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Volumn 114, Issue 4, 2012, Pages 365-370

Next generation of antimicrobial peptides as molecular targeted medicines

Author keywords

Activity regulation; Antibiotic; Antimicrobial peptide; Defensin; Drug delivery; Specifically targeted antimicrobial peptides (STAMPs)

Indexed keywords

ACTIVITY REGULATION; ANTI-MICROBIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; BROAD SPECTRUM; CONVENTIONAL DRUGS; DEFENSINS; GRAM-NEGATIVE BACTERIA; HEMOLYTIC ACTIVITY; HUMAN BODIES; INTEGRAL PART; LIVING ENVIRONMENT; MICROBIOTAS; MICROFLORA; MUCOSAL SURFACE; NOVEL ANTIBIOTICS; PATHOGENIC ORGANISMS; QUALITY-OF-LIFE;

EID: 84865973489     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.05.001     Document Type: Review
Times cited : (62)

References (89)
  • 1
    • 62449089680 scopus 로고    scopus 로고
    • Microbial drug discovery: 80 years of progress
    • Demain A.L., Sanchez S. Microbial drug discovery: 80 years of progress. J. Antibiot. 2009, 62:5-16.
    • (2009) J. Antibiot. , vol.62 , pp. 5-16
    • Demain, A.L.1    Sanchez, S.2
  • 2
    • 84964134387 scopus 로고
    • Streptomycin, a substance exhibiting antibiotic activity against gram-positive and gram-negative bacteria
    • Schatz A., Bugie E., Waksman S.A. Streptomycin, a substance exhibiting antibiotic activity against gram-positive and gram-negative bacteria. Exp. Biol. Med. 1944, 55:66-69.
    • (1944) Exp. Biol. Med. , vol.55 , pp. 66-69
    • Schatz, A.1    Bugie, E.2    Waksman, S.A.3
  • 3
    • 33646799069 scopus 로고    scopus 로고
    • Global and regional burden of disease and risk factors, 2001: systematic analysis of population health data
    • Lopez A.D., Mathers C.D., Ezzati M., Jamison D.T., Murray C.J. Global and regional burden of disease and risk factors, 2001: systematic analysis of population health data. Lancet 2006, 367:1747-1757.
    • (2006) Lancet , vol.367 , pp. 1747-1757
    • Lopez, A.D.1    Mathers, C.D.2    Ezzati, M.3    Jamison, D.T.4    Murray, C.J.5
  • 4
    • 0028955432 scopus 로고
    • Molecular mechanisms of multiple drug resistance in clinical isolates of Mycobacterium tuberculosis
    • Morris S., Bai G.H., Suffys P., Portillo-Gomez L., Fairchok M., Rouse D. Molecular mechanisms of multiple drug resistance in clinical isolates of Mycobacterium tuberculosis. J. Infect. Dis. 1995, 171:954-960.
    • (1995) J. Infect. Dis. , vol.171 , pp. 954-960
    • Morris, S.1    Bai, G.H.2    Suffys, P.3    Portillo-Gomez, L.4    Fairchok, M.5    Rouse, D.6
  • 5
    • 0026705492 scopus 로고
    • Epidemiology of drug resistance: implications for a post-antimicrobial era
    • Cohen M.L. Epidemiology of drug resistance: implications for a post-antimicrobial era. Science 1992, 257:1050-1055.
    • (1992) Science , vol.257 , pp. 1050-1055
    • Cohen, M.L.1
  • 7
    • 0031566835 scopus 로고    scopus 로고
    • Dissemination in Japanese hospitals of strains of Staphylococcus aureus heterogeneously resistant to vancomycin
    • Hiramatsu K., Aritaka N., Hanaki H., Kawasaki S., Hosoda Y., Hori S., Fukuchi Y., Kobayashi I. Dissemination in Japanese hospitals of strains of Staphylococcus aureus heterogeneously resistant to vancomycin. Lancet 1997, 350:1670-1673.
