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Volumn 50, Issue 9, 2011, Pages 1514-1523

Influence of C-terminal amidation on the efficacy of modelin-5

Author keywords

[No Author keywords available]

Indexed keywords

AMIDATION; ANIONIC LIPIDS; BI-LAYER; BI-LAYER STRUCTURE; BINDING COEFFICIENTS; E. COLI; GAIN INSIGHT; HELICAL STRUCTURES; HELICITIES; HELIX FORMATION; HILL COEFFICIENT; LIPID EXTRACT; LOW LEVEL; MEMBRANE DISRUPTION; PHOSPHATIDYLETHANOLAMINE; PRESSURE CHANGE; RATE-LIMITING STEPS; SURFACE ACTIVITIES; THERMO DYNAMIC ANALYSIS;

EID: 79952120584     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101687t     Document Type: Article
Times cited : (63)

References (49)
  • 1
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.07.001, PII S0005273606002616
    • Bechinger, B. and Lohner, K. (2006) Detergent-like actions of linear amphipathic cationic antimicrobial peptides Biochim. Biophys. Acta 1758, 1529-1539 (Pubitemid 44436087)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 2
    • 3042781052 scopus 로고    scopus 로고
    • Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology
    • Marshall, S. H. and Arenas, G. (2003) Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology Electron. J. Biotechnol. 6, 271-284
    • (2003) Electron. J. Biotechnol. , vol.6 , pp. 271-284
    • Marshall, S.H.1    Arenas, G.2
  • 3
    • 32944471770 scopus 로고    scopus 로고
    • Antimicrobial peptides (AMPs): Peptide structure and mode of action
    • Park, Y. and Hahm, K. S. (2005) Antimicrobial peptides (AMPs): Peptide structure and mode of action J. Biochem. Mol. Biol. 38, 507-516
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 507-516
    • Park, Y.1    Hahm, K.S.2
  • 4
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • DOI 10.1016/S0005-2736(97)00051-5, PII S0005273697000515
    • Matsuzaki, K., Sugishita, K., Harada, M., Fujii, N., and Miyajima, K. (1997) Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria Biochim. Biophys. Acta 1327, 119-130 (Pubitemid 27283405)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1327 , Issue.1 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.-I.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 5
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • DOI 10.1016/S0196-9781(01)00498-3, PII S0196978101004983
    • Shai, Y. and Oren, Z. (2001) From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides Peptides 22, 1629-1641 (Pubitemid 32918242)
    • (2001) Peptides , vol.22 , Issue.10 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 6
    • 34948877554 scopus 로고    scopus 로고
    • Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins)
    • DOI 10.1016/j.bbamem.2007.05.023, PII S0005273607002003
    • Epand, R. F., Savage, P. B., and Epand, R. M. (2007) Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins) Biochim. Biophys. Acta 1768, 2500-2509 (Pubitemid 47532031)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.10 , pp. 2500-2509
    • Epand, R.F.1    Savage, P.B.2    Epand, R.M.3
  • 7
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems
    • Lohner, K. and Prenner, E. J. (1999) Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems Biochim. Biophys. Acta 1462, 141-156
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 8
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu, D. and Rivas, L. (1998) Animal antimicrobial peptides: an overview Biopolymers 47, 415-433
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 9
    • 33748919831 scopus 로고    scopus 로고
    • Membrane interactions of antimicrobial peptides from Australian tree frogs
    • DOI 10.1016/j.bbamem.2006.02.010, PII S0005273606000629
    • Boland, M. P. and Separovic, F. (2006) Membrane interactions of antimicrobial peptides from Australian tree frogs Biochim. Biophys. Acta 1758, 1178-1183 (Pubitemid 44436071)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1178-1183
