메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Effect of Selectively Introducing Arginine and D-Amino Acids on the Antimicrobial Activity and Salt Sensitivity in Analogs of Human Beta-Defensins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; ARGININE; BETA DEFENSIN; BETA DEFENSIN 1; BETA DEFENSIN 3; CALCIUM ION; CARBOXYFLUORESCEIN; DEXTRO AMINO ACID; DEXTRO ARGININE; HC 1 PEPTIDE; HC 3 PEPTIDE; ISOLEUCINE; MAGNESIUM ION; PHD 1 PEPTIDE; PHD 3 PEPTIDE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84884696038     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077031     Document Type: Article
Times cited : (19)

References (55)
  • 1
    • 16844377323 scopus 로고    scopus 로고
    • Defensins and other antimicrobial peptides: a historical perspective and an update
    • doi: 10.2174/1386207053764594
    • Ganz T, (2005) Defensins and other antimicrobial peptides: a historical perspective and an update. Comb Chem High Throughput Screen 8: 209-217. doi:10.2174/1386207053764594. PubMed: 15892623.
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 209-217
    • Ganz, T.1
  • 2
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • doi: 10.1038/nrmicro976
    • Lehrer RI, (2004) Primate defensins. Nat Rev Microbiol 2: 727-738. doi:10.1038/nrmicro976. PubMed: 15372083.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 727-738
    • Lehrer, R.I.1
  • 4
    • 78249233244 scopus 로고    scopus 로고
    • Antimicrobial peptides: the ancient arm of the human immune system
    • doi: 10.4161/viru.1.5.12983
    • Wiesner J, Vilcinskas A, (2010) Antimicrobial peptides: the ancient arm of the human immune system. Virulence 1: 440-464. doi:10.4161/viru.1.5.12983. PubMed: 21178486.
    • (2010) Virulence , vol.1 , pp. 440-464
    • Wiesner, J.1    Vilcinskas, A.2
  • 5
    • 33847011002 scopus 로고    scopus 로고
    • Human defensins and cathelicidins in the skin: beyond direct antimicrobial properties
    • doi: 10.1615/CritRevImmunol.v26.i6.60
    • Niyonsaba F, Nagaoka I, Ogawa H, (2006) Human defensins and cathelicidins in the skin: beyond direct antimicrobial properties. Crit Rev Immunol 26: 545-576. doi:10.1615/CritRevImmunol.v26.i6.60. PubMed: 17341194.
    • (2006) Crit Rev Immunol , vol.26 , pp. 545-576
    • Niyonsaba, F.1    Nagaoka, I.2    Ogawa, H.3
  • 6
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • doi: 10.1038/ni1206
    • Selsted ME, Ouellette AJ, (2005) Mammalian defensins in the antimicrobial immune response. Nat Immunol 6: 551-557. doi:10.1038/ni1206. PubMed: 15908936.
    • (2005) Nat Immunol , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 7
    • 0033044786 scopus 로고    scopus 로고
    • Antimicrobial peptides as mediators of epithelial host defense
    • doi: 10.1203/00006450-199906000-00001
    • Huttner KM, Bevins CL, (1999) Antimicrobial peptides as mediators of epithelial host defense. Pediatr Res 45: 785-794. doi:10.1203/00006450-199906000-00001. PubMed: 10367766.
    • (1999) Pediatr Res , vol.45 , pp. 785-794
    • Huttner, K.M.1    Bevins, C.L.2
  • 8
    • 0031581544 scopus 로고    scopus 로고
    • Expression of natural peptide antibiotics in human skin
    • doi: 10.1016/S0140-6736(05)63574-X
    • Fulton C, Anderson GM, Zasloff M, Bull R, Quinn AG, (1997) Expression of natural peptide antibiotics in human skin. Lancet 350: 1750-1751. doi:10.1016/S0140-6736(05)63574-X. PubMed: 9413472.