    • (1997) Lancet , vol.350 , pp. 1670-1673
    • Hiramatsu, K.1    Aritaka, N.2    Hanaki, H.3    Kawasaki, S.4    Hosoda, Y.5    Hori, S.6    Fukuchi, Y.7    Kobayashi, I.8
  • 8
    • 0037084298 scopus 로고    scopus 로고
    • Linezolid: its role in the treatment of gram-positive, drug-resistant bacterial infections
    • Ament P.W., Jamshed N., Horne J.P. Linezolid: its role in the treatment of gram-positive, drug-resistant bacterial infections. Am. Fam. Physician 2002, 65:663-670.
    • (2002) Am. Fam. Physician , vol.65 , pp. 663-670
    • Ament, P.W.1    Jamshed, N.2    Horne, J.P.3
  • 10
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 1987, 84:5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 11
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: an overview of a promising class of therapeutics
    • Giuliani A., Pirri G., Nicoletto S.F. Antimicrobial peptides: an overview of a promising class of therapeutics. Cent. Eur. J. Biol. 2007, 2:1-33.
    • (2007) Cent. Eur. J. Biol. , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.F.3
  • 12
    • 0000010840 scopus 로고    scopus 로고
    • Antifungal spectrum and fungicidal mechanism of an N-terminal peptide of bovine lactoferrin
    • Wakabayashi H., Hiratani T., Uchida K., Yamaguch H. Antifungal spectrum and fungicidal mechanism of an N-terminal peptide of bovine lactoferrin. J. Infect. Chemother. 1996, 1:185-189.
    • (1996) J. Infect. Chemother. , vol.1 , pp. 185-189
    • Wakabayashi, H.1    Hiratani, T.2    Uchida, K.3    Yamaguch, H.4
  • 13
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi K., Tomita M., Giehl T.J., Ellison R.T. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 1993, 61:719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 15
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1999, 1462:157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 16
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • Mani R., Cady S.D., Tang M., Waring A.J., Lehrer R.I., Hong M. Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR. Proc. Natl. Acad. Sci. USA 2006, 103:16242-16247.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Tang, M.3    Waring, A.J.4    Lehrer, R.I.5    Hong, M.6
  • 17
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties
    • Gifford J.L., Hunter H.N., Vogel H.J. Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell Mol. Life Sci. 2005, 62:2588-2598.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 18
    • 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
  • 19
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen L.T., Haney E.F., Vogel H.J. The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 2011, 29:464-472.
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 20
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 22
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1999, 1462:71-87.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 23
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • Matsuzaki K., Sugishita K., Fujii N., Miyajima K. Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. Biochemistry 1995, 34:3423-3429.
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 24
    • 0033569682 scopus 로고    scopus 로고
    • Defensins and host defense
    • Ganz T. Defensins and host defense. Science 1999, 286:420-421.
    • (1999) Science , vol.286 , pp. 420-421
    • Ganz, T.1
  • 25
    • 0033229628 scopus 로고    scopus 로고
    • Prophylactic Lactobacillus GG reduces antibiotic-associated diarrhea in children with respiratory infections: a randomized study
    • Arvola T., Laiho K., Torkkeli S., Mykkanen H., Salminen S., Maunula L., Isolauri E. Prophylactic Lactobacillus GG reduces antibiotic-associated diarrhea in children with respiratory infections: a randomized study. Pediatrics 1999, 104:e64.
    • (1999) Pediatrics , vol.104
    • Arvola, T.1    Laiho, K.2    Torkkeli, S.3    Mykkanen, H.4    Salminen, S.5    Maunula, L.6    Isolauri, E.7
  • 26
  • 27
    • 0025981915 scopus 로고
    • Role of Candida in pathogenesis of antibiotic-associated diarrhoea in elderly inpatients
    • Danna P.L., Urban C., Bellin E., Rahal J.J. Role of Candida in pathogenesis of antibiotic-associated diarrhoea in elderly inpatients. Lancet 1991, 337:511-514.
