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Volumn 1788, Issue 9, 2009, Pages 1790-1796

Fungicidal effect of antimicrobial peptide arenicin-1

Author keywords

Antimicrobial peptide; Arenicin 1; Arenicola marina; Fungicidal effect; Membrane active mechanism

Indexed keywords

ARENICIN 1; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 68749087275     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.06.008     Document Type: Article
Times cited : (57)

References (50)
  • 1
    • 0033198883 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas
    • Relf J., Chisholm J., Kemp G., and Smith V. Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem. 264 (1999) 350-357
    • (1999) Eur. J. Biochem. , vol.264 , pp. 350-357
    • Relf, J.1    Chisholm, J.2    Kemp, G.3    Smith, V.4
  • 2
    • 0024838206 scopus 로고
    • The biological significance of immunity
    • Ratcliffe N.A. The biological significance of immunity. Dev. Comp. Immunol. 13 (1989) 273-283
    • (1989) Dev. Comp. Immunol. , vol.13 , pp. 273-283
    • Ratcliffe, N.A.1
  • 3
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusin I and II: chemical structures and biological activity
    • Miyata T., Tokunaga F., Yoneya T., Yoshikawa K., Iwanaga S., Niwa M., Takao T., and Shimonishi Y. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusin I and II: chemical structures and biological activity. Biochem. J. 106 (1989) 663-668
    • (1989) Biochem. J. , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6    Takao, T.7    Shimonishi, Y.8
  • 4
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus)
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., and Iwanaga S. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). J. Biol. Chem. 263 (1988) 16703-16713
    • (1988) J. Biol. Chem. , vol.263 , pp. 16703-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6
  • 5
    • 0031030885 scopus 로고    scopus 로고
    • Clavanins, α-helical antimicrobial peptides from tunicate hemocytes
    • Lee I., Zhao C., Cho Y., Harwig S., Cooper E., and Lehrer R. Clavanins, α-helical antimicrobial peptides from tunicate hemocytes. FEBS Lett 400 (1997) 158-162
    • (1997) FEBS Lett , vol.400 , pp. 158-162
    • Lee, I.1    Zhao, C.2    Cho, Y.3    Harwig, S.4    Cooper, E.5    Lehrer, R.6
  • 6
    • 0029810861 scopus 로고    scopus 로고
    • Innate immunity: isolation of several cystein-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis
    • Charlet M., Chernysh S., Philippe H., Hetru C., Hoffmann J.A., and Bulet P. Innate immunity: isolation of several cystein-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. J. Biol. Chem. 271 (1996) 21808-21813
    • (1996) J. Biol. Chem. , vol.271 , pp. 21808-21813
    • Charlet, M.1    Chernysh, S.2    Philippe, H.3    Hetru, C.4    Hoffmann, J.A.5    Bulet, P.6
  • 7
    • 0036071479 scopus 로고    scopus 로고
    • Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus
    • Bartlett T., Cuthbertson B.J., Shepard E., Chapman R., Gross P., and Warr G. Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar. Biotechnol. 4 (2002) 278-293
    • (2002) Mar. Biotechnol. , vol.4 , pp. 278-293
    • Bartlett, T.1    Cuthbertson, B.J.2    Shepard, E.3    Chapman, R.4    Gross, P.5    Warr, G.6
  • 11
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield R.B. Solid phase synthesis. Science 232 (1986) 341-347
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 12
    • 0031129664 scopus 로고    scopus 로고
    • Protein identification from 2-DE gels by MALDI mass spectrometry
    • Jungblut P., and Thiede B. Protein identification from 2-DE gels by MALDI mass spectrometry. Mass Spectrom. Rev. 16 (1997) 145-162
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 145-162
    • Jungblut, P.1    Thiede, B.2
  • 13
    • 0036291233 scopus 로고    scopus 로고
    • Antifungal mechanism of an antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1 against Candida albicans
    • Lee D.G., Park Y., Kim H.N., Kim H.K., Kim P.I., Choi B.H., and Hahm K.S. Antifungal mechanism of an antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1 against Candida albicans. Biochem. Biophys. Res. Commun. 291 (2002) 1006-1013
