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Volumn 11, Issue , 2011, Pages

Bacterial membrane activity of -peptide/-peptoid chimeras: Influence of amino acid composition and chain length on the activity against different bacterial strains

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA PEPTIDE BETA PEPTOID CHIMERA; CHIMERIC PROTEIN; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 79959367332     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-11-144     Document Type: Article
Times cited : (32)

References (62)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Antimicrobial peptides of multicellular organisms. M Zasloff, Nature 2002 415 389 395 10.1038/415389a 11807545 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 3
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • Defensins: antimicrobial peptides of innate immunity. T Ganz, Nat Rev Immunol 2003 3 710 720 10.1038/nri1180 12949495 (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 4
    • 0142058024 scopus 로고    scopus 로고
    • Endogenous production of antimicrobial peptides in innate immunity and human disease
    • Endogenous production of antimicrobial peptides in innate immunity and human disease. RL Gallo, V Nizet, Curr Allergy Asthma Rep 2003 3 402 409 10.1007/s11882-003-0074-x 12906776 (Pubitemid 38899107)
    • (2003) Current Allergy and Asthma Reports , vol.3 , Issue.5 , pp. 402-409
    • Gallo, R.L.1    Nizet, V.2
  • 5
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • DOI 10.1016/j.coi.2005.11.004, PII S0952791505001998, Innate Immunity/Antigen Processing and Recognition
    • Cationic host defense (antimicrobial) peptides. KL Brown, RE Hancock, Curr Opin Immunol 2006 18 24 30 10.1016/j.coi.2005.11.004 16337365 (Pubitemid 43049644)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.1 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 6
    • 57749107808 scopus 로고    scopus 로고
    • Bad bugs, no drugs: No ESKAPE! An update from the Infectious Diseases Society of America
    • 10.1086/595011 19035777
    • Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America. HW Boucher, GH Talbot, JS Bradley, JE Edwards, D Gilbert, LB Rice, et al. Clin Infect Dis 2009 48 1 12 10.1086/595011 19035777
    • (2009) Clin Infect Dis , vol.48 , pp. 1-12
    • Boucher, H.W.1    Talbot, G.H.2    Bradley, J.S.3    Edwards, J.E.4    Gilbert, D.5    Rice, L.B.6
  • 7
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • 10.1126/science.1176667 19713519
    • Antibiotics for emerging pathogens. MA Fischbach, CT Walsh, Science 2009 325 1089 1093 10.1126/science.1176667 19713519
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 8
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • DOI 10.1038/nbt1267, PII NBT1267
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. RE Hancock, HG Sahl, Nat Biotechnol 2006 24 1551 1557 10.1038/nbt1267 17160061 (Pubitemid 44967479)
    • (2006) Nature Biotechnology , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 9
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of -helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • 15677462
    • Rational design of -helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. Y Chen, CT Mant, SW Farmer, RE Hancock, ML Vasil, RS Hodges, J Biol Chem 2005 280 12316 12329 15677462
    • (2005) J Biol Chem , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 11
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • DOI 10.1021/bi962507l