    • (1991) Lancet , vol.337 , pp. 511-514
    • Danna, P.L.1    Urban, C.2    Bellin, E.3    Rahal, J.J.4
  • 28
    • 0035433592 scopus 로고    scopus 로고
    • Antibiotic-associated diarrhea and Clostridium difficile colitis: an update
    • Giannella R.A. Antibiotic-associated diarrhea and Clostridium difficile colitis: an update. Rev. Esp. Enferm. Dig. 2001, 93:535-543.
    • (2001) Rev. Esp. Enferm. Dig. , vol.93 , pp. 535-543
    • Giannella, R.A.1
  • 29
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E., Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24:1551-1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 30
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown K.L., Hancock R.E. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 2006, 18:24-30.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 34
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman M.J., Anderson G.M., Stolzenberg E.D., Kari U.P., Zasloff M., Wilson J.M. Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997, 88:553-560.
    • (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    Wilson, J.M.6
  • 35
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study
    • Putsep K., Carlsson G., Boman H.G., Andersson M. Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 2002, 360:1144-1149.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 36
    • 58149252357 scopus 로고    scopus 로고
    • Host defense peptides in the oral cavity and the lung: similarities and differences
    • Diamond G., Beckloff N., Ryan L.K. Host defense peptides in the oral cavity and the lung: similarities and differences. J. Dent. Res. 2008, 87:915-927.
    • (2008) J. Dent. Res. , vol.87 , pp. 915-927
    • Diamond, G.1    Beckloff, N.2    Ryan, L.K.3
  • 37
    • 22944435825 scopus 로고    scopus 로고
    • Antimicrobial peptides in the oral environment: expression and function in health and disease
    • Dale B.A., Fredericks L.P. Antimicrobial peptides in the oral environment: expression and function in health and disease. Curr. Issues Mol. Biol. 2005, 7:119-133.
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 119-133
    • Dale, B.A.1    Fredericks, L.P.2
  • 38
    • 69149102398 scopus 로고    scopus 로고
    • Antimicrobial peptides of the oral cavity
    • Gorr S.-U. Antimicrobial peptides of the oral cavity. Periodontology 2000 2009, 51:152-180.
    • (2009) Periodontology 2000 , vol.51 , pp. 152-180
    • Gorr, S.-U.1
  • 39
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • Ganz T. Defensins: antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 2003, 3:710-720.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 41
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang Y.Q., Yuan J., Osapay G., Osapay K., Tran D., Miller C.J., Ouellette A.J., Selsted M.E. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 1999, 286:498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 45
    • 0033405818 scopus 로고    scopus 로고
    • The individual regulation of granule protein mRNA levels during neutrophil maturation explains the heterogeneity of neutrophil granules
    • Cowland J.B., Borregaard N. The individual regulation of granule protein mRNA levels during neutrophil maturation explains the heterogeneity of neutrophil granules. J. Leukoc. Biol. 1999, 66:989-995.
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 989-995
    • Cowland, J.B.1    Borregaard, N.2
  • 46
    • 0028847478 scopus 로고
    • Rat neutrophil defensins. Precursor structures and expression during neutrophilic myelopoiesis
    • Yount N.Y., Wang M.S., Yuan J., Banaiee N., Ouellette A.J., Selsted M.E. Rat neutrophil defensins. Precursor structures and expression during neutrophilic myelopoiesis. J. Immunol. 1995, 155:4476-4484.
    • (1995) J. Immunol. , vol.155 , pp. 4476-4484
    • Yount, N.Y.1    Wang, M.S.2    Yuan, J.3    Banaiee, N.4    Ouellette, A.J.5    Selsted, M.E.6
  • 48
    • 0023098960 scopus 로고
    • Extracellular release of antimicrobial defensins by human polymorphonuclear leukocytes
    • Ganz T. Extracellular release of antimicrobial defensins by human polymorphonuclear leukocytes. Infect. Immun. 1987, 55:568-571.