    • (1997) Lancet , vol.350 , pp. 1750-1751
    • Fulton, C.1    Anderson, G.M.2    Zasloff, M.3    Bull, R.4    Quinn, A.G.5
  • 9
    • 0030820726 scopus 로고    scopus 로고
    • A peptide antibiotic from human skin
    • doi: 10.1038/43088
    • Harder J, Bartels J, Christophers E, Schröder JM, (1997) A peptide antibiotic from human skin. Nature 387: 861. doi:10.1038/43088. PubMed: 9202117.
    • (1997) Nature , vol.387 , pp. 861
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schröder, J.M.4
  • 10
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic
    • doi: 10.1074/jbc.M008557200
    • Harder J, Bartels J, Christophers E, Schroder JM, (2001) Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. J Biol Chem 276: 5707-5713. doi:10.1074/jbc.M008557200. PubMed: 11085990.
    • (2001) J Biol Chem , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 11
    • 0036178642 scopus 로고    scopus 로고
    • Human beta-defensin-2 production in keratinocytes is regulated by interleukin-1, bacteria, and the state of differentiation
    • doi: 10.1046/j.0022-202x.2001.01651.x
    • Liu AY, Destoumieux D, Wong AV, Park CH, Valore EV, et al. (2002) Human beta-defensin-2 production in keratinocytes is regulated by interleukin-1, bacteria, and the state of differentiation. J Invest Dermatol 118: 275-281. doi:10.1046/j.0022-202x.2001.01651.x. PubMed: 11841544.
    • (2002) J Invest Dermatol , vol.118 , pp. 275-281
    • Liu, A.Y.1    Destoumieux, D.2    Wong, A.V.3    Park, C.H.4    Valore, E.V.5
  • 13
    • 0030569343 scopus 로고    scopus 로고
    • Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells
    • doi: 10.1016/0014-5793(96)01123-4
    • Zhao C, Wang I, Lehrer RI, (1996) Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells. FEBS Lett 396: 319-322. doi:10.1016/0014-5793(96)01123-4. PubMed: 8915011.
    • (1996) FEBS Lett , vol.396 , pp. 319-322
    • Zhao, C.1    Wang, I.2    Lehrer, R.I.3
  • 14
    • 0035430147 scopus 로고    scopus 로고
    • Human beta-defensin 4: a novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity
    • PubMed: 11481241
    • García JR, Krause A, Schulz S, Rodríguez-Jiménez FJ, Klüver E, et al. (2001) Human beta-defensin 4: a novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity. FASEB J 15: 1819-1821. PubMed: 11481241.
    • (2001) FASEB J , vol.15 , pp. 1819-1821
    • García, J.R.1    Krause, A.2    Schulz, S.3    Rodríguez-Jiménez, F.J.4    Klüver, E.5
  • 15
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • doi: 10.1016/S0092-8674(00)81895-4
    • Goldman MJ, Anderson GM, Stolzenberg ED, Kari UP, Zasloff M, et al. (1997) Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88: 553-560. doi:10.1016/S0092-8674(00)81895-4. PubMed: 9038346.
    • (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
  • 16
    • 0032523214 scopus 로고    scopus 로고
    • Human beta-defensin-1: an antimicrobial peptide of urogenital tissues
    • doi: 10.1172/JCI1861
    • Valore EV, Park CH, Quayle AJ, Wiles KR, McCray PB Jr, et al. (1998) Human beta-defensin-1: an antimicrobial peptide of urogenital tissues. J Clin Invest 101: 1633-1642. doi:10.1172/JCI1861. PubMed: 9541493.
    • (1998) J Clin Invest , vol.101 , pp. 1633-1642
    • Valore, E.V.1    Park, C.H.2    Quayle, A.J.3    Wiles, K.R.4    McCray Jr., P.B.5
  • 17
    • 0032169557 scopus 로고    scopus 로고
    • Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung
    • doi: 10.1172/JCI2410
    • Bals R, Wang X, Wu Z, Freeman T, Bafna V, et al. (1998) Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. J Clin Invest 102: 874-880. doi:10.1172/JCI2410. PubMed: 9727055.