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Z Oren, Y Shai, Biochemistry 1997 36 1826 1835 10.1021/bi962507l 9048567 (Pubitemid 27086279)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 12
    • 0036897824 scopus 로고    scopus 로고
    • Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers
    • DOI 10.1016/S1367-5931(02)00385-X
    • Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers. JA Patch, AE Barron, Curr Opin Chem Biol 2002 6 872 877 10.1016/S1367-5931(02)00385-X 12470744 (Pubitemid 35449350)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.6 , pp. 872-877
    • Patch, J.A.1    Barron, A.E.2
  • 13
    • 0037178109 scopus 로고    scopus 로고
    • Mimicry of host-defense peptides by unnatural oligomers: Antimicrobial β-peptides
    • DOI 10.1021/ja0260871
    • Mimicry of host-defense peptides by unnatural oligomers: antimicrobial -peptides. EA Porter, B Weisblum, SH Gellman, J Am Chem Soc 2002 124 7324 7330 10.1021/ja0260871 12071741 (Pubitemid 34670441)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.25 , pp. 7324-7330
    • Porter, E.A.1    Weisblum, B.2    Gellman, S.H.3
  • 14
    • 41949084916 scopus 로고    scopus 로고
    • Structure-activity relationships of antibacterial acyl-lysine oligomers
    • DOI 10.1016/j.chembiol.2008.03.006, PII S1074552108001178
    • Structure-activity relationships of antibacterial acyl-lysine oligomers. IS Radzishevsky, T Kovachi, Y Porat, L Ziserman, F Zaknoon, D Danino, et al. Chem Biol 2008 15 354 362 10.1016/j.chembiol.2008.03.006 18420142 (Pubitemid 351508428)
    • (2008) Chemistry and Biology , vol.15 , Issue.4 , pp. 354-362
    • Radzishevsky, I.S.1    Kovachi, T.2    Porat, Y.3    Ziserman, L.4    Zaknoon, F.5    Danino, D.6    Mor, A.7
  • 16
    • 0028883162 scopus 로고
    • The role of amphipathicity in the folding, self-association and biological activity of multiple subunit small proteins
    • 10.1074/jbc.270.3.1048 7836358
    • The role of amphipathicity in the folding, self-association and biological activity of multiple subunit small proteins. E Perez-Paya, RA Houghten, SE Blondelle, J Biol Chem 1995 270 1048 1056 10.1074/jbc.270.3.1048 7836358
    • (1995) J Biol Chem , vol.270 , pp. 1048-1056
    • Perez-Paya, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 17
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • DOI 10.1016/j.peptides.2003.08.023
    • The relationship between peptide structure and antibacterial activity. JP Powers, RE Hancock, Peptides 2003 24 1681 1691 10.1016/j.peptides.2003.08.023 15019199 (Pubitemid 38198075)
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1681-1691
    • Powers, J.-P.S.1    Hancock, R.E.W.2
  • 18
    • 3042812727 scopus 로고    scopus 로고
    • Unexpected relationships between structure and function in α,β-peptides: Antimicrobial foldamers with heterogeneous backbones
    • DOI 10.1021/ja048546z
    • Unexpected relationships between structure and function in,-peptides: antimicrobial foldamers with heterogeneous backbones. MA Schmitt, B Weisblum, SH Gellman, J Am Chem Soc 2004 126 6848 6849 10.1021/ja048546z 15174837 (Pubitemid 38855366)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.22 , pp. 6848-6849
    • Schmitt, M.A.1    Weisblum, B.2    Gellman, S.H.3
  • 19
    • 33846251959 scopus 로고    scopus 로고
    • Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of α/β-peptides
    • DOI 10.1021/ja0666553
    • Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of /-peptides. MA Schmitt, B Weisblum, SH Gellman, J Am Chem Soc 2007 129 417 428 10.1021/ja0666553 17212422 (Pubitemid 46106642)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.2 , pp. 417-428
