메뉴 건너뛰기




Volumn 44, Issue 4, 2013, Pages 1215-1224

Rational design of cationic antimicrobial peptides by the tandem of leucine-rich repeat

Author keywords

Antimicrobial peptides; Leucine rich repeat; Membrane peptide interaction

Indexed keywords

CATION; LEUCINE; LEUCYLARGINYLARGINYLLEUCYLTRYPTOPHYLLEUCYLARGINYLALANYLASPARAGINYLARGINYLLEUCINE; LEUCYLARGINYLARGINYLLEUCYLTRYPTOPHYLLEUCYLARGINYLALANYLASPARAGINYLARGINYLLEUCINELEUCYLARGINYLARGINYLLEUCYLTRYPTOPHYLLEUCYLARGINYLALANYLASPARAGINYLARGINYLLEUCINE; LIPID; MELITTIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84876668699     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-012-1457-x     Document Type: Article
Times cited : (31)

References (36)
  • 1
    • 33746807690 scopus 로고    scopus 로고
    • Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells
    • DOI 10.1074/jbc.M602378200
    • Ahmad A, Yadav SP, Asthana N, Mitra K, Srivastava SP, Ghosh JK (2006) Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells. J Biol Chem 281:22029-22038 (Pubitemid 44181907)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.31 , pp. 22029-22038
    • Ahmad, A.1    Yadav, S.P.2    Asthana, N.3    Mitra, K.4    Srivastava, S.P.5    Ghosh, J.K.6
  • 2
    • 78751581724 scopus 로고    scopus 로고
    • Studies on the assembly of a leucine zipper antibacterial peptide and its analogs onto mammalian cells and bacteria
    • 20857151 1:CAS:528:DC%2BC3MXlt1yrsw%3D%3D 10.1007/s00726-010-0744-7
    • Ahmad A, Azmi S, Ghosh JK (2011) Studies on the assembly of a leucine zipper antibacterial peptide and its analogs onto mammalian cells and bacteria. Amino Acids 40:749-759
    • (2011) Amino Acids , vol.40 , pp. 749-759
    • Ahmad, A.1    Azmi, S.2    Ghosh, J.K.3
  • 3
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin: A leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity
    • DOI 10.1074/jbc.M408881200
    • Asthana N, Yadav SP, Ghosh JK (2004) Dissection of antibacterial and toxic activity of melittin. J Biol Chem 279:55042-55050 (Pubitemid 40066496)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 5
    • 34548491198 scopus 로고    scopus 로고
    • Internalins: A complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes
    • DOI 10.1016/j.micinf.2007.05.003, PII S1286457907001797, Forum on Listeria From Genomics to Pathagonesis
    • Bierne H, Sabet C, Personnic N, Cossart P (2007) Internalins: a complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes. Microbes Infect 9:1156-1166 (Pubitemid 47375143)
    • (2007) Microbes and Infection , vol.9 , Issue.10 , pp. 1156-1166
    • Bierne, H.1    Sabet, C.2    Personnic, N.3    Cossart, P.4
  • 6
    • 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
    • Brown KL, Hancock REW (2006) Cationic host defense (antimicrobial) peptides. Curr Opin Immunol 18:24-30 (Pubitemid 43049644)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.1 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 7
    • 0032577067 scopus 로고    scopus 로고
    • 2+-binding loop of synaptotagmin with lipid bilayers
    • DOI 10.1074/jbc.273.22.13995
    • 2+-binding loop of synaptotagmin with lipid bilayers. J Biol Chem 273:13995-14001 (Pubitemid 28268455)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.22 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 8
    • 33846272114 scopus 로고    scopus 로고
    • Plant NBS-LRR proteins in pathogen sensing and host defense
    • DOI 10.1038/ni1410, PII NI1410
    • DeYoung BJ, Innes RW (2006) Plant NBS-LRR proteins in pathogen sensing and host defense. Nat Immunol 7:1243-1249 (Pubitemid 46111241)
    • (2006) Nature Immunology , vol.7 , Issue.12 , pp. 1243-1249
    • DeYoung, B.J.1    Innes, R.W.2
  • 9
    • 49449103767 scopus 로고    scopus 로고
    • Induction by cationic antimicrobial peptides and involvement in intrinsic polymyxin and antimicrobial peptide resistance, biofilm formation, and swarming motility of PsrA in Pseudomonas aeruginosa
    • 18556795 1:CAS:528:DC%2BD1cXpslOjtLY%3D 10.1128/JB.00594-08
    • Gooderham WJ, Bains M, McPhee JB, Wiegand I, Hancock REW (2008) Induction by cationic antimicrobial peptides and involvement in intrinsic polymyxin and antimicrobial peptide resistance, biofilm formation, and swarming motility of PsrA in Pseudomonas aeruginosa. J Bacteriol 190:5624-5634
    • (2008) J Bacteriol , vol.190 , pp. 5624-5634
    • Gooderham, W.J.1    Bains, M.2    McPhee, J.B.3    Wiegand, I.4    Hancock, R.E.W.5
  • 10
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • DOI 10.1126/science.1129818
