메뉴 건너뛰기




Volumn 400, Issue 3, 2010, Pages 352-357

Antifungal properties and mode of action of psacotheasin, a novel knottin-type peptide derived from Psacothea hilaris

Author keywords

Antifungal activity; Antifungal peptide; Membrane active mechanism; Psacothea hilaris; Psacotheasin

Indexed keywords

ANTIFUNGAL AGENT; DEXTRAN; LIPOSOME; POLYPEPTIDE ANTIBIOTIC AGENT; PSACOTHEASIN; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; PEPTIDE; PSACOTHEASIN PEPTIDE, PSACOTHEA HILARIS;

EID: 77956934522     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.08.063     Document Type: Article
Times cited : (37)

References (40)
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 2001, 1:156-164.
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 3
    • 46749108538 scopus 로고    scopus 로고
    • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides
    • Jiang Z., Vasil A.I., Hale J.D., Hancock R.E., Vasil M.L., Hodges R.S. Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides. Biopolymers 2008, 90:369-383.
    • (2008) Biopolymers , vol.90 , pp. 369-383
    • Jiang, Z.1    Vasil, A.I.2    Hale, J.D.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 4
    • 11344267777 scopus 로고    scopus 로고
    • Insect antimicrobial peptides: structures, properties and gene regulation
    • Bulet P., Stöcklin R. Insect antimicrobial peptides: structures, properties and gene regulation. Protein Pept. Lett. 2005, 12:3-11.
    • (2005) Protein Pept. Lett. , vol.12 , pp. 3-11
    • Bulet, P.1    Stöcklin, R.2
  • 6
    • 77954999999 scopus 로고    scopus 로고
    • Isolation and characterization of psacotheasin, a novel knottin-type antimicrobial peptide, from Psacothea hilaris
    • Hwang J.S., Lee J., Hwang B., Nam S.H., Yun E.Y., Kim S.R., Lee D.G. Isolation and characterization of psacotheasin, a novel knottin-type antimicrobial peptide, from Psacothea hilaris. J. Microbiol. Biotechnol. 2010, 20:708-711.
    • (2010) J. Microbiol. Biotechnol. , vol.20 , pp. 708-711
    • Hwang, J.S.1    Lee, J.2    Hwang, B.3    Nam, S.H.4    Yun, E.Y.5    Kim, S.R.6    Lee, D.G.7
  • 8
    • 70349414437 scopus 로고    scopus 로고
    • Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins
    • Kolmar H. Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins. Curr. Opin. Pharmacol. 2009, 9:608-614.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 608-614
    • Kolmar, H.1
  • 9
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield R.B. Solid phase synthesis. Science 1986, 232:341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 10
    • 0141838723 scopus 로고    scopus 로고
    • The fluorenylmethoxycarbonyl group in solid phase synthesis
    • Sheppard R. The fluorenylmethoxycarbonyl group in solid phase synthesis. J. Pept. Sci. 2003, 9:545-552.
    • (2003) J. Pept. Sci. , vol.9 , pp. 545-552
    • Sheppard, R.1
  • 11
    • 0031129664 scopus 로고    scopus 로고
    • Protein identification from 2-DE gels by MALDI mass spectrometry
    • Jungblut P., Thiede B. Protein identification from 2-DE gels by MALDI mass spectrometry. Mass Spectrom. Rev. 1997, 16:145-162.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 145-162
    • Jungblut, P.1    Thiede, B.2
  • 12
    • 77956932050 scopus 로고    scopus 로고
    • Clinical and Laboratory Standards Institute Performance Standards for Antimicrobial Susceptibility Testing, Fifteenth Informational Supplement, Approved Standard MS100-S15, CLSI, Wayne, PA,
    • Clinical and Laboratory Standards Institute Performance Standards for Antimicrobial Susceptibility Testing, Fifteenth Informational Supplement, Approved Standard MS100-S15, CLSI, Wayne, PA, 2005.
    • (2005)
  • 13
    • 0028817139 scopus 로고
    • Susceptibility testing of Candida albicans and Aspergillus species by a simple microtiter menadione-augmented 3-(4, 5-dimethyl-2-thiazolyl)-2, 5-diphynyl-2H-tetrazolium bromide assay
