메뉴 건너뛰기




Volumn 237, Issue 3, 2012, Pages 312-317

Synthesis and secretory expression of hybrid antimicrobial peptide CecA-mag and its mutants in Pichia pastoris

Author keywords

Bacteriostatic activity; Hybrid antimicrobial peptide CecA mag; Pichia pastoris secretary expression

Indexed keywords

ALCOHOL OXIDASE; AMINO ACID; CECROPIN A; HYBRID PROTEIN;

EID: 84863369257     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.1258/ebm.2011.011153     Document Type: Article
Times cited : (10)

References (24)
  • 1
    • 0018820115 scopus 로고
    • Insect immunity purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark D, Steiner H, Rasmusson T, Boman HG. Insect immunity purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur J Biochem 1980;106:7-16
    • (1980) Eur J Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmusson, T.3    Boman, H.G.4
  • 3
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engstrom A, Bennich H, Boman HG. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981;292:246-8
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 4
    • 69949177644 scopus 로고    scopus 로고
    • Isolation of antifungal peptides from hemolymph of housefly larvae by gel filtration
    • Zhang Y, Wu J, Gu L. Isolation of antifungal peptides from hemolymph of housefly larvae by gel filtration. Chin J Vector Biol Control 2007;18:200-4
    • (2007) Chin J Vector Biol Control , vol.18 , pp. 200-204
    • Zhang, Y.1    Wu, J.2    Gu, L.3
  • 5
    • 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;84:5449-53
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 6
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • Zasloff M, Martin B, Chen H. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc Natl Acad Sci USA 1988;85:910-3
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.3
  • 7
    • 84863382684 scopus 로고    scopus 로고
    • Potential therapeutic applications of magainins and other antimicrobial agents of animal origin
    • In: Marsh J, Goode JA, eds, Chichester, UK: John Wiley & Sons,. DOI: 10.1002/9780470514658.ch12
    • Jacob L, Zasloff M. Potential therapeutic applications of magainins and other antimicrobial agents of animal origin. In: Marsh J, Goode JA, eds. Ciba Foundation Symposium 186-Antimicrobial Peptides. Chichester, UK: John Wiley & Sons, 1997. DOI: 10.1002/9780470514658.ch12
    • (1997) Ciba Foundation Symposium 186-Antimicrobial Peptides
    • Jacob, L.1    Zasloff, M.2
  • 8
    • 0343666850 scopus 로고
    • Use of genes encoding novel lytic peptides and proteins that enhance microbial disease resistance in plants
    • Jaynes JM. Use of genes encoding novel lytic peptides and proteins that enhance microbial disease resistance in plants. ISHS Acta Hort 1993;336:33-9
    • (1993) ISHS Acta Hort , vol.336 , pp. 33-39
    • Jaynes, J.M.1
  • 9
    • 0024392058 scopus 로고
    • Design, synthesis and antibacterial activity of cecropin-like model peptides
    • Fink J, Boman A, Boman HG, Merrifield RB. Design, synthesis and antibacterial activity of cecropin-like model peptides. Int J Pept Protein Res 1989;33:412-21
    • (1989) Int J Pept Protein Res , vol.33 , pp. 412-421
    • Fink, J.1    Boman, A.2    Boman, H.G.3    Merrifield, R.B.4
  • 10
    • 84863361253 scopus 로고    scopus 로고
    • A simple and efficient modified touchdown PCR
    • Wang T, Zhang G, Xue L. A simple and efficient modified touchdown PCR. Prog Biotechnol 2003;23:80-2
    • (2003) Prog Biotechnol , vol.23 , pp. 80-82
    • Wang, T.1    Zhang, G.2    Xue, L.3
  • 12
    • 34249050938 scopus 로고    scopus 로고
    • Comparison of four methods to prepare pichia genomic DNA for PCR
    • Ju H, Liang D, Guo G, Zhang J. Comparison of four methods to prepare pichia genomic DNA for PCR. Tianjing Med J 2003;31:270-2
    • (2003) Tianjing Med J , vol.31 , pp. 270-272
    • Ju, H.1    Liang, D.2    Guo, G.3    Zhang, J.4
  • 13
    • 79958075175 scopus 로고    scopus 로고
    • Expression of Cecropin B in Pichia pastoris and its bioactivity in vitro
    • Wang X, Zhu M, Yang G, Zhang A, Yang F, Chen P. Expression of Cecropin B in Pichia pastoris and its bioactivity in vitro. Exp Ther Med 2011;2:655-60
    • (2011) Exp Ther Med , vol.2 , pp. 655-660
    • Wang, X.1    Zhu, M.2    Yang, G.3    Zhang, A.4    Yang, F.5    Chen, P.6
  • 14
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100KD
    • Schagger H, Von Jagow G. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100KD. Anal Biochem 1987;166:368-79
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 15
    • 42649107142 scopus 로고    scopus 로고
    • Iron regulatory and bactericidal properties of human recombinant hepcidin expressed in
    • Koliaraki V, Marinou M, Samiotaki M. Iron regulatory and bactericidal properties of human recombinant hepcidin expressed in Pichia pastoris. Biochimie 2008;90:726-35
    • (2008) Pichia pastoris. Biochimie , vol.90 , pp. 726-735
    • Koliaraki, V.1    Marinou, M.2    Samiotaki, M.3
  • 16
    • 0032752132 scopus 로고    scopus 로고
    • Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria
    • Scott MG, Gold Michael R, Hancock Robert EW. Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria. Infect Immun 1999;67:6445-53
    • (1999) Infect Immun , vol.67 , pp. 6445-6453
    • Scott, M.G.1    Gold Michael, R.2    Hancock Robert, E.W.3
  • 17
  • 18
    • 0030583613 scopus 로고    scopus 로고
    • Determination of the disulfide array of the first inducible antifungal peptide from insects: Drosomycin from Drosophila melanogaster
    • Michaut L, Fehlbaum P, Moniatte M, Van Dorsselaer A, Reichhart J-M, Bulet P. Determination of the disulfide array of the first inducible antifungal peptide from insects: drosomycin from Drosophila melanogaster. FEBS Lett 1996;395:6-10
    • (1996) FEBS Lett , vol.395 , pp. 6-10
    • Michaut, L.1    Fehlbaum, P.2    Moniatte, M.3    van Dorsselaer, A.4    Reichhart, J-M.5    Bulet, P.6
  • 19
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes
    • Saberwalg G, Nagaraj R. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes. Biochim Biophys Acta 1994;1197:109-31
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 109-131
    • Saberwalg, G.1    Nagaraj, R.2
  • 20
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Yechiel S. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1999;1462:55-70
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Yechiel, S.1
  • 22
    • 0034684272 scopus 로고    scopus 로고
    • Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism
    • Ibrahim HR, Sugimoto Y, Aoki T. Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim Biophys Acta 2000;1523:196-205
    • (2000) Biochim Biophys Acta , vol.1523 , pp. 196-205
    • Ibrahim, H.R.1    Sugimoto, Y.2    Aoki, T.3
  • 23
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melitin and alamethicin
    • Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melitin and alamethicin. Mem Biol 1997;156:197-211
    • (1997) Mem Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 24
    • 0034960109 scopus 로고    scopus 로고
    • The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity
    • Yang D, Chertov O, Oppenheim JJ. The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity. Cell Mol Life Sci 2001;58:978-89
    • (2001) Cell Mol Life Sci , vol.58 , pp. 978-989
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.