    • (1998) J Clin Invest , vol.102 , pp. 874-880
    • Bals, R.1    Wang, X.2    Wu, Z.3    Freeman, T.4    Bafna, V.5
  • 18
    • 0000215491 scopus 로고    scopus 로고
    • Production of beta-defensins by human airway epithelia
    • doi: 10.1073/pnas.95.25.14961
    • Singh PK, Jia HP, Wiles K, Hesselberth J, Liu L, et al. (1998) Production of beta-defensins by human airway epithelia. Proc Natl Acad Sci U S A 95: 14961-14966. doi:10.1073/pnas.95.25.14961. PubMed: 9843998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14961-14966
    • Singh, P.K.1    Jia, H.P.2    Wiles, K.3    Hesselberth, J.4    Liu, L.5
  • 19
    • 0041923585 scopus 로고    scopus 로고
    • Antimicrobial characterization of human beta-defensin 3 derivatives
    • doi: 10.1128/AAC.47.9.2804-2809.2003
    • Hoover DM, Wu Z, Tucker K, Lu W, Lubkowski J, (2003) Antimicrobial characterization of human beta-defensin 3 derivatives. Antimicrob Agents Chemother 47: 2804-2809. doi:10.1128/AAC.47.9.2804-2809.2003. PubMed: 12936977.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2804-2809
    • Hoover, D.M.1    Wu, Z.2    Tucker, K.3    Lu, W.4    Lubkowski, J.5
  • 20
    • 33645820597 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of beta-defensins, multi-functional peptides of the immune system
    • doi: 10.1002/psc.749
    • Klüver E, Adermann K, Schulz A, (2006) Synthesis and structure-activity relationship of beta-defensins, multi-functional peptides of the immune system. J Pept Sci 12: 243-257. doi:10.1002/psc.749. PubMed: 16491514.
    • (2006) J Pept Sci , vol.12 , pp. 243-257
    • Klüver, 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
    • doi: 10.1021/bi050272k
    • Klüver E, Schulz-Maronde S, Scheid S, Meyer B, Forssmann WG, et al. (2005) Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 44: 9804-9816. doi:10.1021/bi050272k. PubMed: 16008365.
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Klüver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5
  • 22
    • 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
    • doi: 10.1021/bi034403y
    • Krishnakumari V, Sharadadevi A, Singh S, Nagaraj R, (2003) 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: 9307-9315. doi:10.1021/bi034403y. PubMed: 12899617.
    • (2003) Biochemistry , vol.42 , pp. 9307-9315
    • Krishnakumari, V.1    Sharadadevi, A.2    Singh, S.3    Nagaraj, R.4
  • 23
    • 33750083071 scopus 로고    scopus 로고
    • Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human beta-defensins 1-3
    • doi: 10.1016/j.peptides.2006.06.004
    • Krishnakumari V, Singh S, Nagaraj R, (2006) Antibacterial activities of synthetic peptides corresponding to the carboxy-terminal region of human beta-defensins 1-3. Peptides 27: 2607-2613. doi:10.1016/j.peptides.2006.06.004. PubMed: 16860904.
    • (2006) Peptides , vol.27 , pp. 2607-2613
    • Krishnakumari, V.1    Singh, S.2    Nagaraj, R.3
  • 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
    • doi: 10.1016/S0196-9781(01)00628-3
    • Mandal M, Jagannadham MV, Nagaraj R, (2002) Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs:structural and disulfide bridge requirements for activity. Peptides 23: 413-418. doi:10.1016/S0196-9781(01)00628-3. PubMed: 11835989.
    • (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
    • doi: 10.1034/j.1399-3011.2002.01945.x
    • Mandal M, Nagaraj R, (2002) Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges. J Pept Res 59: 95-104. doi:10.1034/j.1399-3011.2002.01945.x. PubMed: 11985703.
    • (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
    • doi: 10.2174/138161207782110381
    • Pazgier M, Li X, Lu W, Lubkowski J, (2007) Human defensins: synthesis and structural properties. Curr Pharm Des 13: 3096-3118. doi:10.2174/138161207782110381. PubMed: 17979752.