    • Jahn B., Martin E., Stueben A., Bhakdi S. Susceptibility testing of Candida albicans and Aspergillus species by a simple microtiter menadione-augmented 3-(4, 5-dimethyl-2-thiazolyl)-2, 5-diphynyl-2H-tetrazolium bromide assay. J. Clin. Microbiol. 1995, 33:661-667.
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 661-667
    • Jahn, B.1    Martin, E.2    Stueben, A.3    Bhakdi, S.4
  • 15
    • 41149103818 scopus 로고    scopus 로고
    • Pleurocidin-derived antifungal peptides with selective membrane-disruption effect, Biochem. Biophys. Res. Commun.
    • W.S. Sung, D.G. Lee, Pleurocidin-derived antifungal peptides with selective membrane-disruption effect, Biochem. Biophys. Res. Commun. 369 (2008) 858-861.
    • (2008) , vol.369 , pp. 858-861
    • Sung, W.S.1    Lee, D.G.2
  • 16
    • 45549086415 scopus 로고    scopus 로고
    • Antimicrobial effect and membrane-active mechanism of Urechistachykinins, neuropeptides derived from Urechis unicinctus
    • Sung W.S., Park S.H., Lee D.G. Antimicrobial effect and membrane-active mechanism of Urechistachykinins, neuropeptides derived from Urechis unicinctus. FEBS Lett. 2008, 582:2463-2466.
    • (2008) FEBS Lett. , vol.582 , pp. 2463-2466
    • Sung, W.S.1    Park, S.H.2    Lee, D.G.3
  • 17
    • 0030876947 scopus 로고    scopus 로고
    • Rapid flow cytometric susceptibility testing of Candida albicans
    • Ramani R., Ramani A., Wong S.J. Rapid flow cytometric susceptibility testing of Candida albicans. J. Clin. Microbiol. 1997, 35:2320-2324.
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 2320-2324
    • Ramani, R.1    Ramani, A.2    Wong, S.J.3
  • 18
    • 68749087275 scopus 로고    scopus 로고
    • Fungicidal effect of antimicrobial peptide arenicin-1
    • Park C., Lee D.G. Fungicidal effect of antimicrobial peptide arenicin-1. Biochim. Biophys. Acta 2009, 1788:1790-1796.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1790-1796
    • Park, C.1    Lee, D.G.2
  • 19
    • 72949093131 scopus 로고    scopus 로고
    • A novel antifungal analog peptide derived from Protaetiamycine
    • Lee J., Hong H.J., Kim J.K., Hwang J.S., Kim Y., Lee D.G. A novel antifungal analog peptide derived from Protaetiamycine. Mol. Cells 2009, 28:473-477.
    • (2009) Mol. Cells , vol.28 , pp. 473-477
    • Lee, J.1    Hong, H.J.2    Kim, J.K.3    Hwang, J.S.4    Kim, Y.5    Lee, D.G.6
  • 21
    • 45449126405 scopus 로고
    • Lipid swelling and liposome formation mediated by electric fields
    • Dimitrov D.S., Angelova M.I. Lipid swelling and liposome formation mediated by electric fields. J. Electroanal. Chem. 1988, 253:323-336.
    • (1988) J. Electroanal. Chem. , vol.253 , pp. 323-336
    • Dimitrov, D.S.1    Angelova, M.I.2
  • 23
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • Habermann E. Bee and wasp venoms. Science 1972, 177:314-322.
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 24
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • Lee M.T., Hung W.C., Chen F.Y., Huang H.W. Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides. Proc. Natl. Acad. Sci. USA 2008, 105:5087-5092.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5087-5092
    • Lee, M.T.1    Hung, W.C.2    Chen, F.Y.3    Huang, H.W.4
  • 25
    • 70449658983 scopus 로고    scopus 로고
    • Postantibiotic effect of purified melittin from honeybee (Apis mellifera) venom against Escherichia coli and Staphylococcus aureus
    • Han S., Yeo J., Baek H., Lin S.M., Meyer S., Molan P. Postantibiotic effect of purified melittin from honeybee (Apis mellifera) venom against Escherichia coli and Staphylococcus aureus. J. Asian Nat. Prod. Res. 2009, 11:796-804.
    • (2009) J. Asian Nat. Prod. Res. , vol.11 , pp. 796-804
    • Han, S.1    Yeo, J.2    Baek, H.3    Lin, S.M.4    Meyer, S.5    Molan, P.6
  • 26
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: a membrane-active peptide with diverse functions
    • Raghuraman H., Chattopadhyay A. Melittin: a membrane-active peptide with diverse functions. Biosci. Rep. 2007, 27:189-223.
