메뉴 건너뛰기




Volumn 369, Issue 2, 2008, Pages 609-615

NMR based structure-activity relationship analysis of an antimicrobial peptide, thanatin, engineered by site-specific chemical modification: Activity improvement and spectrum alteration

Author keywords

Activity spectrum; Antimicrobial peptide; Disulfide bridge; NMR solution structure; Site specific chemical modification; Thanatin

Indexed keywords

CYSTEINE; DISULFIDE; POLYPEPTIDE ANTIBIOTIC AGENT; THANATIN; UNCLASSIFIED DRUG;

EID: 40849133839     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.02.057     Document Type: Article
Times cited : (21)

References (32)
  • 1
  • 3
    • 0026760182 scopus 로고
    • The crisis in antibiotic resistance
    • Neu H.C. The crisis in antibiotic resistance. Science 257 (1992) 1064-1073
    • (1992) Science , vol.257 , pp. 1064-1073
    • Neu, H.C.1
  • 4
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock R.E. Peptide antibiotics. Lancet 349 (1997) 418-422
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 5
    • 0031037207 scopus 로고    scopus 로고
    • The search for antimicrobial agents effective against bacteria resistant to multiple antibiotics
    • Chopra I., Hodgson J., Metcalf B., and Poste G. The search for antimicrobial agents effective against bacteria resistant to multiple antibiotics. Antimicrob. Agents Chemother. 41 (1997) 497-503
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 497-503
    • Chopra, I.1    Hodgson, J.2    Metcalf, B.3    Poste, G.4
  • 6
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy W.L., and Kari U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37 (1995) 105-122
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 7
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes structural and charge requirements for activity
    • Sitaram N., and Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes structural and charge requirements for activity. Biochim. Biophys. Acta 1462 (1999) 29-54
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 8
    • 0030071417 scopus 로고    scopus 로고
    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog antimicrobial peptides
    • Fehlbaum P., Bulet P., Chemysh S., Briand J.P., Roussel J.P., Letellier L., Hetru C., and Hoffmann J.A. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog antimicrobial peptides. Proc. Natl. Acad. Sci. USA 6 (1996) 1221-1225
    • (1996) Proc. Natl. Acad. Sci. USA , vol.6 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chemysh, S.3    Briand, J.P.4    Roussel, J.P.5    Letellier, L.6    Hetru, C.7    Hoffmann, J.A.8
  • 9
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • Wu M., and Hancock R.E. Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274 (1999) 29-35
    • (1999) J. Biol. Chem. , vol.274 , pp. 29-35
    • Wu, M.1    Hancock, R.E.2
  • 10
    • 0031696867 scopus 로고    scopus 로고
    • Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data
    • Mandard N., Sodano P., Labbe H., Bonmatin J.M., Bulet P., Hetru C., Ptak M., and Vovelle F. Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data. Eur. J. Biochem. 256 (1998) 404-410
    • (1998) Eur. J. Biochem. , vol.256 , pp. 404-410
    • Mandard, N.1    Sodano, P.2    Labbe, H.3    Bonmatin, J.M.4    Bulet, P.5    Hetru, C.6    Ptak, M.7    Vovelle, F.8
  • 11
    • 0035997990 scopus 로고    scopus 로고
    • Role of amino acid residues within the disulfide loop of thanatin, a potent antibiotic peptide
    • Lee M.K., Cha L., Lee S.H., and Hahm K.S. Role of amino acid residues within the disulfide loop of thanatin, a potent antibiotic peptide. J. Biochem. Mol. Biol. 35 (2002) 291-296
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 291-296
    • Lee, M.K.1    Cha, L.2    Lee, S.H.3    Hahm, K.S.4
  • 12
    • 0027096816 scopus 로고
    • Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa
    • Morikawa N., Hagiwara K., and Nakajima T. Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. Biochem. Biophys. Res. Commun. 189 (1992) 184-190
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 184-190
    • Morikawa, N.1    Hagiwara, K.2    Nakajima, T.3
  • 13
    • 0027232845 scopus 로고
    • Novel antimicrobial peptides from skin secretion of the European frog Rana esculentra
    • Simmaco M., Mignogna G., Barra D., and Bossa F. Novel antimicrobial peptides from skin secretion of the European frog Rana esculentra. FEBS Lett. 324 (1993) 159-161
    • (1993) FEBS Lett. , vol.324 , pp. 159-161
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3    Bossa, F.4
  • 14
    • 0033661762 scopus 로고    scopus 로고
    • Functional mapping against Escherichia coli for the broad-spectrum antimicrobial peptide, thanatin, based on an in vivo monitoring assay system
    • Taguchi S., Kuwasako K., Suenaga A., Okada M., and Momose H. Functional mapping against Escherichia coli for the broad-spectrum antimicrobial peptide, thanatin, based on an in vivo monitoring assay system. J. Biochem. 128 (2000) 745-754
    • (2000) J. Biochem. , vol.128 , pp. 745-754
    • Taguchi, S.1    Kuwasako, K.2    Suenaga, A.3    Okada, M.4    Momose, H.5
  • 16
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., and Davis D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65 (1985) 355-360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 17
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R.R., and Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95 (1980) 1-6
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 18
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U., Sorensen O.W., and Ernst R.R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104 (1982) 6800-6801
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sorensen, O.W.2    Ernst, R.R.3
  • 19
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., and Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2 (1992) 661-665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 22
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim Y., and Prestegtard J.H. Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Reson. 84 (1989) 9-13
    • (1989) J. Magn. Reson. , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegtard, J.H.2
  • 23
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 24
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 25
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 26
    • 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
  • 27
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 28
  • 29
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • Kluver E., Schulz-Maronde S., Scheid S., Meyer B., Forssmann W.G., and Adermann K. Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 44 (2005) 9804-9816
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Kluver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 30
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics
    • Privalov P.L., and Makhatadze G.I. Contribution of hydration to protein folding thermodynamics. J. Mol. Biol. 232 (1993) 660-679
    • (1993) J. Mol. Biol. , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 31
    • 0032815802 scopus 로고    scopus 로고
    • Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds
    • Rao A.G. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch. Biochem. Biophys. 361 (1999) 127-134
    • (1999) Arch. Biochem. Biophys. , vol.361 , pp. 127-134
    • Rao, A.G.1
  • 32
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matuszaki 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
    • Matuszaki, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.