    • Hasper HE, Kramer NE, Smith JL, Hillman JD, Zachariah C, Kuipers OP, de Kruijff B, Breukink E (2006) An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313:1636-1637 (Pubitemid 44414037)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5    Kuipers, O.P.6    De Kruijff, B.7    Breukink, E.8
  • 11
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • DOI 10.1021/bi000946l
    • Huang HW (2000) Action of antimicrobial peptides: two-state model. Biochemistry 39:8347-8352 (Pubitemid 30489931)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8347-8352
    • Huang, H.W.1
  • 12
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • 11560930 1:STN:280:DC%2BD3MnnvVCruw%3D%3D 10.1074/jbc.M106317200
    • Ibrahim HR, Thomas U, Pellegrini A (2001) A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J Biol Chem 276:43767-43774
    • (2001) J Biol Chem , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 13
    • 10644260444 scopus 로고    scopus 로고
    • Membrane translocation mechanism of the antimicrobial peptide buforin 2
    • DOI 10.1021/bi048206q
    • Kobayashi S, Chikushi A, Tougu S, Imura Y, Nishida M, Yano Y, Matsuzaki K (2004) Membrane translocation mechanism of the antimicrobial peptide buforin 2. Biochemistry 43:15610-15616 (Pubitemid 39647487)
    • (2004) Biochemistry , vol.43 , Issue.49 , pp. 15610-15616
    • Kobayashi, S.1    Chikushi, A.2    Tougu, S.3    Imura, Y.4    Nishida, M.5    Yano, Y.6    Matsuzaki, K.7
  • 14
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • DOI 10.1016/S0005-2736(01)00382-0, PII S0005273601003820
    • Ladokhin AS, White SH (2001) 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim Biophys Acta 1514:253-260 (Pubitemid 32831013)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1514 , Issue.2 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 15
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA-binding proteins
    • 3289117 1:CAS:528:DyaL1cXks12jtbw%3D 10.1126/science.3289117
    • Landschulz WH, Johnson PF, McKnight SL (1988) The leucine zipper: a hypothetical structure common to a new class of DNA-binding proteins. Science 240:1759-1764
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 16
    • 32944472272 scopus 로고    scopus 로고
    • Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori
    • DOI 10.1042/BJ20051574
    • Lee KH, Lee DG, Park Y, Kand DI, Shin SY, Hahm KS, Kim Y (2006) Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori. Biochem J 394:105-114 (Pubitemid 43259660)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 105-114
    • Lee, K.H.1    Lee, D.G.2    Park, Y.3    Kang, D.-I.4    Shin, S.Y.5    Hahm, K.-S.6    Kim, Y.7
  • 17
    • 0021170801 scopus 로고
    • Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa
    • Loh B, Grant C, Hancock REW (1984) Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa. Antimicrob Agents Chemother 26:546-551 (Pubitemid 14018094)
    • (1984) Antimicrobial Agents and Chemotherapy , vol.26 , Issue.4 , pp. 546-551
    • Loh, B.1    Grant, C.2    Hancock, R.E.W.3
  • 18
    • 33645440966 scopus 로고    scopus 로고
    • Super-motifs of leucine-rich repeats (LRRs) proteins
    • 1:CAS:528:DC%2BD3MXjsVWht78%3D
    • Matsushima N, Kamiya M, Suzuki N, Tanaka T (2000) Super-motifs of leucine-rich repeats (LRRs) proteins. Genome Inform 11:343-345
    • (2000) Genome Inform , vol.11 , pp. 343-345
    • Matsushima, N.1    Kamiya, M.2    Suzuki, N.3    Tanaka, T.4
  • 19
    • 77956491889 scopus 로고    scopus 로고
    • A nested leucine rich repeat (LRR) domain: The precursor of LRRs is a ten or eleven residue motif
    • 20825685 10.1186/1471-2180-10-235
    • Matsushima N, Miyashita H, Mikami T, Kuroki Y (2010) A nested leucine rich repeat (LRR) domain: the precursor of LRRs is a ten or eleven residue motif. BMC Microbiol 10:235-244
    • (2010) BMC Microbiol , vol.10 , pp. 235-244
    • Matsushima, N.1    Miyashita, H.2    Mikami, T.3    Kuroki, Y.4
  • 20
    • 33745040554 scopus 로고    scopus 로고
    • Plant NBS-LRR proteins: Adaptable guards
    • DOI 10.1186/gb-2006-7-4-212
    • McHale L, Tan X, Koehl P, Michelmore RW (2006) Plant NBS-LRR proteins: adaptable guards. Genome Biol 7:212 (Pubitemid 44774178)
    • (2006) Genome Biology , vol.7 , Issue.4 , pp. 212
    • McHale, L.1    Tan, X.2    Koehl, P.3    Michelmore, R.W.4
  • 22
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides
    • DOI 10.1021/bi0267846
    • Papo N, Shai Y (2003) Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 42:458-466 (Pubitemid 36105764)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 23
    • 0035913957 scopus 로고    scopus 로고
    • Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata
    • DOI 10.1016/S0014-5793(01)02956-8, PII S0014579301029568