    • Boland, M.P.1    Separovic, F.2
  • 11
    • 0028174888 scopus 로고
    • The NH2-terminal α-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity
    • Mor, A. and Nicolas, P. (1994) The NH2-terminal α-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity J. Biol. Chem. 269, 1934-1939
    • (1994) J. Biol. Chem. , vol.269 , pp. 1934-1939
    • Mor, A.1    Nicolas, P.2
  • 12
    • 0015924632 scopus 로고
    • Biosynthesis of melittin, a toxic peptide from bee venom. Amino-acid sequence of the precursor
    • Kreil, G. (1973) Biosynthesis of melittin, a toxic peptide from bee venom. Amino-acid sequence of the precursor Eur. J. Biochem. 33, 558-566
    • (1973) Eur. J. Biochem. , vol.33 , pp. 558-566
    • Kreil, G.1
  • 14
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • DOI 10.1111/j.0105-2896.2004.0124.x
    • Bulet, P., Stocklin, R., and Menin, L. (2004) Anti-microbial peptides: From invertebrates to vertebrates Immunol. Rev. 198, 169-184 (Pubitemid 38406943)
    • (2004) Immunological Reviews , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 15
    • 0028504387 scopus 로고
    • Preliminary experimental anticancer activity of cecropins
    • Moore, A. J., Devine, D. A., and Bibby, M. C. (1994) Preliminary experimental anticancer activity of cecropins Pept. Res. 7, 265-269
    • (1994) Pept. Res. , vol.7 , pp. 265-269
    • Moore, A.J.1    Devine, D.A.2    Bibby, M.C.3
  • 16
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • DOI 10.1016/S0304-4157(98)00021-5, PII S0304415798000215
    • White, S. H. and Wimley, W. C. (1998) Hydrophobic interactions of peptides with membrane interfaces Biochim. Biophys. Acta 1376, 339-352 (Pubitemid 28517884)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 17
    • 0037062560 scopus 로고    scopus 로고
    • Structural consequences of carboxyamidation of dermaseptin S3
    • DOI 10.1021/bi016013m
    • Shalev, D. E., Mor, A., and Kustanovich, I. (2002) Structural consequences of carboxyamidation of dermaseptin S3 Biochemistry 41, 7312-7317 (Pubitemid 34602447)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7312-7317
    • Shalev, D.E.1    Mor, A.2    Kustanovich, I.3
  • 18
    • 0032528858 scopus 로고    scopus 로고
    • Identification and characterization of the antimicrobial peptide corresponding to C-terminal β-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor
    • Lee, K. H., Hong, S. Y., Oh, J. E., Kwon, M., Yoon, J. H., Lee, J., Lee, B. L., and Moon, H. M. (1998) Identification and characterization of the antimicrobial peptide corresponding to C-terminal β-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor Biochem. J. 334 (Part 1) 99-105 (Pubitemid 28420977)
    • (1998) Biochemical Journal , vol.334 , Issue.1 , pp. 99-105
    • Lee, K.H.1    Hong, S.Y.2    Oh, J.E.3    Kwon, M.Y.4    Yoon, J.H.5    Lee, J.H.6    Lee, B.L.7    Moon, H.M.8
  • 19
    • 0027988532 scopus 로고
    • The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms
    • Mor, A., Hani, K., and Nicolas, P. (1994) The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms J. Biol. Chem. 269, 31635-31641 (Pubitemid 24379527)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.50 , pp. 31635-31641
    • Mor, A.1    Hani, K.2    Nicolas, P.3
  • 20
    • 0030997215 scopus 로고    scopus 로고
    • Improved activity of a synthetic indolicidin analog
    • Falla, T. J. and Hancock, R. E. (1997) Improved activity of a synthetic indolicidin analog Antimicrob. Agents Chemother. 41, 771-775 (Pubitemid 27150529)
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , Issue.4 , pp. 771-775
    • Falla, T.J.1    Hancock, R.E.W.2
  • 21
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α helical antimicrobial peptides
    • Giangaspero, A., Sandri, L., and Tossi, A. (2001) Amphipathic α helical antimicrobial peptides Eur. J. Biochem. 268, 5589-5600
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 23
