메뉴 건너뛰기




Volumn 170, Issue 1, 2010, Pages 172-179

Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems

Author keywords

Antimicrobial; Membrane binding; NMR spectroscopy; Paramagnetic relaxation; Peptides

Indexed keywords

DODECYL SULFATE SODIUM; DODECYLPHOSPHORYLCHOLINE; MAXIMIN 1; MAXIMIN H 1; MAXIMIN H 5; MAXIMIN H 6; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 77950519481     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.12.026     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 33749001207 scopus 로고    scopus 로고
    • A trimerizing GxxxG motif is uniquely inserted in the severe acute respiratory syndrome (SARS) coronavirus spike protein transmembrane domain
    • Arbely E., Granot Z., Kass I., Orly J., Arkin I.T. A trimerizing GxxxG motif is uniquely inserted in the severe acute respiratory syndrome (SARS) coronavirus spike protein transmembrane domain. Biochemistry 2006, 45:11349-11356.
    • (2006) Biochemistry , vol.45 , pp. 11349-11356
    • Arbely, E.1    Granot, Z.2    Kass, I.3    Orly, J.4    Arkin, I.T.5
  • 2
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and the normal microflora
    • Boman H.G. Innate immunity and the normal microflora. Immunol. Rev. 2000, 173:5-16.
    • (2000) Immunol. Rev. , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 2005, 3:238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 5
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik L.V., Kozlov M.M. Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 2003, 72:175-207.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 6
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 1999, 13:289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 9
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • Friedrich C.L., Moyles D., Beveridge T.J., Hancock R.E. Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria. Antimicrob. Agents Chemother. 2000, 44:2086-2092.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4
  • 10
    • 0026354641 scopus 로고
    • Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis
    • Gibson B.W., Tang D.Z., Mandrell R., Kelly M., Spindel E.R. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. J. Biol. Chem. 1991, 266:23103-23111.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23103-23111
    • Gibson, B.W.1    Tang, D.Z.2    Mandrell, R.3    Kelly, M.4    Spindel, E.R.5
  • 11
    • 77950518974 scopus 로고    scopus 로고
    • submitted for publication. Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape
    • Göbl, C., Dulle, M., Hohlweg, W., Grossauer, J., Falsone, S.F., Glatter, O., Zangger, K., submitted for publication. Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape. J. Phys. Chem.
    • J. Phys. Chem.
    • Göbl, C.1    Dulle, M.2    Hohlweg, W.3    Grossauer, J.4    Falsone, S.F.5    Glatter, O.6    Zangger, K.7
  • 12
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E., Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 1998, 16:82-88.
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 13
    • 67649277613 scopus 로고    scopus 로고
    • Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?
    • Haney E.F., Hunter H.N., Matsuzaki K., Vogel H.J. Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?. Biochim. Biophys. Acta 2009, 1788:1639-1655.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1639-1655
    • Haney, E.F.1    Hunter, H.N.2    Matsuzaki, K.3    Vogel, H.J.4
  • 14
    • 0020366780 scopus 로고
    • Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae
    • Hultmark D., Engstrom A., Bennich H., Kapur R., Boman H.G. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur. J. Biochem. 1982, 127:207-217.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 207-217
    • Hultmark, D.1    Engstrom, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 16
    • 34249765651 scopus 로고
    • A computer program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4:603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 17
    • 50549170868 scopus 로고
    • On the venomous skin secretions of the orange-speckled frog Bombina variegata
    • Kiss G., Michl H. On the venomous skin secretions of the orange-speckled frog Bombina variegata. Toxicon 1962, 1:33-37.
    • (1962) Toxicon , vol.1 , pp. 33-37
    • Kiss, G.1    Michl, H.2
  • 19
    • 0036166552 scopus 로고    scopus 로고
    • Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima
    • Lai R., Zheng Y.T., Shen J.H., Liu G.J., Liu H., Lee W.H., Tang S.Z., Zhang Y. Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Peptides 2002, 23:427-435.
    • (2002) Peptides , vol.23 , pp. 427-435
    • Lai, R.1    Zheng, Y.T.2    Shen, J.H.3    Liu, G.J.4    Liu, H.5    Lee, W.H.6    Tang, S.Z.7    Zhang, Y.8
  • 20
    • 17444409673 scopus 로고    scopus 로고
    • Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification
    • Lee W.H., Li Y., Lai R., Li S., Zhang Y., Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. Eur. J. Immunol. 2005, 35:1220-1229.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 1220-1229