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 1006-1013
    • Lee, D.G.1    Park, Y.2    Kim, H.N.3    Kim, H.K.4    Kim, P.I.5    Choi, B.H.6    Hahm, K.S.7
  • 14
    • 0028817139 scopus 로고
    • Susceptibility testing of Candida albicans and Aspergillus species by a simple microtiter menadioneaugmented 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphynyl-2H-tetrazolium bromide assay
    • Jahn B., martin E., Stueben A., and Bhakdi S. Susceptibility testing of Candida albicans and Aspergillus species by a simple microtiter menadioneaugmented 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphynyl-2H-tetrazolium bromide assay. J. Clin. Microbiol. 33 (1995) 661-667
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 661-667
    • Jahn, B.1    martin, E.2    Stueben, A.3    Bhakdi, S.4
  • 15
    • 0031979493 scopus 로고    scopus 로고
    • Influence of test conditions on antifungal time-kill curve results: proposal for standardized methods
    • Klepser M.E., Ernst E.J., Lewis R.E., Ernst M.E., and Pfaller M.A. Influence of test conditions on antifungal time-kill curve results: proposal for standardized methods. Antimicrob. Agents Chemother. 42 (1998) 1207-1212
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1207-1212
    • Klepser, M.E.1    Ernst, E.J.2    Lewis, R.E.3    Ernst, M.E.4    Pfaller, M.A.5
  • 16
    • 2042454166 scopus 로고    scopus 로고
    • Determination of fungicidal activities against yeasts and molds: lessons learned from bactericidal testing and the need for standardization
    • Pfaller M.A., Sheehan D.J., and Rex J.H. Determination of fungicidal activities against yeasts and molds: lessons learned from bactericidal testing and the need for standardization. Clin. Microbiol. Rev. 17 (2004) 268-280
    • (2004) Clin. Microbiol. Rev. , vol.17 , pp. 268-280
    • Pfaller, M.A.1    Sheehan, D.J.2    Rex, J.H.3
  • 17
    • 36949028956 scopus 로고    scopus 로고
    • Damage to the cytoplasmic membrane and cell death caused by lycopene in Candida albicans
    • Sung W.S., Lee I.S., and Lee D.G. Damage to the cytoplasmic membrane and cell death caused by lycopene in Candida albicans. J. Microbiol. Biotechnol. 17 (2007) 1797-1804
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1797-1804
    • Sung, W.S.1    Lee, I.S.2    Lee, D.G.3
  • 18
    • 33646402378 scopus 로고    scopus 로고
    • Biological activity of Tat (47-58) peptide on human pathogenic fungi
    • Jung H.J., Park Y., Hahm K.S., and Lee D.G. Biological activity of Tat (47-58) peptide on human pathogenic fungi. Biochem. Biophys. Res. Commun. 345 (2006) 222-228
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 222-228
    • Jung, H.J.1    Park, Y.2    Hahm, K.S.3    Lee, D.G.4
  • 21
    • 0030876947 scopus 로고    scopus 로고
    • Rapid flow cytometric susceptibility testing of Candida albicans
    • Raman R., Ramani A., and Wong S.J. Rapid flow cytometric susceptibility testing of Candida albicans. J. Clin. Microbiol. 35 (1997) 2320-2324
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 2320-2324
    • Raman, R.1    Ramani, A.2    Wong, S.J.3
  • 22
    • 0030667206 scopus 로고    scopus 로고
    • A yeast mutant showing diagnostic markers of early and late apoptosis
    • Madeo F., Fröhlich E., and Fröhlich K.U. A yeast mutant showing diagnostic markers of early and late apoptosis. J. Cell Biol. 139 (1997) 729-734
    • (1997) J. Cell Biol. , vol.139 , pp. 729-734
    • Madeo, F.1    Fröhlich, E.2    Fröhlich, K.U.3
  • 23
    • 58549098767 scopus 로고    scopus 로고
    • Isocryptomerin, a novel membrane-active antifungal compound from Selaginella tamariscina
    • Lee J., Choi Y., Woo E.R., and Lee D.G. Isocryptomerin, a novel membrane-active antifungal compound from Selaginella tamariscina. Biochem. Biophys. Res. Commun. 379 (2009) 676-680
    • (2009) Biochem. Biophys. Res. Commun. , vol.379 , pp. 676-680
    • Lee, J.1    Choi, Y.2    Woo, E.R.3    Lee, D.G.4
  • 24
    • 0027953945 scopus 로고