    • 70450262224 scopus 로고    scopus 로고
    • U.S. Patent 6875744, Helix BioMedix, Inc.
    • Owen, D. R. (2005) Short bioactive peptides. U.S. Patent 6875744, Helix BioMedix, Inc.
    • (2005) Short Bioactive Peptides
    • Owen, D.R.1
  • 24
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G. and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification Can. J. Med. Sci. 37, 911-917
    • (1959) Can. J. Med. Sci. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 25
    • 0023263405 scopus 로고
    • Local anesthetics and pressure: A comparison of dibucaine binding to lipid monolayers and bilayers
    • Seeling, A. (1987) Local anesthetics and pressure: A comparison of dibucaine binding to lipid monolayers and bilayers Biochim. Biophys. Acta 899, 196-204
    • (1987) Biochim. Biophys. Acta , vol.899 , pp. 196-204
    • Seeling, A.1
  • 26
    • 8844224914 scopus 로고    scopus 로고
    • Comparative physicochemical study of SIKVAV peptide and its retro and retro-enantio analogues
    • DOI 10.1016/j.colsurfa.2004.08.041, PII S0927775704005801, Ist International Meeting on Applied Physics
    • Alminana, N., Alsina, M. A., Ortiz, A., and Reig, F. (2004) Comparative physicochemical study of SIKVAV peptide and its retro and retro-enantio analogues Colloids Surf., A 249, 19-24 (Pubitemid 39531582)
    • (2004) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.249 , Issue.1-3 , pp. 19-24
    • Alminana, N.1    Alsina, M.A.2    Ortiz, A.3    Reig, F.4
  • 28
    • 0001270572 scopus 로고
    • Random packing in two dimensions and the structure of monolayers
    • Quickenden, T. I. and Tan, G. K. (1974) Random packing in two dimensions and the structure of monolayers J. Colloid Interface Sci. 48, 382-393
    • (1974) J. Colloid Interface Sci. , vol.48 , pp. 382-393
    • Quickenden, T.I.1    Tan, G.K.2
  • 30
    • 0029283976 scopus 로고
    • The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions
    • Wall, J., Golding, C. A., Van Veen, M., and OShea, P. (1995) The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide-membrane interactions Mol. Membr. Biol. 12, 183-192
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 183-192
    • Wall, J.1    Golding, C.A.2    Van Veen, M.3    Oshea, P.4
  • 31
    • 34548702205 scopus 로고    scopus 로고
    • Characterization of the interaction of two peptides from the N terminus of the NHR domain of HIV-1 gp41 with phospholipid membranes
    • DOI 10.1021/bi700911g
    • Moreno, M. R., Guillen, J., Perez-Berna, A. J., Amoros, D., Gomez, A. I., Bernabeu, A., and Villalain, J. (2007) Characterization of the interaction of two peptides from the N terminus of the NHR domain of HIV-1 gp41 with phospholipid membranes Biochemistry 46, 10572-10584 (Pubitemid 47417252)
    • (2007) Biochemistry , vol.46 , Issue.37 , pp. 10572-10584
    • Moreno, M.R.1    Guillen, J.2    Perez-Berna, A.J.3    Amoros, D.4    Gomez, A.I.5    Bernabeu, A.6    Villalain, J.7
  • 33
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock, R. E. and Diamond, G. (2000) The role of cationic antimicrobial peptides in innate host defences Trends Microbiol. 8, 402-410
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 34
    • 33847175151 scopus 로고    scopus 로고
    • The interactions of aurein 1.2 with cancer cell membranes
    • Dennison, S. R., Harris, F., and Phoenix, D. A. (2007) The interactions of aurein 1.2 with cancer cell membranes Biophys. Chem. 127, 78-83
    • (2007) Biophys. Chem. , vol.127 , pp. 78-83
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 35
    • 0005489659 scopus 로고    scopus 로고
    • Physicochemical interaction of a lipophilic derivative of HAV antigen VP3(110-121) with lipid monolayers
    • Sospedra, P., Haro, I., Alsina, M. A., Reig, F., and Mestres, C. (1999) Physicochemical interaction of a lipophilic derivative of HAV antigen VP3(110-121) with lipid monolayers Mater. Sci. Eng., C 8-9, 543-549