    • (2007) Curr Pharm Des , vol.13 , pp. 3096-3118
    • Pazgier, M.1    Li, X.2    Lu, W.3    Lubkowski, J.4
  • 27
    • 0042808526 scopus 로고    scopus 로고
    • Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3
    • doi: 10.1073/pnas.1533186100
    • Wu Z, Hoover DM, Yang D, Boulègue C, Santamaria F, et al. (2003) Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3. Proc Natl Acad Sci U S A 100: 8880-8885. doi:10.1073/pnas.1533186100. PubMed: 12840147.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8880-8885
    • Wu, Z.1    Hoover, D.M.2    Yang, D.3    Boulègue, C.4    Santamaria, F.5
  • 28
    • 78751653584 scopus 로고    scopus 로고
    • Reduction of disulphide bonds unmasks potent antimicrobial activity of human beta-defensin 1
    • doi: 10.1038/nature09674
    • Schroeder BO, Wu Z, Nuding S, Groscurth S, Marcinowski M, et al. (2011) Reduction of disulphide bonds unmasks potent antimicrobial activity of human beta-defensin 1. Nature 469: 419-423. doi:10.1038/nature09674. PubMed: 21248850.
    • (2011) Nature , vol.469 , pp. 419-423
    • Schroeder, B.O.1    Wu, Z.2    Nuding, S.3    Groscurth, S.4    Marcinowski, M.5
  • 29
    • 59749096989 scopus 로고    scopus 로고
    • Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3
    • doi: 10.1128/AAC.00470-08
    • Krishnakumari V, Rangaraj N, Nagaraj R, (2009) Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3. Antimicrob Agents Chemother 53: 256-260. doi:10.1128/AAC.00470-08. PubMed: 18809937.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 256-260
    • Krishnakumari, V.1    Rangaraj, N.2    Nagaraj, R.3
  • 30
    • 70350417487 scopus 로고    scopus 로고
    • Through the looking glass, mechanistic insights from enantiomeric human defensins
    • doi: 10.1074/jbc.M109.018085
    • Wei G, de Leeuw E, Pazgier M, Yuan W, Zou G, et al. (2009) Through the looking glass, mechanistic insights from enantiomeric human defensins. J Biol Chem 284: 29180-29192. doi:10.1074/jbc.M109.018085. PubMed: 19640840.
    • (2009) J Biol Chem , vol.284 , pp. 29180-29192
    • Wei, G.1    de Leeuw, E.2    Pazgier, M.3    Yuan, W.4    Zou, G.5
  • 31
    • 25444478690 scopus 로고    scopus 로고
    • Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids
    • doi: 10.1074/jbc.M503084200
    • Xie C, Prahl A, Ericksen B, Wu Z, Zeng P, et al. (2005) Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. J Biol Chem 280: 32921-32929. doi:10.1074/jbc.M503084200. PubMed: 15894545.
    • (2005) J Biol Chem , vol.280 , pp. 32921-32929
    • Xie, C.1    Prahl, A.2    Ericksen, B.3    Wu, Z.4    Zeng, P.5
  • 32
    • 70350461418 scopus 로고    scopus 로고
    • Electropositive charge in alpha-defensin bactericidal activity: functional effects of Lys-for-Arg substitutions vary with the peptide primary structure
    • doi: 10.1128/IAI.00695-09
    • Llenado RA, Weeks CS, Cocco MJ, Ouellette AJ, (2009) Electropositive charge in alpha-defensin bactericidal activity: functional effects of Lys-for-Arg substitutions vary with the peptide primary structure. Infect Immun 77: 5035-5043. doi:10.1128/IAI.00695-09. PubMed: 19737896.
    • (2009) Infect Immun , vol.77 , pp. 5035-5043
    • Llenado, R.A.1    Weeks, C.S.2    Cocco, M.J.3    Ouellette, A.J.4
  • 33
    • 12144289841 scopus 로고    scopus 로고
    • Structure-activity determinants in paneth cell alpha-defensins: loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions
    • doi: 10.1074/jbc.M310251200
    • Tanabe H, Qu X, Weeks CS, Cummings JE, Kolusheva S, et al. (2004) Structure-activity determinants in paneth cell alpha-defensins: loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions. J Biol Chem 279: 11976-11983. doi:10.1074/jbc.M310251200. PubMed: 14702345.