    • Mode of action of the antibacterial cecropin B2: a sepctrofluorometric study
    • Grazit E., Lee W.J., Brey P.T., and Shai Y. Mode of action of the antibacterial cecropin B2: a sepctrofluorometric study. Biochemistry 33 (1994) 10681-10692
    • (1994) Biochemistry , vol.33 , pp. 10681-10692
    • Grazit, E.1    Lee, W.J.2    Brey, P.T.3    Shai, Y.4
  • 25
    • 34248993592 scopus 로고    scopus 로고
    • Fungicidal effect of pleurocidin by membrane-active mechanism and design of enatiomeric analogue for proteolytic resistance
    • Jung H.J., Park Y., Sung W.S., Suh B.K., Lee J., Hahm K.S., and Lee D.G. Fungicidal effect of pleurocidin by membrane-active mechanism and design of enatiomeric analogue for proteolytic resistance. Biochim. Biophys. Acta Biomembr. 1768 (2007) 1400-1405
    • (2007) Biochim. Biophys. Acta Biomembr. , vol.1768 , pp. 1400-1405
    • Jung, H.J.1    Park, Y.2    Sung, W.S.3    Suh, B.K.4    Lee, J.5    Hahm, K.S.6    Lee, D.G.7
  • 26
    • 38149030149 scopus 로고    scopus 로고
    • Amphipathic α-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions
    • Park S.C., Kim M.H., Hossain M.A., Shin S.Y., Kim Y., Stella L., Wade J.D., Park Y., and Hahm K.S. Amphipathic α-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions. Biochim. Biophys. Acta Biomembr. 1778 (2008) 229-241
    • (2008) Biochim. Biophys. Acta Biomembr. , vol.1778 , pp. 229-241
    • Park, S.C.1    Kim, M.H.2    Hossain, M.A.3    Shin, S.Y.4    Kim, Y.5    Stella, L.6    Wade, J.D.7    Park, Y.8    Hahm, K.S.9
  • 29
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki K., Yoneyama S., and Miyajima K. Pore formation and translocation of melittin. Biophys. J. 73 (1997) 831-838
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 30
    • 0344630224 scopus 로고    scopus 로고
    • Apoptosis induced by environmental stresses and amphotericin B in Candida albicans
    • Phillips A.J., Sudbery I., and Ramsdale M. Apoptosis induced by environmental stresses and amphotericin B in Candida albicans. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 14327-14332
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14327-14332
    • Phillips, A.J.1    Sudbery, I.2    Ramsdale, M.3
  • 31
    • 0034541844 scopus 로고    scopus 로고
    • Changes in external trehalase activity during human serum-induced dimorphic transition in Candida albicans
    • Alvarez-Peral F.J., and Arguelles J.C. Changes in external trehalase activity during human serum-induced dimorphic transition in Candida albicans. Res. Microbiol. 151 (2000) 837-843
    • (2000) Res. Microbiol. , vol.151 , pp. 837-843
    • Alvarez-Peral, F.J.1    Arguelles, J.C.2
  • 33
    • 0032169024 scopus 로고    scopus 로고
    • Regulation of intracellular pH during H+-coupled oligopeptide absorption in enterocytes from Guinea-pig ileum
    • Hayashi H., and Suzuki Y. Regulation of intracellular pH during H+-coupled oligopeptide absorption in enterocytes from Guinea-pig ileum. J. Physiol. 511 (1998) 573-586
    • (1998) J. Physiol. , vol.511 , pp. 573-586
    • Hayashi, H.1    Suzuki, Y.2
  • 35
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462 (1999) 1-10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 37
    • 0035522314 scopus 로고    scopus 로고
    • Cytometric approach for a rapid evaluation of susceptibility of Candida strains to antifungals
    • Pina-Vaz C., Sansonetty F., and Rodrigues A.G. Cytometric approach for a rapid evaluation of susceptibility of Candida strains to antifungals. Clin. Microbiol. Infect. 7 (2001) 609-618
    • (2001) Clin. Microbiol. Infect. , vol.7 , pp. 609-618
    • Pina-Vaz, C.1    Sansonetty, F.2    Rodrigues, A.G.3
  • 38
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 39
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 40
    • 47249135720 scopus 로고    scopus 로고
    • Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide
    • Lee J.Y., Lee S.T., Lee S.K., Jung H.H., Shin S.Y., Hahm K.S., and Kim J.I. Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide. FEBS J. 275 (2008) 3911-3920
    • (2008) FEBS J. , vol.275 , pp. 3911-3920