    • Park S, Park SH, Ahn HC, Kim S, Kim SS, Lee BJ, Lee BJ (2001) Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata. FEBS Lett 507:95-100 (Pubitemid 33000304)
    • (2001) FEBS Letters , vol.507 , Issue.1 , pp. 95-100
    • Park, S.1    Park, S.-H.2    Ahn, H.-C.3    Kim, S.4    Kim, S.S.5    Lee, B.J.6    Lee, B.-J.7
  • 25
    • 79955542011 scopus 로고    scopus 로고
    • Rationale-based, de novo design of dehydrophenylalanine-containing antibiotic peptides and systematic modification in sequence for enhanced potency
    • 21321136 1:CAS:528:DC%2BC3MXhsFClsL%2FF 10.1128/AAC.01493-10
    • Pathak S, Chauhan VS (2011) Rationale-based, de novo design of dehydrophenylalanine-containing antibiotic peptides and systematic modification in sequence for enhanced potency. Antimicrob Agents Chemother 55:2178-2188
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 2178-2188
    • Pathak, S.1    Chauhan, V.S.2
  • 26
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles
    • DOI 10.1021/bi971009p
    • Rex S, Schwarz G (1998) Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles. Biochemistry 37:2336-2345 (Pubitemid 28119307)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 27
    • 34447618237 scopus 로고    scopus 로고
    • New insights into innate immunity in Arabidopsis
    • DOI 10.1111/j.1462-5822.2007.00991.x
    • Ryan CA, Huffaker A, Yamaguchi Y (2007) New insights into innate immunity in Arabidopsis. Cell Microbiol 9:1902-1908 (Pubitemid 47087082)
    • (2007) Cellular Microbiology , vol.9 , Issue.8 , pp. 1902-1908
    • Ryan, C.A.1    Huffaker, A.2    Yamaguchi, Y.3
  • 28
    • 0036840580 scopus 로고    scopus 로고
    • Cationic hydrophobic peptides with antimicrobial activity
    • DOI 10.1128/AAC.46.11.3585-3590.2002
    • Stark M, Liu LP, Deber CM (2002) Cationic hydrophobic peptides with antimicrobial activity. Antimicrob Agents Ch 46:3585-3590 (Pubitemid 35192930)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.11 , pp. 3585-3590
    • Stark, M.1    Liu, L.-P.2    Deber, C.M.3
  • 30
    • 0029984176 scopus 로고    scopus 로고
    • 1H-NMR and CD. Evidence for specific peptide-SDS interactions
    • DOI 10.1016/0005-2760(96)00037-9
    • Wang G, Treleaven WD, Cushley RJ (1996) Conformation of human serum apolipoprotein A-I (166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions. Biochim Biophys Acta 1301:174-184 (Pubitemid 26193075)
    • (1996) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1301 , Issue.3 , pp. 174-184
    • Wang, G.1    Treleaven, W.D.2    Cushley, R.J.3
  • 31
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • DOI 10.1021/bi9826299
    • Wu M, Maier E, Benz R, Hancock REW (1999) Mechanism of Interaction of Different Classes of Cationic Antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38:7235-7242 (Pubitemid 29262785)
    • (1999) Biochemistry , vol.38 , Issue.22 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 32
    • 0344838675 scopus 로고    scopus 로고
    • Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure
    • DOI 10.1016/S0014-5793(03)00266-7
    • Yang ST, Shin SY, Lee CW, Kim YC, Hahm KS, Kim JI (2003) Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure. FEBS Lett 540:229-233 (Pubitemid 36398062)
    • (2003) FEBS Letters , vol.540 , Issue.1-3 , pp. 229-233
    • Yang, S.-T.1    Shin, S.Y.2    Lee, C.W.3    Kim, Y.-C.4    Hahm, K.-S.5    Kim, J.I.6
  • 33
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • DOI 10.1124/pr.55.1.2
    • Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55:27-55 (Pubitemid 36268398)
    • (2003) Pharmacological Reviews , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 34
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 35
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides-Using a sequence template to guide structure-activity relationship studies
    • DOI 10.1016/j.bbamem.2006.03.021, PII S0005273606001088
    • Zelezetsky I, Tossi A (2006) Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies. Biochim Biophys Acta 1758:1436-1449 (Pubitemid 44436080)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 36
    • 34249070808 scopus 로고    scopus 로고
    • Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action
    • DOI 10.1016/j.bbamem.2007.03.010, PII S0005273607001046
    • Zhu WL, Song YM, Park Y, Park KH, Yang ST, Kim JI, Park IS, Hahm KS, Shin SY (2007) Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action. Biochim Biophys Acta 1768:1506-1517 (Pubitemid 46782713)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.6 , pp. 1506-1517
    • Zhu, W.L.1    Song, Y.M.2    Park, Y.3    Park, K.H.4    Yang, S.-T.5    Kim, J.I.6    Park, I.-S.7    Hahm, K.-S.8    Shin, S.Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.