    • (2004) J Biol Chem , vol.279 , pp. 11976-11983
    • Tanabe, H.1    Qu, X.2    Weeks, C.S.3    Cummings, J.E.4    Kolusheva, S.5
  • 34
    • 34547120485 scopus 로고    scopus 로고
    • Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs
    • doi: 10.1074/jbc.M611003200
    • Zou G, de Leeuw E, Li C, Pazgier M, Zeng P, et al. (2007) Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs. J Biol Chem 282: 19653-19665. doi:10.1074/jbc.M611003200. PubMed: 17452329.
    • (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
  • 35
    • 12044255356 scopus 로고
    • Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications
    • doi: 10.1021/ja00017a044
    • Tam JP, Wu CR, Liu W, Zhang JW, (1991) Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications. J Am Chem Soc 113: 6657-6662. doi:10.1021/ja00017a044.
    • (1991) J Am Chem Soc , vol.113 , pp. 6657-6662
    • Tam, J.P.1    Wu, C.R.2    Liu, W.3    Zhang, J.W.4
  • 36
    • 0032539938 scopus 로고    scopus 로고
    • A fast and inexpensive method for N-terminal fluorescein-labeling of peptides
    • doi: 10.1016/S0960-894X(98)00084-5
    • Weber PJ, Bader JE, Folkers G, Beck-Sickinger AG, (1998) A fast and inexpensive method for N-terminal fluorescein-labeling of peptides. Bioorg Med Chem Lett 8: 597-600. doi:10.1016/S0960-894X(98)00084-5. PubMed: 9871567.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 597-600
    • Weber, P.J.1    Bader, J.E.2    Folkers, G.3    Beck-Sickinger, A.G.4
  • 37
    • 27644584146 scopus 로고    scopus 로고
    • Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines
    • doi: 10.1128/AAC.49.11.4561-4566.2005
    • Varkey J, Nagaraj R, (2005) Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines. Antimicrob Agents Chemother 49: 4561-4566. doi:10.1128/AAC.49.11.4561-4566.2005. PubMed: 16251296.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4561-4566
    • Varkey, J.1    Nagaraj, R.2
  • 38
    • 0033818544 scopus 로고    scopus 로고
    • Effect of ions on antibacterial activity of human beta defensin 2
    • PubMed: 11092238
    • Tomita T, Hitomi S, Nagase T, Matsui H, Matsuse T, et al. (2000) Effect of ions on antibacterial activity of human beta defensin 2. Microbiol Immunol 44: 749-754. PubMed: 11092238.
    • (2000) Microbiol Immunol , vol.44 , pp. 749-754
    • Tomita, T.1    Hitomi, S.2    Nagase, T.3    Matsui, H.4    Matsuse, T.5
  • 39
    • 0032551383 scopus 로고    scopus 로고
    • Human beta-defensin-1: A urinary peptide present in variant molecular forms and its putative functional implication
    • PubMed: 9682027
    • Zucht HD, Grabowsky J, Schrader M, Liepke C, Jürgens M, et al. (1998) Human beta-defensin-1: A urinary peptide present in variant molecular forms and its putative functional implication. Eur J Med Res 3: 315-323. PubMed: 9682027.
    • (1998) Eur J Med Res , vol.3 , pp. 315-323
    • Zucht, H.D.1    Grabowsky, J.2    Schrader, M.3    Liepke, C.4    Jürgens, M.5
  • 40
    • 0034635459 scopus 로고    scopus 로고
    • Engineered salt-insensitive alpha-defensins with end-to-end circularized structures
    • doi: 10.1074/jbc.275.6.3943
    • Yu Q, Lehrer RI, Tam JP, (2000) Engineered salt-insensitive alpha-defensins with end-to-end circularized structures. J Biol Chem 275: 3943-3949. doi:10.1074/jbc.275.6.3943. PubMed: 10660548.
