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Volumn 263, Issue 3, 1999, Pages 921-927

Expression and activity of cyclic and linear analogues of esculentin-1, an anti-microbial peptide from amphibian skin

Author keywords

Anti microbial peptide; Inclusion bodies; Intramolecular disulfide; Peptide expression; Salt inactivation

Indexed keywords

ANTIINFECTIVE AGENT; ESCULENTIN 1; ESCULENTIN 1 DERIVATIVE; INORGANIC SALT; MUTANT PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0033178536     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00597.x     Document Type: Article
Times cited : (57)

References (26)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • 1. Boman, H.G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immun. 13, 61-92.
    • (1995) Annu. Rev. Immun. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • 2. Lehrer, R.I. & Ganz, T. (1999) Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11, 23-27.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 3
    • 0025761657 scopus 로고
    • Cytolytic pore-forming proteins and peptides: Is there a common structural motifs?
    • 3. Ojcius, D.M. & Young, J.D. (1991) Cytolytic pore-forming proteins and peptides: is there a common structural motifs? Trends Biochem. Sci. 16, 225-229.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 225-229
    • Ojcius, D.M.1    Young, J.D.2
  • 4
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • 4. Shai, Y. (1995) Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20, 460-464.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 5
    • 0032014842 scopus 로고    scopus 로고
    • The challenge of antibiotic resistance
    • March issue
    • 5. Levy, S.B. (1998) The challenge of antibiotic resistance. Scientific American, March issue, pp. 32-39.
    • (1998) Scientific American , pp. 32-39
    • Levy, S.B.1
  • 6
    • 0027445909 scopus 로고    scopus 로고
    • 1993 Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria
    • 6. Piers, K.L., Brown, M.H. & Hancock, R.E. (1993) Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria. Gene 134, 7-13.
    • Gene , vol.134 , pp. 7-13
    • Piers, K.L.1    Brown, M.H.2    Hancock, R.E.3
  • 7
    • 0032006495 scopus 로고    scopus 로고
    • Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli
    • 7. Lee, J.H., Minn, I., Park, C.B. & Kim, S.C. (1998) Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli. Protein Expr. Purif. 12, 53-60.
    • (1998) Protein Expr. Purif. , vol.12 , pp. 53-60
    • Lee, J.H.1    Minn, I.2    Park, C.B.3    Kim, S.C.4
  • 8
    • 0032577940 scopus 로고    scopus 로고
    • Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria
    • 8. Zhang, L., Falla, T., Wu, M., Fidai, S., Burian, J., Kay, W. & Hancock, R.E. (1998) Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria. Biochem. Biophys. Res. Commun. 247, 674-680.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 674-680
    • Zhang, L.1    Falla, T.2    Wu, M.3    Fidai, S.4    Burian, J.5    Kay, W.6    Hancock, R.E.7
  • 9
    • 0028364262 scopus 로고
    • Antimicrobial peptides from skin secretion of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides
    • 9. Simmaco, M., Mignogna, G., Barra, D. & Bossa, F. (1994) Antimicrobial peptides from skin secretion of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. J. Biol. Chem. 269, 11956-11961.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11956-11961
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3    Bossa, F.4
  • 10
    • 0028832108 scopus 로고
    • Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase
    • 10. De Biase, D., Barra, D., Simmaco, M., John, R.A. & Bossa, F. (1995) Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur. J. Biochem. 227, 476-480.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 476-480
    • De Biase, D.1    Barra, D.2    Simmaco, M.3    John, R.A.4    Bossa, F.5
  • 11
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • 11. Marston, F.A. (1986) The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240, 1-12.
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.1
  • 12
    • 0032560497 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and innate immunity. Do 'animalcules' have defence budgets?
    • 12. Barra, D., Simmaco, M. & Boman, H.G. (1998) Gene-encoded peptide antibiotics and innate immunity. Do 'animalcules' have defence budgets? FEBS Lett. 430, 130-134.