    • Lee, W.H.1    Li, Y.2    Lai, R.3    Li, S.4    Zhang, Y.5    Wang, W.6
  • 21
    • 70350025590 scopus 로고    scopus 로고
    • Use of relaxation enhancements in a paramagnetic environment for the structure determination of proteins using NMR spectroscopy
    • Madl T., Bermel W., Zangger K. Use of relaxation enhancements in a paramagnetic environment for the structure determination of proteins using NMR spectroscopy. Angew. Chem., Int. Ed. Engl. 2009, 48:8259-8262.
    • (2009) Angew. Chem., Int. Ed. Engl. , vol.48 , pp. 8259-8262
    • Madl, T.1    Bermel, W.2    Zangger, K.3
  • 23
    • 0033696634 scopus 로고    scopus 로고
    • Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions
    • Mangoni M.L., Grovale N., Giorgi A., Mignogna G., Simmaco M., Barra D. Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions. Peptides 2000, 21:1673-1679.
    • (2000) Peptides , vol.21 , pp. 1673-1679
    • Mangoni, M.L.1    Grovale, N.2    Giorgi, A.3    Mignogna, G.4    Simmaco, M.5    Barra, D.6
  • 24
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1999, 1462:1-10.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 25
    • 0001082209 scopus 로고
    • An investigation of the micelllar phase of sodium dodecyl sulfate in aqueous sodium chloride solutions using quasielastic light scattering spectroscopy
    • Mazer N.A., Benedek G.B., Carey M.C. An investigation of the micelllar phase of sodium dodecyl sulfate in aqueous sodium chloride solutions using quasielastic light scattering spectroscopy. J. Phys. Chem. 1976, 80:1075-1085.
    • (1976) J. Phys. Chem. , vol.80 , pp. 1075-1085
    • Mazer, N.A.1    Benedek, G.B.2    Carey, M.C.3
  • 26
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer A.G. NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 2004, 104:3623-3640.
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer, A.G.1
  • 27
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate
    • Pintacuda G., Otting G. Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate. J. Am. Chem. Soc. 2002, 124:372-373.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 28
    • 34247536274 scopus 로고    scopus 로고
    • Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves
    • Respondek M., Madl T., Göbl C., Golser R., Zangger K. Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves. J. Am. Chem. Soc. 2007, 129:5228-5234.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5228-5234
    • Respondek, M.1    Madl, T.2    Göbl, C.3    Golser, R.4    Zangger, K.5
  • 30
    • 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
    • Shai Y. 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 1999, 1462:55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 31
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002, 66:236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 32
    • 67649408946 scopus 로고    scopus 로고
    • Bombinins, antimicrobial peptides from Bombina species
    • Simmaco M., Kreil G., Barra D. Bombinins, antimicrobial peptides from Bombina species. Biochim. Biophys. Acta 2009, 1788:1551-1555.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1551-1555
    • Simmaco, M.1    Kreil, G.2    Barra, D.3
  • 34
    • 0038825375 scopus 로고    scopus 로고
    • Hypothesis: spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion
    • Tamm L.K. Hypothesis: spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion. Biochim. Biophys. Acta 2003, 1614:14-23.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 14-23
    • Tamm, L.K.1
  • 36
    • 0015821003 scopus 로고
    • The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy
    • Verkleij A.J., Zwaal R.F., Roelofsen B., Comfurius P., Kastelijn D., van Deenen L.L. The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim. Biophys. Acta 1973, 323:178-193.
    • (1973) Biochim. Biophys. Acta , vol.323 , pp. 178-193
    • Verkleij, A.J.1    Zwaal, R.F.2    Roelofsen, B.3    Comfurius, P.4    Kastelijn, D.5    van Deenen, L.L.6
  • 37
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 1996, 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 38
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: magainin and protegrin
    • Yang L., Weiss T.M., Lehrer R.I., Huang H.W. Crystallization of antimicrobial pores in membranes: magainin and protegrin. Biophys. J. 2000, 79:2002-2009.
    • (2000) Biophys. J. , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 39
    • 49449096526 scopus 로고    scopus 로고
    • Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4
    • Zangger K., Gossler R., Khatai L., Lohner K., Jilek A. Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4. Toxicon 2008, 52:246-254.
    • (2008) Toxicon , vol.52 , pp. 246-254
    • Zangger, K.1    Gossler, R.2    Khatai, L.3    Lohner, K.4    Jilek, A.5
  • 41
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature (London, United Kingdom) 2002, 415:389-395.
    • (2002) Nature (London, United Kingdom) , vol.415 , pp. 389-395
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.