메뉴 건너뛰기




Volumn 40, Issue 2, 2005, Pages 404-410

Expression and purification of antimicrobial peptide adenoregulin with C-amidated terminus in Escherichia coli

Author keywords

Adenoregulin; Antimicrobial peptide; C amidated terminus; Escherichia coli; Expression

Indexed keywords


EID: 14844333166     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.12.007     Document Type: Article
Times cited : (41)

References (25)
  • 1
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antimicrobial activity
    • J.S. Powers, and R.E.W. Hancock The relationship between peptide structure and antimicrobial activity Peptides 24 2003 1681 1691
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.S.1    Hancock, R.E.W.2
  • 2
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 3
    • 1542315480 scopus 로고    scopus 로고
    • In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin
    • H. Saido-Sakanaka, J. Ishibashi, and E. Momotani In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin Peptides 25 2004 19 27
    • (2004) Peptides , vol.25 , pp. 19-27
    • Saido-Sakanaka, H.1    Ishibashi, J.2    Momotani, E.3
  • 4
    • 2942592590 scopus 로고    scopus 로고
    • Inactivation of virus infecting ectothermic animals by amphibian and piscine antimicrobial peptides
    • V.G. Chinchar, L. Bryan, and U. Silphadaung Inactivation of virus infecting ectothermic animals by amphibian and piscine antimicrobial peptides Virology 323 2004 268 275
    • (2004) Virology , vol.323 , pp. 268-275
    • Chinchar, V.G.1    Bryan, L.2    Silphadaung, U.3
  • 5
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • R.E.W. Hancock Peptide antibiotics Lancet 349 1997 418 422
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 6
    • 0026493568 scopus 로고
    • Frog secretions and hunting magic in the upper Amazon: Identification of a peptide that interacts with an adenosine receptor
    • J.W. Daly, J. Caceres, and R.W. Moni Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor Proc. Natl. Acad. Sci. USA 89 1992 10960 10963
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10960-10963
    • Daly, J.W.1    Caceres, J.2    Moni, R.W.3
  • 7
    • 0037147330 scopus 로고    scopus 로고
    • Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta
    • G.D. Brand Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta J. Biol. Chem. 277 2002 49332 49340
    • (2002) J. Biol. Chem. , vol.277 , pp. 49332-49340
    • Brand, G.D.1
  • 8
    • 0031465747 scopus 로고    scopus 로고
    • Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic plasmodium falciparum and the underlying molecular basis
    • J.K. Ghosh, D. Shaool, and P. Guillaud Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic plasmodium falciparum and the underlying molecular basis J. Biol. Chem. 272 1997 31609 31616
    • (1997) J. Biol. Chem. , vol.272 , pp. 31609-31616
    • Ghosh, J.K.1    Shaool, D.2    Guillaud, P.3
  • 9
    • 0034635367 scopus 로고    scopus 로고
    • Structure-activity relationship study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity
    • R. Feder, A. Dagan, and A. Mor Structure-activity relationship study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity J. Biol. Chem. 275 2000 4230 4238
    • (2000) J. Biol. Chem. , vol.275 , pp. 4230-4238
    • Feder, R.1    Dagan, A.2    Mor, A.3
  • 10
    • 0032498840 scopus 로고    scopus 로고
    • Synthetic, antimicrobial activity and gene structure of a novel member of the dermaseptin B family
    • Y. Fleury, and Veronique Synthetic, antimicrobial activity and gene structure of a novel member of the dermaseptin B family Biochim. Biophys. Acta 1396 1998 228 236
    • (1998) Biochim. Biophys. Acta , vol.1396 , pp. 228-236
    • Fleury, Y.1    Veronique2
  • 11
    • 0027204174 scopus 로고
    • Molecular cloning of a cDNA encoding the precursor of adenoregulin from frog skin
    • M. Amiche, F. Ducancel, and E. Lajeunesse Molecular cloning of a cDNA encoding the precursor of adenoregulin from frog skin Biochem. Biophys. Res. Commun. 191 1993 983 990
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 983-990
    • Amiche, M.1    Ducancel, F.2    Lajeunesse, E.3
  • 12
    • 0028240042 scopus 로고
    • Structure, synthesis and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: Relationship with adenoregulin
    • A. Mor, M. Amiche, and P. Nicolas Structure, synthesis and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin Biochemistry 33 1994 6642 6650
    • (1994) Biochemistry , vol.33 , pp. 6642-6650
    • Mor, A.1    Amiche, M.2    Nicolas, P.3
  • 13
    • 0028225882 scopus 로고
    • Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins
    • M. Amiche, F. Ducancal, and A. Mort Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins J. Biol. Chem. 269 1994 17847 17852
    • (1994) J. Biol. Chem. , vol.269 , pp. 17847-17852
    • Amiche, M.1    Ducancal, F.2    Mort, A.3
  • 14
    • 0025944451 scopus 로고
    • Biologically active and amidated cecropin produced in a baculovirus expression system from a fusion construct containing the antibody-binding part of protein a
    • D. Andersons, and A. Engstrom Biologically active and amidated cecropin produced in a baculovirus expression system from a fusion construct containing the antibody-binding part of protein A Biochem. J. 280 1991 219 224
    • (1991) Biochem. J. , vol.280 , pp. 219-224
    • Andersons, D.1    Engstrom, A.2
  • 15
    • 14844283088 scopus 로고    scopus 로고
    • Effects of the terminal structure of antimicrobial peptide CMIV on the activity
    • F. Dou, W. Xie, and X. Dong Effects of the terminal structure of antimicrobial peptide CMIV on the activity Science China (Series C) 30 2000 59 64
    • (2000) Science China (Series C) , vol.30 , pp. 59-64
    • Dou, F.1    Xie, W.2    Dong, X.3
  • 16
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • H. Schagger, and G. von Jagow Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 17
    • 1842587737 scopus 로고    scopus 로고
    • Design of novel analogues with potent antibiotic activity based on the antimicrobial peptide, HP(2-9)-ME(1-12)
    • Y. Park, H.N. Kim, and S.N. Park Design of novel analogues with potent antibiotic activity based on the antimicrobial peptide, HP(2-9)-ME(1-12) Biotechnol. Lett. 26 2004 493 498
    • (2004) Biotechnol. Lett. , vol.26 , pp. 493-498
    • Park, Y.1    Kim, H.N.2    Park, S.N.3
  • 18
    • 0030813755 scopus 로고    scopus 로고
    • Size-exclusion high-performance liquid chromatography of peptides: A review
    • G.B. Irvine Size-exclusion high-performance liquid chromatography of peptides: a review Anal. Chim. Acta 352 1997 387 397
    • (1997) Anal. Chim. Acta , vol.352 , pp. 387-397
    • Irvine, G.B.1
  • 19
    • 0034597709 scopus 로고    scopus 로고
    • High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies
    • J.H. Lee, J.H. Kim, and S.W. Hwang High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies Biochem. Biophys. Res. Commun. 277 2000 575 580
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 575-580
    • Lee, J.H.1    Kim, J.H.2    Hwang, S.W.3
  • 20
    • 0032006495 scopus 로고    scopus 로고
    • Acid peptide-mediated expression of the antimicrobial peptide Buforin II as tandem repeats in Escherichia coli
    • J.H. Lee, H. Minn, C.B. Park, and S.C. Kim Acid peptide-mediated expression of the antimicrobial peptide Buforin II as tandem repeats in Escherichia coli Protein Expr. Purif. 12 1998 53 60
    • (1998) Protein Expr. Purif. , vol.12 , pp. 53-60
    • Lee, J.H.1    Minn, H.2    Park, C.B.3    Kim, S.C.4
  • 21
    • 0032577940 scopus 로고    scopus 로고
    • Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria
    • L. Zhang, T. Falla, and M. Wu Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria Biochem. Biophys. Res. Commun. 247 1998 674 680
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 674-680
    • Zhang, L.1    Falla, T.2    Wu, M.3
  • 22
    • 3042545322 scopus 로고    scopus 로고
    • A novel carrier molecule for high-level expression of peptide antibiotics in Escherichia coli
    • X.C. Rao, and S. Li A novel carrier molecule for high-level expression of peptide antibiotics in Escherichia coli Protein Expr. Purif. 36 2004 11 18
    • (2004) Protein Expr. Purif. , vol.36 , pp. 11-18
    • Rao, X.C.1    Li, S.2
  • 23
    • 0023644485 scopus 로고
    • Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Surcophugu peregrinu
    • Y. Nakajima, and X. Qu Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Surcophugu peregrinu J. Biol. Chem. 262 1987 1665 1669
    • (1987) J. Biol. Chem. , vol.262 , pp. 1665-1669
    • Nakajima, Y.1    Qu, X.2
  • 24
    • 0027988532 scopus 로고
    • The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms
    • A. Mor, K. Hani, and P. Nicolas The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms J. Biol. Chem. 269 1994 31635 31641
    • (1994) J. Biol. Chem. , vol.269 , pp. 31635-31641
    • Mor, A.1    Hani, K.2    Nicolas, P.3
  • 25
    • 0028174888 scopus 로고
    • 2-terminal α-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity
    • 2-terminal α-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity J. Biol. Chem. 269 1994 1934 1939
    • (1994) J. Biol. Chem. , vol.269 , pp. 1934-1939
    • Mor, A.1    Nicolas, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.