    • (1987) Infect. Immun. , vol.55 , pp. 568-571
    • Ganz, T.1
  • 49
    • 0026765474 scopus 로고
    • Defensins: microbicidal and cytotoxic peptides of mammalian host defense cells
    • Ganz T., Oren A., Lehrer R.I. Defensins: microbicidal and cytotoxic peptides of mammalian host defense cells. Med. Microbiol. Immunol. 1992, 181:99-105.
    • (1992) Med. Microbiol. Immunol. , vol.181 , pp. 99-105
    • Ganz, T.1    Oren, A.2    Lehrer, R.I.3
  • 50
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • Faurschou M., Borregaard N. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect. 2003, 5:1317-1327.
    • (2003) Microbes Infect. , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 51
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengelov H., Kjeldsen L., Borregaard N. Control of exocytosis in early neutrophil activation. J. Immunol. 1993, 150:1535-1543.
    • (1993) J. Immunol. , vol.150 , pp. 1535-1543
    • Sengelov, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 52
    • 1542513868 scopus 로고    scopus 로고
    • Human beta-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms
    • Joly S., Maze C., McCray P.B., Guthmiller J.M. Human beta-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms. J. Clin. Microbiol. 2004, 42:1024-1029.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 1024-1029
    • Joly, S.1    Maze, C.2    McCray, P.B.3    Guthmiller, J.M.4
  • 54
    • 0036121584 scopus 로고    scopus 로고
    • Immunohistochemical study on expression of alpha-defensin and beta-defensin-2 in human buccal epithelia with candidiasis
    • Sawaki K., Mizukawa N., Yamaai T., Fukunaga J., Sugahara T. Immunohistochemical study on expression of alpha-defensin and beta-defensin-2 in human buccal epithelia with candidiasis. Oral Dis. 2002, 8:37-41.
    • (2002) Oral Dis. , vol.8 , pp. 37-41
    • Sawaki, K.1    Mizukawa, N.2    Yamaai, T.3    Fukunaga, J.4    Sugahara, T.5
  • 55
    • 0346881404 scopus 로고    scopus 로고
    • Innate immune response of oral and foreskin keratinocytes: utilization of different signaling pathways by various bacterial species
    • Chung W.O., Dale B.A. Innate immune response of oral and foreskin keratinocytes: utilization of different signaling pathways by various bacterial species. Infect. Immun. 2004, 72:352-358.
    • (2004) Infect. Immun. , vol.72 , pp. 352-358
    • Chung, W.O.1    Dale, B.A.2
  • 56
    • 0037218616 scopus 로고    scopus 로고
    • By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide
    • Liu L., Roberts A.A., Ganz T. By IL-1 signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide. J. Immunol. 2003, 170:575-580.
    • (2003) J. Immunol. , vol.170 , pp. 575-580
    • Liu, L.1    Roberts, A.A.2    Ganz, T.3
  • 58
    • 0038189571 scopus 로고    scopus 로고
    • Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors
    • Sorensen O.E., Cowland J.B., Theilgaard-Monch K., Liu L., Ganz T., Borregaard N. Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors. J. Immunol. 2003, 170:5583-5589.
    • (2003) J. Immunol. , vol.170 , pp. 5583-5589
    • Sorensen, O.E.1    Cowland, J.B.2    Theilgaard-Monch, K.3    Liu, L.4    Ganz, T.5    Borregaard, N.6
  • 59
    • 0031913244 scopus 로고    scopus 로고
    • Mouse beta-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract
    • Bals R., Goldman M.J., Wilson J.M. Mouse beta-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract. Infect. Immun. 1998, 66:1225-1232.