    • (2007) Biosci. Rep. , vol.27 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 27
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999, 1462:11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 28
    • 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
  • 29
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: two-state model
    • Huang H.W. Action of antimicrobial peptides: two-state model. Biochemistry 2000, 39:8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 30
    • 27144503650 scopus 로고    scopus 로고
    • Alternative Candida albicans lifestyle: growth on surfaces
    • Kumamoto C.A., Vinces M.D. Alternative Candida albicans lifestyle: growth on surfaces. Annu. Rev. Microbiol. 2005, 59:113-133.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 113-133
    • Kumamoto, C.A.1    Vinces, M.D.2
  • 31
    • 0032960631 scopus 로고    scopus 로고
    • Assessment of the effect of amphotericin B on the vitality of Candida albicans
    • Liao R.S., Rennie R.P., Talbot J.A. Assessment of the effect of amphotericin B on the vitality of Candida albicans. Antimicrob. Agents Chemother. 1999, 43:1034-1041.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1034-1041
    • Liao, R.S.1    Rennie, R.P.2    Talbot, J.A.3
  • 32
    • 33646003271 scopus 로고    scopus 로고
    • A flow cytometric assay to monitor antimicrobial activity of defensins and cationic tissue extracts
    • Nuding S., Fellermann K., Wehkamp J., Mueller H.A., Stange E.F. A flow cytometric assay to monitor antimicrobial activity of defensins and cationic tissue extracts. J. Microbiol. Methods 2006, 65:335-345.
    • (2006) J. Microbiol. Methods , vol.65 , pp. 335-345
    • Nuding, S.1    Fellermann, K.2    Wehkamp, J.3    Mueller, H.A.4    Stange, E.F.5
  • 34
    • 23944500330 scopus 로고    scopus 로고
    • Controlled alteration of the shape and conformational stability of alpha-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., Tossi A. Controlled alteration of the shape and conformational stability of alpha-helical cell-lytic peptides: effect on mode of action and cell specificity. Biochem. J. 2005, 390:177-188.
    • (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
  • 35
    • 0036736465 scopus 로고    scopus 로고
    • Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: implications for systemic use
    • Pacor S., Giangaspero A., Bacac M., Sava G., Tossi A. Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: implications for systemic use. J. Antimicrob. Chemother. 2002, 50:339-348.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 339-348
    • Pacor, S.1    Giangaspero, A.2    Bacac, M.3    Sava, G.4    Tossi, A.5
  • 36
    • 28544437689 scopus 로고    scopus 로고
    • Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability
    • Tamba Y., Yamazaki M. Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability. Biochemistry 2005, 44:15823-15833.
    • (2005) Biochemistry , vol.44 , pp. 15823-15833
    • Tamba, Y.1    Yamazaki, M.2
  • 37
    • 67249136866 scopus 로고    scopus 로고
    • Giant unilamellar vesicles - a perfect tool to visualize phase separation and lipid rafts in model systems
    • Wesołowska O., Michalak K., Maniewska J., Hendrich A.B. Giant unilamellar vesicles - a perfect tool to visualize phase separation and lipid rafts in model systems. Acta Biochim. Pol. 2009, 56:33-39.
    • (2009) Acta Biochim. Pol. , vol.56 , pp. 33-39
    • Wesołowska, O.1    Michalak, K.2    Maniewska, J.3    Hendrich, A.B.4
  • 38
    • 22244489401 scopus 로고    scopus 로고
    • PH-dependent antifungal lipopeptides and their plausible mode of action
    • Makovitzki A., Shai Y. PH-dependent antifungal lipopeptides and their plausible mode of action. Biochemistry 2005, 44:9775-9784.
    • (2005) Biochemistry , vol.44 , pp. 9775-9784
    • Makovitzki, A.1    Shai, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.