    • Schmitt, M.A.1    Weisblum, B.2    Gellman, S.H.3
  • 20
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. A Tossi, C Tarantino, D Romeo, Eur J Biochem 1997 250 549 558 10.1111/j.1432-1033.1997.0549a.x 9428709 (Pubitemid 28012699)
    • (1997) European Journal of Biochemistry , vol.250 , Issue.2 , pp. 549-558
    • Tossi, A.1    Tarantino, C.2    Romeo, D.3
  • 21
    • 49649115502 scopus 로고    scopus 로고
    • Dimeric building blocks for solid-phase synthesis of -peptide - Peptoid chimeras
    • Dimeric building blocks for solid-phase synthesis of -peptide - peptoid chimeras. G Bonke, L Vedel, M Witt, JW Jaroszewski, CA Olsen, H Franzyk, Synthesis 2008 15 2381 2390
    • (2008) Synthesis , vol.15 , pp. 2381-2390
    • Bonke, G.1    Vedel, L.2    Witt, M.3    Jaroszewski, J.W.4    Olsen, C.A.5    Franzyk, H.6
  • 23
    • 77954373564 scopus 로고    scopus 로고
    • Antimicrobial, hemolytic, and cytotoxic activities of -peptoid-peptide hybrid oligomers: Improved properties compared to natural AMPs
    • 10.1002/cbic.201000232 20503219
    • Antimicrobial, hemolytic, and cytotoxic activities of -peptoid-peptide hybrid oligomers: improved properties compared to natural AMPs. CA Olsen, HL Ziegler, HM Nielsen, N Frimodt-Moller, JW Jaroszewski, H Franzyk, Chembiochem 2010 11 1356 1360 10.1002/cbic.201000232 20503219
    • (2010) Chembiochem , vol.11 , pp. 1356-1360
    • Olsen, C.A.1    Ziegler, H.L.2    Nielsen, H.M.3    Frimodt-Moller, N.4    Jaroszewski, J.W.5    Franzyk, H.6
  • 24
    • 54049116616 scopus 로고    scopus 로고
    • Cellular uptake and membrane-destabilising properties of -peptide/-peptoid chimeras: Lessons for the design of new cell-penetrating peptides
    • 10.1016/j.bbamem.2008.06.020 18675778
    • Cellular uptake and membrane-destabilising properties of -peptide/-peptoid chimeras: lessons for the design of new cell-penetrating peptides. C Foged, H Franzyk, S Bahrami, S Frokjaer, JW Jaroszewski, HM Nielsen, et al. Biochim Biophys Acta 2008 1778 2487 2495 10.1016/j.bbamem.2008.06.020 18675778
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2487-2495
    • Foged, C.1    Franzyk, H.2    Bahrami, S.3    Frokjaer, S.4    Jaroszewski, J.W.5    Nielsen, H.M.6
  • 26
    • 0025724956 scopus 로고
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic α-helical model peptides of various chain lengths
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic -helical model peptides of various chain lengths. Y Agawa, S Lee, S Ono, H Aoyagi, M Ohno, T Taniguchi, et al. J Biol Chem 1991 266 20218 20222 1718959 (Pubitemid 21908448)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.30 , pp. 20218-20222
    • Agawa, Y.1    Lee, S.2    Ono, S.3    Aoyagi, H.4    Ohno, M.5    Taniguchi, T.6    Anzai, K.7    Kirino, Y.8
  • 27
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • 10.1074/jbc.M104925200 11473117
    • Interaction of cationic antimicrobial peptides with model membranes. L Zhang, A Rozek, RE Hancock, J Biol Chem 2001 276 35714 35722 10.1074/jbc.M104925200 11473117
    • (2001) J Biol Chem , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.3
  • 28
    • 59449106241 scopus 로고    scopus 로고
    • Interaction of an artificial antimicrobial peptide with lipid membranes
    • 10.1016/j.bbamem.2008.10.005 19013127