    • (1998) FEBS Lett. , vol.430 , pp. 130-134
    • Barra, D.1    Simmaco, M.2    Boman, H.G.3
  • 13
    • 0020686109 scopus 로고
    • Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia
    • 13. Hultmark, D., Engström, A., Andersson, K., Steiner, H., Bennich, H. & Boman, H.G. (1983) Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 2, 571-576.
    • (1983) EMBO J. , vol.2 , pp. 571-576
    • Hultmark, D.1    Engström, A.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 14
    • 0027370683 scopus 로고
    • Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata
    • 14. Mignogna, G., Simmaco, M., Kreil, G. & Barra, D. (1993) Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. EMBO J. 12, 4829-4832.
    • (1993) EMBO J. , vol.12 , pp. 4829-4832
    • Mignogna, G.1    Simmaco, M.2    Kreil, G.3    Barra, D.4
  • 15
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
    • 15. Lehrer, R.I., Barton, A. & Ganz, T. (1988) Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry. J. Immunol. Methods 108, 153-158.
    • (1988) J. Immunol. Methods , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 16
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • 16. Shine, J. & Dalgarno, L. (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl Acad. Sci. USA 71, 1342-1346.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 17
    • 0020480282 scopus 로고
    • Characterization of translational initiation sites in E. coli
    • 17. Stormo, G.D., Schneider, T.D. & Gold, L.M. (1982) Characterization of translational initiation sites in E. coli. Nucleic Acids Res. 10, 2971-2996.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2971-2996
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.M.3
  • 18
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • 18. Luo, P. & Baldwin, R.L. (1997) Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36, 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 19
    • 0014955318 scopus 로고
    • In vivo degradation of nonsense fragments in E. coli
    • 19. Goldschmidt, R. (1970) In vivo degradation of nonsense fragments in E. coli. Nature 228, 1151-1154.
    • (1970) Nature , vol.228 , pp. 1151-1154
    • Goldschmidt, R.1
  • 20
    • 0015500749 scopus 로고
    • β-Galactosidase. Rates of synthesis and degradation of incomplete chains
    • 20. Lin, S. & Zabin, I. (1972) β-Galactosidase. Rates of synthesis and degradation of incomplete chains. J. Biol, Chem. 247, 2206-2211.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2206-2211
    • Lin, S.1    Zabin, I.2
  • 21
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • 21. Guan, C., Riggs, P.D. & Inouye, H. (1987) Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67, 21-30.
    • (1987) Gene , vol.67 , pp. 21-30
    • Guan, C.1    Riggs, P.D.2    Inouye, H.3
  • 22
    • 0030792188 scopus 로고    scopus 로고
    • Simultaneous production of the 34-kDa and 40-kDa proteins from Bacillus thuringiensis subsp. thompsoni is required for the formation of inclusion bodies
    • 22. Rang, C., Bes, M., Moar, W.J. & Frutos, R. (1997) Simultaneous production of the 34-kDa and 40-kDa proteins from Bacillus thuringiensis subsp. thompsoni is required for the formation of inclusion bodies. FEBS Lett. 412, 587-591.
    • (1997) FEBS Lett. , vol.412 , pp. 587-591
    • Rang, C.1    Bes, M.2    Moar, W.J.3    Frutos, R.4
  • 24
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • 24. Wu, M. & Hancock, R.E.W. (1999) Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274, 29-35.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29-35
    • Wu, M.1    Hancock, R.E.W.2
  • 25
    • 0029831079 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations
    • 25. Harwig, S.L., Waring, A., Yang, H.J., Cho, Y., Tan, L. & Lehrer, R. (1996) Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations. Eur. J. Biochem. 240, 352-357.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 352-357
    • Harwig, S.L.1    Waring, A.2    Yang, H.J.3    Cho, Y.4    Tan, L.5    Lehrer, R.6
  • 26
    • 0032544607 scopus 로고    scopus 로고
    • Novel defensin subfamily from spinach (Spinacia oleracea)
    • 26. Segura, A., Moreno, M., Molina, A. & Garcia-Olmedo, F. (1998) Novel defensin subfamily from spinach (Spinacia oleracea). FEBS Lett. 435, 159-162.
    • (1998) FEBS Lett. , vol.435 , pp. 159-162
    • Segura, A.1    Moreno, M.2    Molina, A.3    Garcia-Olmedo, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.