    • (1998) Infect. Immun. , vol.66 , pp. 1225-1232
    • Bals, R.1    Goldman, M.J.2    Wilson, J.M.3
  • 60
    • 26644469527 scopus 로고    scopus 로고
    • Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes
    • Glukhov E., Stark M., Burrows L.L., Deber C.M. Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes. J. Biol. Chem. 2005, 280:33960-33967.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33960-33967
    • Glukhov, E.1    Stark, M.2    Burrows, L.L.3    Deber, C.M.4
  • 61
    • 33748941585 scopus 로고    scopus 로고
    • Interactions of bovine lactoferricin with acidic phospholipid bilayers and its antimicrobial activity as studied by solid-state NMR
    • Umeyama M., Kira A., Nishimura K., Naito A. Interactions of bovine lactoferricin with acidic phospholipid bilayers and its antimicrobial activity as studied by solid-state NMR. Biochim. Biophys. Acta 2006, 1758:1523-1528.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1523-1528
    • Umeyama, M.1    Kira, A.2    Nishimura, K.3    Naito, A.4
  • 63
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981, 292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 64
  • 65
    • 79956000536 scopus 로고    scopus 로고
    • Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides
    • Juretic D., Vukicevic D., Petrov D., Novkovic M., Bojovic V., Lucic B., Ilic N., Tossi A. Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides. Eur. Biophys. J. 2011, 40:371-385.
    • (2011) Eur. Biophys. J. , vol.40 , pp. 371-385
    • Juretic, D.1    Vukicevic, D.2    Petrov, D.3    Novkovic, M.4    Bojovic, V.5    Lucic, B.6    Ilic, N.7    Tossi, A.8
  • 67
    • 24644515282 scopus 로고    scopus 로고
    • Overview of nosocomial infections caused by gram-negative bacilli
    • Gaynes R., Edwards J.R. Overview of nosocomial infections caused by gram-negative bacilli. Clin. Infect. Dis. 2005, 41:848-854.
    • (2005) Clin. Infect. Dis. , vol.41 , pp. 848-854
    • Gaynes, R.1    Edwards, J.R.2
  • 68
    • 77952298917 scopus 로고    scopus 로고
    • Hospital-acquired infections due to gram-negative bacteria
    • Peleg A.Y., Hooper D.C. Hospital-acquired infections due to gram-negative bacteria. N. Engl. J. Med. 2010, 362:1804-1813.
    • (2010) N. Engl. J. Med. , vol.362 , pp. 1804-1813
    • Peleg, A.Y.1    Hooper, D.C.2
  • 69
    • 79952980526 scopus 로고    scopus 로고
    • Structures of beta-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance
    • Su Y., Waring A.J., Ruchala P., Hong M. Structures of beta-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance. Biochemistry 2011, 50:2072-2083.
    • (2011) Biochemistry , vol.50 , pp. 2072-2083
    • Su, Y.1    Waring, A.J.2    Ruchala, P.3    Hong, M.4
  • 70
    • 0035873909 scopus 로고    scopus 로고
    • Design of Gram-negative selective antimicrobial peptides
    • Muhle S.A., Tam J.P. Design of Gram-negative selective antimicrobial peptides. Biochemistry 2001, 40:5777-5785.
    • (2001) Biochemistry , vol.40 , pp. 5777-5785
    • Muhle, S.A.1    Tam, J.P.2
  • 71
    • 0034665513 scopus 로고    scopus 로고
    • An alpha-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression
    • Scott M.G., Rosenberger C.M., Gold M.R., Finlay B.B., Hancock R.E. An alpha-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression. J. Immunol. 2000, 165:3358-3365.
    • (2000) J. Immunol. , vol.165 , pp. 3358-3365
    • Scott, M.G.1    Rosenberger, C.M.2    Gold, M.R.3    Finlay, B.B.4    Hancock, R.E.5
  • 72
    • 0024454751 scopus 로고
    • Apidaecins: antibacterial peptides from honeybees
    • Casteels P., Ampe C., Jacobs F., Vaeck M., Tempst P. Apidaecins: antibacterial peptides from honeybees. EMBO J. 1989, 8:2387-2391.