    • Interaction of an artificial antimicrobial peptide with lipid membranes. L Yu, L Guo, JL Ding, B Ho, SS Feng, J Popplewell, et al. Biochim Biophys Acta 2009 1788 333 344 10.1016/j.bbamem.2008.10.005 19013127
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 333-344
    • Yu, L.1    Guo, L.2    Ding, J.L.3    Ho, B.4    Feng, S.S.5    Popplewell, J.6
  • 29
    • 35348936718 scopus 로고    scopus 로고
    • Antiplasmodial and prehemolytic activities of α-peptide-β- peptoid chimeras
    • DOI 10.1002/cbic.200700385
    • Antiplasmodial and prehemolytic activities of -peptide - peptoid chimeras. L Vedel, G Bonke, C Foged, H Ziegler, H Franzyk, JW Jaroszewski, et al. Chembiochem 2007 8 1781 1784 10.1002/cbic.200700385 17854020 (Pubitemid 47612865)
    • (2007) ChemBioChem , vol.8 , Issue.15 , pp. 1781-1784
    • Vedel, L.1    Bonke, G.2    Foged, C.3    Ziegler, H.4    Franzyk, H.5    Jaroszewski, J.W.6    Olsen, C.A.7
  • 31
    • 0031019137 scopus 로고    scopus 로고
    • Protamine-induced permeabilization of cell envelopes of gram-positive and gram-negative bacteria
    • Protamine-induced permeabilization of cell envelopes of gram-positive and gram-negative bacteria. C Johansen, A Verheul, L Gram, T Gill, T Abee, Appl Environ Microbiol 1997 63 1155 1159 9055431 (Pubitemid 27098511)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.3 , pp. 1155-1159
    • Johansen, C.1    Verheul, A.2    Gram, L.3    Gill, T.4    Abee, T.5
  • 32
    • 0022888115 scopus 로고
    • Determination of bacterial cell volume with the Coulter Counter
    • Determination of bacterial cell volume with the Coulter Counter. HE Kubitschek, JA Friske, J Bacteriol 1986 168 1466 1467 3536882 (Pubitemid 17226844)
    • (1986) Journal of Bacteriology , vol.168 , Issue.3 , pp. 1466-1467
    • Kubitschek, H.E.1    Friske, J.A.2
  • 33
    • 0018142263 scopus 로고
    • Chemical and electrophoretic changes induced by polymyxin B on outer membrane components from Serratia marcescens
    • Chemical and electrophoretic changes induced by polymyxin B on outer membrane components from Serratia marcescens. DA Brown, JC Tsang, J Antibiot (Tokyo) 1978 31 603 609 (Pubitemid 8402856)
    • (1978) Journal of Antibiotics , vol.31 , Issue.6 , pp. 603-609
    • Brown, D.A.1    Tsang, J.C.2
  • 34
    • 0034951497 scopus 로고    scopus 로고
    • Identification of Proteus mirabilis mutants with increased sensitivity to antimicrobial peptides
    • DOI 10.1128/AAC.45.7.2030-2037.2001
    • Identification of Proteus mirabilis mutants with increased sensitivity to antimicrobial peptides. AJ McCoy, H Liu, TJ Falla, JS Gunn, Antimicrob Agents Chemother 2001 45 2030 2037 10.1128/AAC.45.7.2030-2037.2001 11408219 (Pubitemid 32591694)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.7 , pp. 2030-2037
    • McCoy, A.J.1    Liu, H.2    Falla, T.J.3    Gunn, J.S.4
  • 36
    • 0029010091 scopus 로고
    • Lipopolysaccharides of polymyxin B-resistant mutants of Escherichia coli are extensively substituted by 2-aminoethyl pyrophosphate and contain aminoarabinose in lipid A
    • 10.1111/j.1365-2958.1995.tb02299.x 7565089
    • Lipopolysaccharides of polymyxin B-resistant mutants of Escherichia coli are extensively substituted by 2-aminoethyl pyrophosphate and contain aminoarabinose in lipid A. K Nummila, I Kilpelainen, U Zahringer, M Vaara, IM Helander, Mol Microbiol 1995 16 271 278 10.1111/j.1365-2958.1995.tb02299.x 7565089
    • (1995) Mol Microbiol , vol.16 , pp. 271-278
    • Nummila, K.1    Kilpelainen, I.2    Zahringer, U.3    Vaara, M.4    Helander, I.M.5
  • 37
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic helical antimicrobial peptides