    • (1999) Mater. Sci. Eng., C , vol.89 , pp. 543-549
    • Sospedra, P.1    Haro, I.2    Alsina, M.A.3    Reig, F.4    Mestres, C.5
  • 36
    • 0032694324 scopus 로고    scopus 로고
    • The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes
    • Maget-Dana, R. (1999) The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes Biochim. Biophys. Acta 1462, 109-140
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 109-140
    • Maget-Dana, R.1
  • 40
    • 3042546066 scopus 로고    scopus 로고
    • Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin
    • DOI 10.1016/j.bbamem.2004.03.013, PII S0005273604000938
    • Ambroggio, E. E., Separovic, F., Bowie, J., and Fidelio, G. D. (2004) Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin Biochim. Biophys. Acta 1664, 31-37 (Pubitemid 38829314)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1664 , Issue.1 , pp. 31-37
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.3    Fidelio, G.D.4
  • 41
    • 0031822695 scopus 로고    scopus 로고
    • Introduction of potential helix-capping residues into an engineered helical protein
    • Parker, M. H. and Hefford, M. A. (1998) Introduction of potential helix-capping residues into an engineered helical protein Biotechnol. Appl. Biochem. 28 (Part 1) 69-76 (Pubitemid 28369908)
    • (1998) Biotechnology and Applied Biochemistry , vol.28 , Issue.1 , pp. 69-76
    • Parker, M.H.1    Hefford, M.A.2
  • 43
    • 33644925279 scopus 로고    scopus 로고
    • The antibiotic and DNA-transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes
    • DOI 10.1096/fj.05-4293fje
    • Mason, A. J., Martinez, A., Glaubitz, C., Danos, O., Kichler, A., and Bechinger, B. (2006) The antibiotic and DNA-transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes FASEB J. 20, 320-322 (Pubitemid 46671157)
    • (2006) FASEB Journal , vol.20 , Issue.2 , pp. 320-322
    • Mason, A.J.1    Martinez, A.2    Glaubitz, C.3    Danos, O.4    Kichler, A.5    Bechinger, B.6
  • 46
    • 54249087977 scopus 로고    scopus 로고
    • Helical peptides derived from lactoferrin bind hepatitis C virus envelope protein E2
    • Beleid, R., Douglas, D., Kneteman, N., and Kaur, K. (2008) Helical peptides derived from lactoferrin bind hepatitis C virus envelope protein E2 Chem. Biol. Drug Des. 72, 436-443
    • (2008) Chem. Biol. Drug Des. , vol.72 , pp. 436-443
    • Beleid, R.1    Douglas, D.2    Kneteman, N.3    Kaur, K.4
  • 47
    • 77952554008 scopus 로고    scopus 로고
    • Thermodynamics of RTA3 peptide binding to membranes and consequences for antimicrobial activity
    • Hawrani, A., Howe, R. A., Walsh, T. R., and Dempsey, C. E. (2010) Thermodynamics of RTA3 peptide binding to membranes and consequences for antimicrobial activity Biochim. Biophys. Acta 1798, 1254-1262
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1254-1262
    • Hawrani, A.1    Howe, R.A.2    Walsh, T.R.3    Dempsey, C.E.4
  • 48
    • 0034213003 scopus 로고    scopus 로고
    • Investigations of spectrin-lipid interactions using fluoresceinphosphatidylethanolamine as a membrane probe
    • DOI 10.1016/S0005-2736(00)00168-1, PII S0005273600001681
    • OToole, P. J., Morrison, I. E., and Cherry, R. J. (2000) Investigations of spectrin-lipid interactions using fluoresceinphosphatidylethanolamine as a membrane probe Biochim. Biophys. Acta 1466, 39-46 (Pubitemid 30312963)
    • (2000) Biochimica et Biophysica Acta - Biomembranes , vol.1466 , Issue.1-2 , pp. 39-46
    • O'Toole, P.J.1    Morrison, I.E.G.2    Cherry, R.J.3
  • 49
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • Schiffer, M. and Edmundson, A. B. (1967) Use of helical wheels to represent the structures of proteins and to identify segments with helical potential Biophys. J. 7, 121-135
    • (1967) Biophys. J. , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2


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