    • (2000) J Biol Chem , vol.275 , pp. 3943-3949
    • Yu, Q.1    Lehrer, R.I.2    Tam, J.P.3
  • 41
    • 77952626078 scopus 로고    scopus 로고
    • Novel synthetic, salt-resistant analogs of human beta-defensins 1 and 3 endowed with enhanced antimicrobial activity
    • doi: 10.1128/AAC.01550-09
    • Scudiero O, Galdiero S, Cantisani M, Di Noto R, Vitiello M, et al. (2010) Novel synthetic, salt-resistant analogs of human beta-defensins 1 and 3 endowed with enhanced antimicrobial activity. Antimicrob Agents Chemother 54: 2312-2322. doi:10.1128/AAC.01550-09. PubMed: 20308372.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 2312-2322
    • Scudiero, O.1    Galdiero, S.2    Cantisani, M.3    Di Noto, R.4    Vitiello, M.5
  • 42
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity
    • doi: 10.1016/S0005-2736(99)00199-6
    • Sitaram N, Nagaraj R, (1999) Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim Biophys Acta 1462: 29-54. doi:10.1016/S0005-2736(99)00199-6. PubMed: 10590301.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 43
    • 70350729306 scopus 로고    scopus 로고
    • Structure-dependent charge density as a determinant of antimicrobial activity of peptide analogues of defensin
    • doi: 10.1021/bi900670d
    • Bai Y, Liu S, Jiang P, Zhou L, Li J, et al. (2009) Structure-dependent charge density as a determinant of antimicrobial activity of peptide analogues of defensin. Biochemistry 48: 7229-7239. doi:10.1021/bi900670d. PubMed: 19580334.
    • (2009) Biochemistry , vol.48 , pp. 7229-7239
    • Bai, Y.1    Liu, S.2    Jiang, P.3    Zhou, L.4    Li, J.5
  • 44
    • 79952341527 scopus 로고    scopus 로고
    • Human beta-defensin 2 and beta-defensin 3 chimeric peptides reveal the structural basis of the pathogen specificity of their parent molecules
    • doi: 10.1128/AAC.00872-10
    • Jung S, Mysliwy J, Spudy B, Lorenzen I, Reiss K, et al. (2011) Human beta-defensin 2 and beta-defensin 3 chimeric peptides reveal the structural basis of the pathogen specificity of their parent molecules. Antimicrob Agents Chemother 55: 954-960. doi:10.1128/AAC.00872-10. PubMed: 21189349.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 954-960
    • Jung, S.1    Mysliwy, J.2    Spudy, B.3    Lorenzen, I.4    Reiss, K.5
  • 45
    • 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
    • doi: 10.1074/jbc.M108830200
    • Schibli DJ, Hunter HN, Aseyev V, Starner TD, Wiencek JM, et al. (2002) 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: 8279-8289. doi:10.1074/jbc.M108830200. PubMed: 11741980.
    • (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
  • 46
    • 78650129716 scopus 로고    scopus 로고
    • Interaction of human beta-defensin 2 (HBD2) with glycosaminoglycans
    • doi: 10.1021/bi1011749
    • Seo ES, Blaum BS, Vargues T, De Cecco M, Deakin JA, et al. (2010) Interaction of human beta-defensin 2 (HBD2) with glycosaminoglycans. Biochemistry 49: 10486-10495. doi:10.1021/bi1011749. PubMed: 21062008.
    • (2010) Biochemistry , vol.49 , pp. 10486-10495
    • Seo, E.S.1    Blaum, B.S.2    Vargues, T.3    De Cecco, M.4    Deakin, J.A.5
  • 47
    • 0034693159 scopus 로고    scopus 로고
    • The structure of human beta-defensin-2 shows evidence of higher order oligomerization
    • doi: 10.1074/jbc.M006098200
    • Hoover DM, Rajashankar KR, Blumenthal R, Puri A, Oppenheim JJ, et al. (2000) The structure of human beta-defensin-2 shows evidence of higher order oligomerization. J Biol Chem 275: 32911-32918. doi:10.1074/jbc.M006098200. PubMed: 10906336.