    • 10.1046/j.1432-1033.2001.02494.x 11683882
    • Amphipathic helical antimicrobial peptides. A Giangaspero, L Sandri, A Tossi, Eur J Biochem 2001 268 5589 5600 10.1046/j.1432-1033.2001.02494.x 11683882
    • (2001) Eur J Biochem , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 38
    • 48749098846 scopus 로고    scopus 로고
    • Analogous oligo-acyl-lysines with distinct antibacterial mechanisms
    • 10.1096/fj.07-105015 18385215
    • Analogous oligo-acyl-lysines with distinct antibacterial mechanisms. S Rotem, IS Radzishevsky, D Bourdetsky, S Navon-Venezia, Y Carmeli, A Mor, FASEB J 2008 22 2652 2661 10.1096/fj.07-105015 18385215
    • (2008) FASEB J , vol.22 , pp. 2652-2661
    • Rotem, S.1    Radzishevsky, I.S.2    Bourdetsky, D.3    Navon-Venezia, S.4    Carmeli, Y.5    Mor, A.6
  • 39
    • 46049119398 scopus 로고    scopus 로고
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp
    • 10.1016/j.ijantimicag.2008.04.003 18586467
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. HT Chou, TY Kuo, JC Chiang, MJ Pei, WT Yang, HC Yu, et al. Int J Antimicrob Agents 2008 32 130 138 10.1016/j.ijantimicag.2008.04.003 18586467
    • (2008) Int J Antimicrob Agents , vol.32 , pp. 130-138
    • Chou, H.T.1    Kuo, T.Y.2    Chiang, J.C.3    Pei, M.J.4    Yang, W.T.5    Yu, H.C.6
  • 40
    • 11244267508 scopus 로고    scopus 로고
    • De novo generation of cationic antimicrobial peptides: Influence of length and tryptophan substitution on antimicrobial activity
    • DOI 10.1128/AAC.49.1.316-322.2005
    • De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. B Deslouches, SM Phadke, V Lazarevic, M Cascio, K Islam, RC Montelaro, et al. Antimicrob Agents Chemother 2005 49 316 322 10.1128/AAC.49.1.316-322.2005 15616311 (Pubitemid 40065808)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.1 , pp. 316-322
    • Deslouches, B.1    Phadke, S.M.2    Lazarevic, V.3    Cascio, M.4    Islam, K.5    Montelaro, R.C.6    Mietzner, T.A.7
  • 41
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • DOI 10.1074/jbc.274.1.29
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. M Wu, RE Hancock, J Biol Chem 1999 274 29 35 10.1074/jbc.274.1.29 9867806 (Pubitemid 29035025)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 29-35
    • Wu, M.1    Hancock, R.E.W.2
  • 43
    • 76749084670 scopus 로고    scopus 로고
    • Synthetic antimicrobial peptide L8 (MHLHKTSRVTLYLL) has membrane permeabilisation and bacterial aggregation activity
    • 10.1016/j.ijantimicag.2009.12.003 20129762
    • Synthetic antimicrobial peptide L8 (MHLHKTSRVTLYLL) has membrane permeabilisation and bacterial aggregation activity. E Loit, MT Hincke, I Altosaar, Int J Antimicrob Agents 2010 35 410 411 10.1016/j.ijantimicag.2009.12. 003 20129762
    • (2010) Int J Antimicrob Agents , vol.35 , pp. 410-411
    • Loit, E.1    Hincke, M.T.2    Altosaar, I.3
  • 44
    • 0038745414 scopus 로고    scopus 로고
    • Antibiotics acting on the translational machinery
    • DOI 10.1242/jcs.00365
    • Antibiotics acting on the translational machinery. JM Harms, H Bartels, F Schlunzen, A Yonath, J Cell Sci 2003 116 1391 1393 10.1242/jcs.00365 12640024 (Pubitemid 36527486)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1391-1393
    • Harms, J.M.1    Bartels, H.2    Schlunzen, F.3    Yonath, A.4
  • 45
    • 0036387387 scopus 로고    scopus 로고
    • Activity of quinolones against gram-positive cocci: Mechanisms of drug action and bacterial resistance