    • (1989) EMBO J. , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Vaeck, M.4    Tempst, P.5
  • 74
    • 77954725852 scopus 로고    scopus 로고
    • Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens
    • Knappe D., Piantavigna S., Hansen A., Mechler A., Binas A., Nolte O., Martin L.L., Hoffmann R. Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens. J. Med. Chem. 2010, 53:5240-5247.
    • (2010) J. Med. Chem. , vol.53 , pp. 5240-5247
    • Knappe, D.1    Piantavigna, S.2    Hansen, A.3    Mechler, A.4    Binas, A.5    Nolte, O.6    Martin, L.L.7    Hoffmann, R.8
  • 75
    • 0032808386 scopus 로고    scopus 로고
    • Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes
    • Shamova O., Brogden K.A., Zhao C., Nguyen T., Kokryakov V.N., Lehrer R.I. Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes. Infect. Immun. 1999, 67:4106-4111.
    • (1999) Infect. Immun. , vol.67 , pp. 4106-4111
    • Shamova, O.1    Brogden, K.A.2    Zhao, C.3    Nguyen, T.4    Kokryakov, V.N.5    Lehrer, R.I.6
  • 76
    • 77951236068 scopus 로고    scopus 로고
    • Systematic approach to optimizing specifically targeted antimicrobial peptides against Streptococcus mutans
    • He J., Yarbrough D.K., Kreth J., Anderson M.H., Shi W., Eckert R. Systematic approach to optimizing specifically targeted antimicrobial peptides against Streptococcus mutans. Antimicrob. Agents Chemother. 2010, 54:2143-2151.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2143-2151
    • He, J.1    Yarbrough, D.K.2    Kreth, J.3    Anderson, M.H.4    Shi, W.5    Eckert, R.6
  • 77
    • 33645767676 scopus 로고    scopus 로고
    • Adding selectivity to antimicrobial peptides: rational design of a multidomain peptide against Pseudomonas spp.
    • Eckert R., Qi F., Yarbrough D.K., He J., Anderson M.H., Shi W. Adding selectivity to antimicrobial peptides: rational design of a multidomain peptide against Pseudomonas spp. Antimicrob. Agents Chemother. 2006, 50:1480-1488.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1480-1488
    • Eckert, R.1    Qi, F.2    Yarbrough, D.K.3    He, J.4    Anderson, M.H.5    Shi, W.6
  • 78
    • 2442715491 scopus 로고    scopus 로고
    • Virulence properties of Streptococcus mutans
    • Banas J.A. Virulence properties of Streptococcus mutans. Front Biosci. 2004, 9:1267-1277.
    • (2004) Front Biosci. , vol.9 , pp. 1267-1277
    • Banas, J.A.1
  • 79
    • 0022993292 scopus 로고
    • Role of Streptococcus mutans in human dental decay
    • Loesche W.J. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 1986, 50:353-380.
    • (1986) Microbiol. Rev. , vol.50 , pp. 353-380
    • Loesche, W.J.1
  • 80
    • 33750584025 scopus 로고    scopus 로고
    • Targeted killing of Streptococcus mutans by a pheromone-guided " smart" antimicrobial peptide
    • Eckert R., He J., Yarbrough D.K., Qi F., Anderson M.H., Shi W. Targeted killing of Streptococcus mutans by a pheromone-guided " smart" antimicrobial peptide. Antimicrob. Agents Chemother. 2006, 50:3651-3657.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3651-3657
    • Eckert, R.1    He, J.2    Yarbrough, D.K.3    Qi, F.4    Anderson, M.H.5    Shi, W.6
  • 81
    • 79953894994 scopus 로고    scopus 로고
    • Targeted antimicrobial therapy against Streptococcus mutans establishes protective non-cariogenic oral biofilms and reduces subsequent infection
    • Li L.N., Guo L.H., Lux R., Eckert R., Yarbrough D., He J., Anderson M., Shi W.Y. Targeted antimicrobial therapy against Streptococcus mutans establishes protective non-cariogenic oral biofilms and reduces subsequent infection. Int. J. Oral. Sci. 2010, 2:66-73.