    • (2000) J Biol Chem , vol.275 , pp. 32911-32918
    • Hoover, D.M.1    Rajashankar, K.R.2    Blumenthal, R.3    Puri, A.4    Oppenheim, J.J.5
  • 48
    • 67650081577 scopus 로고    scopus 로고
    • Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue
    • doi: 10.1021/bi900154f
    • Chandrababu KB, Ho B, Yang D, (2009) Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue. Biochemistry 48: 6052-6061. doi:10.1021/bi900154f. PubMed: 19480463.
    • (2009) Biochemistry , vol.48 , pp. 6052-6061
    • Chandrababu, K.B.1    Ho, B.2    Yang, D.3
  • 49
    • 77952693839 scopus 로고    scopus 로고
    • Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci
    • doi: 10.1128/IAI.00688-09
    • Sass V, Schneider T, Wilmes M, Körner C, Tossi A, et al. (2010) Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci. Infect Immun 78: 2793-2800. doi:10.1128/IAI.00688-09. PubMed: 20385753.
    • (2010) Infect Immun , vol.78 , pp. 2793-2800
    • Sass, V.1    Schneider, T.2    Wilmes, M.3    Körner, C.4    Tossi, A.5
  • 50
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • doi: 10.1111/j.1574-6968.2002.tb11000.x
    • Hancock RE, Rozek A, (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol Lett 206: 143-149. doi:10.1111/j.1574-6968.2002.tb11000.x. PubMed: 11814654.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 143-149
    • Hancock, R.E.1    Rozek, A.2
  • 51
    • 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 RE, (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. doi:10.1021/bi9826299. PubMed: 10353835.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 52
    • 0036086590 scopus 로고    scopus 로고
    • Treponema denticola is resistant to human beta-defensins
    • doi: 10.1128/IAI.70.7.3982-3984.2002
    • Brissette CA, Lukehart SA, (2002) Treponema denticola is resistant to human beta-defensins. Infect Immun 70: 3982-3984. doi:10.1128/IAI.70.7.3982-3984.2002. PubMed: 12065549.
    • (2002) Infect Immun , vol.70 , pp. 3982-3984
    • Brissette, C.A.1    Lukehart, S.A.2
  • 53
    • 0036717730 scopus 로고    scopus 로고
    • Susceptibility of nontypeable Haemophilus influenzae to human beta-defensins is influenced by lipooligosaccharide acylation
    • doi: 10.1128/IAI.70.9.5287-5289.2002
    • Starner TD, Swords WE, Apicella MA, McCray PB Jr, (2002) Susceptibility of nontypeable Haemophilus influenzae to human beta-defensins is influenced by lipooligosaccharide acylation. Infect Immun 70: 5287-5289. doi:10.1128/IAI.70.9.5287-5289.2002. PubMed: 12183584.
    • (2002) Infect Immun , vol.70 , pp. 5287-5289
    • Starner, T.D.1    Swords, W.E.2    Apicella, M.A.3    McCray Jr., P.B.4
  • 54
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • doi: 10.1074/jbc.274.13.8405
    • Peschel A, Otto M, Jack RW, Kalbacher H, Jung G, et al. (1999) Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J Biol Chem 274: 8405-8410. doi:10.1074/jbc.274.13.8405. PubMed: 10085071.
    • (1999) J Biol Chem , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5
  • 55
    • 77951271759 scopus 로고    scopus 로고
    • Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II
    • doi: 10.1016/j.febslet.2010.03.004
    • de Leeuw E, Li C, Zeng P, Diepeveen-de Buin M, Lu WY, et al. (2010) Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II. FEBS Lett 584: 1543-1548. doi:10.1016/j.febslet.2010.03.004. PubMed: 20214904.
    • (2010) FEBS Lett , vol.584 , pp. 1543-1548
    • de Leeuw, E.1    Li, C.2    Zeng, P.3    Diepeveen-de Buin, M.4    Lu, W.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.