    • 10.1007/s10096-002-0788-z 12373497
    • Activity of quinolones against gram-positive cocci: mechanisms of drug action and bacterial resistance. FJ Schmitz, PG Higgins, S Mayer, AC Fluit, A Dalhoff, Eur J Clin Microbiol Infect Dis 2002 21 647 659 10.1007/s10096-002- 0788-z 12373497
    • (2002) Eur J Clin Microbiol Infect Dis , vol.21 , pp. 647-659
    • Schmitz, F.J.1    Higgins, P.G.2    Mayer, S.3    Fluit, A.C.4    Dalhoff, A.5
  • 47
    • 0017119767 scopus 로고
    • Evidences for complex formation between polymyxin B and lipopolysaccharides from Serratia marcescens
    • Evidences for complex formation between polymyxin B and lipopolysaccharides from Serratia marcescens. JC Tsang, DA Weber, DA Brown, J Antibiot (Tokyo) 1976 29 735 742
    • (1976) J Antibiot (Tokyo) , vol.29 , pp. 735-742
    • Tsang, J.C.1    Weber, D.A.2    Brown, D.A.3
  • 48
    • 0031050613 scopus 로고    scopus 로고
    • The bacterial outer membrane as a drug barrier
    • DOI 10.1016/S0966-842X(97)81773-8, PII S0966842X96100731
    • The bacterial outer membrane as a drug barrier. RE Hancock, Trends Microbiol 1997 5 37 42 10.1016/S0966-842X(97)81773-8 9025234 (Pubitemid 27077171)
    • (1997) Trends in Microbiology , vol.5 , Issue.1 , pp. 37-42
    • Hancock, R.E.W.1
  • 49
    • 80052967428 scopus 로고    scopus 로고
    • Bacterial membrane lipids in the action of antimicrobial agents
    • Bacterial membrane lipids in the action of antimicrobial agents. RM Epand, RF Epand, J Pept Sci 2010
    • (2010) J Pept Sci
    • Epand, R.M.1    Epand, R.F.2
  • 51
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • 10.1016/S0005-2736(99)00205-9 10590307
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. B Bechinger, Biochim Biophys Acta 1999 1462 157 183 10.1016/S0005-2736(99)00205-9 10590307
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 52
    • 0030829207 scopus 로고    scopus 로고
    • The cytoplasmic membrane is a primary target for the staphylocidal action of thrombin-induced platelet microbicidal protein
    • The cytoplasmic membrane is a primary target for the staphylocidal action of thrombin-induced platelet microbicidal protein. SP Koo, MR Yeaman, CC Nast, AS Bayer, Infect Immun 1997 65 4795 4800 9353067 (Pubitemid 27463259)
    • (1997) Infection and Immunity , vol.65 , Issue.11 , pp. 4795-4800
    • Koo, S.-P.1    Yeaman, M.R.2    Nast, C.C.3    Bayer, A.S.4
  • 53
    • 77952976637 scopus 로고    scopus 로고
    • Plectasin, a fungal defensin, targets the bacterial cell wall precursor Lipid II
    • 10.1126/science.1185723 20508130
    • Plectasin, a fungal defensin, targets the bacterial cell wall precursor Lipid II. T Schneider, T Kruse, R Wimmer, I Wiedemann, V Sass, U Pag, et al. Science 2010 328 1168 1172 10.1126/science.1185723 20508130
    • (2010) Science , vol.328 , pp. 1168-1172
    • Schneider, T.1    Kruse, T.2    Wimmer, R.3    Wiedemann, I.4    Sass, V.5    Pag, U.6
  • 54
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity
    • 10.1006/bbrc.1994.1234 8123032
    • Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. P Casteels, P Tempst, Biochem Biophys Res Commun 1994 199 339 345 10.1006/bbrc.1994.1234 8123032
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 55
    • 67749122303 scopus 로고    scopus 로고
    • Antibacterial properties and mode of action of a short acyl-lysyl oligomer
    • 10.1128/AAC.00010-09 19487442
    • Antibacterial properties and mode of action of a short acyl-lysyl oligomer. F Zaknoon, H Sarig, S Rotem, L Livne, A Ivankin, D Gidalevitz, et al. Antimicrob Agents Chemother 2009 53 3422 3429 10.1128/AAC.00010-09 19487442
