophys. J. , vol.81 , pp. 949-959
    • Polozov, I.V.1    Anantharamaiah, G.M.2    Segrest, J.P.3    Epand, R.M.4
  • 59
    • 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


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