    • Lee, J.Y.1    Lee, S.T.2    Lee, S.K.3    Jung, H.H.4    Shin, S.Y.5    Hahm, K.S.6    Kim, J.I.7
  • 41
    • 0037184958 scopus 로고    scopus 로고
    • Correlations of cationic charges with salt sensitivity and microbial specificity of cystine-stabilized beta-strand antimicrobial peptides
    • Tam J.P., Lu Y.A., and Yang J.L. Correlations of cationic charges with salt sensitivity and microbial specificity of cystine-stabilized beta-strand antimicrobial peptides. J. Biol. Chem. 277 (2002) 50450-50456
    • (2002) J. Biol. Chem. , vol.277 , pp. 50450-50456
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 42
    • 23944500330 scopus 로고    scopus 로고
    • Controlled alteration of the shape and conformational stability of α-helical cell-lytic peptides: effect on mode of action and cell specificity
    • Zelezetsky I., Pacor S., Pag U., Papo N., Shai Y., Sahl H.-G., and Tossi A. Controlled alteration of the shape and conformational stability of α-helical cell-lytic peptides: effect on mode of action and cell specificity. Biochem. J. 390 (2005) 177-188
    • (2005) Biochem. J. , vol.390 , pp. 177-188
    • Zelezetsky, I.1    Pacor, S.2    Pag, U.3    Papo, N.4    Shai, Y.5    Sahl, H.-G.6    Tossi, A.7
  • 44
    • 2942585398 scopus 로고    scopus 로고
    • Cytoplasmic membrane polarization in Gram-positive and Gram-negative bacteria grown in the absence and presence of tetracycline
    • Vincent M., England L.S., and Trevors J.T. Cytoplasmic membrane polarization in Gram-positive and Gram-negative bacteria grown in the absence and presence of tetracycline. Biochim. Biophys. Acta 1672 (2004) 131-134
    • (2004) Biochim. Biophys. Acta , vol.1672 , pp. 131-134
    • Vincent, M.1    England, L.S.2    Trevors, J.T.3
  • 45
    • 0022104096 scopus 로고
    • Membrane structural domains; resolution limits using diphenylhexatriene fluorescence decay
    • Barrow D.A., and Lentz B.R. Membrane structural domains; resolution limits using diphenylhexatriene fluorescence decay. Biophys. J. 48 (1985) 221-234
    • (1985) Biophys. J. , vol.48 , pp. 221-234
    • Barrow, D.A.1    Lentz, B.R.2
  • 46
    • 22244489401 scopus 로고    scopus 로고
    • pH-dependent antifungal lipopeptides and their plausible mode of action
    • Makovitzki A., and Shai Y. pH-dependent antifungal lipopeptides and their plausible mode of action. Biochemistry 44 (2005) 9775-9784
    • (2005) Biochemistry , vol.44 , pp. 9775-9784
    • Makovitzki, A.1    Shai, Y.2
  • 47
    • 0001378233 scopus 로고    scopus 로고
    • Giant vesicles : imitating the cytological processes of cell membranes
    • Menger F.M., and Angelova M.I. Giant vesicles : imitating the cytological processes of cell membranes. Acc. Chem. Res. 31 (1998) 789-797
    • (1998) Acc. Chem. Res. , vol.31 , pp. 789-797
    • Menger, F.M.1    Angelova, M.I.2
  • 48
    • 0032248006 scopus 로고    scopus 로고
    • Chemistry and physics of giant vesicles as biomembrane models
    • Menger F.M., and Keiper J.S. Chemistry and physics of giant vesicles as biomembrane models. Curr. Opin. Chem. Biol. 2 (1998) 726-732
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 726-732
    • Menger, F.M.1    Keiper, J.S.2
  • 49
    • 34247626376 scopus 로고    scopus 로고
    • method reveals interaction of tea catechin (-)-epigallocatechin gallate with lipid membranes
    • Tamba Y., Ohba S., Kubota M., Yoshioka H., Yamazaki M., and Single G. method reveals interaction of tea catechin (-)-epigallocatechin gallate with lipid membranes. Biophys. J. 97 (2007) 3178-3194
    • (2007) Biophys. J. , vol.97 , pp. 3178-3194
    • Tamba, Y.1    Ohba, S.2    Kubota, M.3    Yoshioka, H.4    Yamazaki, M.5    Single, G.6
  • 50
    • 0037337245 scopus 로고    scopus 로고
    • Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3
    • Chen H.M., Leung K.W., Thakur N.N., Tan A., and Jack R.W. Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3. Eur. J. Biochem. 270 (2003) 911-920
    • (2003) Eur. J. Biochem. , vol.270 , pp. 911-920
    • Chen, H.M.1    Leung, K.W.2    Thakur, N.N.3    Tan, A.4    Jack, R.W.5


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