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 3422-3429
    • Zaknoon, F.1    Sarig, H.2    Rotem, S.3    Livne, L.4    Ivankin, A.5    Gidalevitz, D.6
  • 56
    • 0027202188 scopus 로고
    • Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP
    • Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP. G Guihard, H Benedetti, M Besnard, L Letellier, J Biol Chem 1993 268 17775 17780 7688731 (Pubitemid 23260286)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 17775-17780
    • Guihard, G.1    Benedetti, H.2    Besnard, M.3    Letellier, L.4
  • 57
    • 78649774177 scopus 로고    scopus 로고
    • A plausible mode of action of pseudin-2, an antimicrobial peptide from Pseudis paradoxa
    • 10.1016/j.bbamem.2010.08.023 20826126
    • A plausible mode of action of pseudin-2, an antimicrobial peptide from Pseudis paradoxa. SC Park, JY Kim, C Jeong, S Yoo, KS Hahm, Y Park, Biochim Biophys Acta 2011 1808 171 182 10.1016/j.bbamem.2010.08.023 20826126
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 171-182
    • Park, S.C.1    Kim, J.Y.2    Jeong, C.3    Yoo, S.4    Hahm, K.S.5    Park, Y.6
  • 58
    • 77958460527 scopus 로고    scopus 로고
    • Sequence-dependent interaction of -peptides with membranes
    • 10.1021/jp1070242 20882985
    • Sequence-dependent interaction of -peptides with membranes. J Mondal, X Zhu, Q Cui, A Yethiraj, J Phys Chem B 2010 114 13585 13592 10.1021/jp1070242 20882985
    • (2010) J Phys Chem B , vol.114 , pp. 13585-13592
    • Mondal, J.1    Zhu, X.2    Cui, Q.3    Yethiraj, A.4
  • 59
    • 0014127769 scopus 로고
    • Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus
    • 10.1016/0042-6822(67)90105-5 4227577
    • Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus. R Novick, Virology 1967 33 155 166 10.1016/0042-6822(67) 90105-5 4227577
    • (1967) Virology , vol.33 , pp. 155-166
    • Novick, R.1
  • 60
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coli K-12
    • 4568763
    • Pedigrees of some mutant strains of Escherichia coli K-12. BJ Bachmann, Bacteriol Rev 1972 36 525 557 4568763
    • (1972) Bacteriol Rev , vol.36 , pp. 525-557
    • Bachmann, B.J.1
  • 61
    • 0036841862 scopus 로고    scopus 로고
    • In vitro and in vivo invasiveness of different pulsed-field gel electrophoresis types of Listeria monocytogenes
    • In vitro and in vivo invasiveness of different pulsed-field gel electrophoresis types of Listeria monocytogenes. CN Larsen, B Norrung, HM Sommer, M Jakobsen, Appl Environ Microbiol 2002 68 5698 5703 10.1128/AEM.68.11.5698-5703.2002 12406767 (Pubitemid 35265710)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.11 , pp. 5698-5703
    • Larsen, C.N.1    Norrung, B.2    Sommer, H.M.3    Jakobsen, M.4
  • 62
    • 33745172477 scopus 로고    scopus 로고
    • One group of genetically similar Listeria monocytogenes strains frequently dominates and persists in several fish slaughter- and smokehouses
    • DOI 10.1128/AEM.02288-05
    • One group of genetically similar Listeria monocytogenes strains frequently dominates and persists in several fish slaughter- and smokehouses. G Wulff, L Gram, P Ahrens, BF Vogel, Appl Environ Microbiol 2006 72 4313 4322 10.1128/AEM.02288-05 16751546 (Pubitemid 43898662)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.6 , pp. 4313-4322
    • Wulff, G.1    Gram, L.2    Ahrens, P.3    Vogel, B.F.4


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