    • (2010) Int. J. Oral. Sci. , vol.2 , pp. 66-73
    • Li, L.N.1    Guo, L.H.2    Lux, R.3    Eckert, R.4    Yarbrough, D.5    He, J.6    Anderson, M.7    Shi, W.Y.8
  • 82
    • 0037901299 scopus 로고    scopus 로고
    • Multiple stress responses in Streptococcus mutans and the induction of general and stress-specific proteins
    • Svensater G., Sjogreen B., Hamilton I.R. Multiple stress responses in Streptococcus mutans and the induction of general and stress-specific proteins. Microbiology 2000, 146:107-117.
    • (2000) Microbiology , vol.146 , pp. 107-117
    • Svensater, G.1    Sjogreen, B.2    Hamilton, I.R.3
  • 83
    • 0031030885 scopus 로고    scopus 로고
    • Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes
    • Lee I.H., Zhao C., Cho Y., Harwig S.S., Cooper E.L., Lehrer R.I. Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes. FEBS Lett. 1997, 400:158-162.
    • (1997) FEBS Lett. , vol.400 , pp. 158-162
    • Lee, I.H.1    Zhao, C.2    Cho, Y.3    Harwig, S.S.4    Cooper, E.L.5    Lehrer, R.I.6
  • 85
    • 0024423057 scopus 로고
    • Correlation between culture medium pH, extracellular proteinase activity, and cell growth of Candida albicans in insoluble stratum corneum-supplemented media
    • Tsuboi R., Matsuda K., Ko I.J., Ogawa H. Correlation between culture medium pH, extracellular proteinase activity, and cell growth of Candida albicans in insoluble stratum corneum-supplemented media. Arch. Dermatol. Res. 1989, 281:342-345.
    • (1989) Arch. Dermatol. Res. , vol.281 , pp. 342-345
    • Tsuboi, R.1    Matsuda, K.2    Ko, I.J.3    Ogawa, H.4
  • 86
    • 67649262183 scopus 로고    scopus 로고
    • Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin
    • Gottler L.M., Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin. Biochim. Biophys. Acta 2009, 1788:1680-1686.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 87
    • 0033979588 scopus 로고    scopus 로고
    • Site-specific polymer-streptavidin bioconjugate for pH-controlled binding and triggered release of biotin
    • Bulmus V., Ding Z., Long C.J., Stayton P.S., Hoffman A.S. Site-specific polymer-streptavidin bioconjugate for pH-controlled binding and triggered release of biotin. Bioconjug. Chem. 2000, 11:78-83.
    • (2000) Bioconjug. Chem. , vol.11 , pp. 78-83
    • Bulmus, V.1    Ding, Z.2    Long, C.J.3    Stayton, P.S.4    Hoffman, A.S.5
  • 88
    • 0035834259 scopus 로고    scopus 로고
    • Modulated insulin delivery from glucose-sensitive hydrogel dosage forms
    • Kim J.J., Park K. Modulated insulin delivery from glucose-sensitive hydrogel dosage forms. J. Control. Release 2001, 77:39-47.
    • (2001) J. Control. Release , vol.77 , pp. 39-47
    • Kim, J.J.1    Park, K.2
  • 89
    • 60849123435 scopus 로고    scopus 로고
    • Smart polymers for controlled delivery of proteins and peptides: a review of patents
    • Fogueri L.R., Singh S. Smart polymers for controlled delivery of proteins and peptides: a review of patents. Recent Pat. Drug Deliv. Formul. 2009, 3:40-48.
    • (2009) Recent Pat. Drug Deliv. Formul. , vol.3 , pp. 40-48
    • Fogueri, L.R.1    Singh, S.2


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