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Volumn 13, Issue 5, 2007, Pages 327-333

Conformational solution studies of the anti-microbial temporin A retro-analogues by using NMR spectroscopy

Author keywords

Analogues; Anti microbial peptides; NMR; Structure; Temporin A; TFE

Indexed keywords

ANTIINFECTIVE AGENT; GLYCYLISOLEUCYLLEUCYLPROLYLLEUCYLPHENYLALANYLARGINYLVALYLLEUCYLSERYLGLYCYLISOLEUCYLLEUCINAMIDE; LEUCYLISOLEUCYLGLYCYLSERYLLEUCYLVALYLARGINYLGLYCYLISOLEUCYLLEUCYLPROLYLLEUCYLPHENYLALANINAMIDE; PEPTIDE DERIVATIVE; SOLVENT; TEMPORIN A; TEMPORIN A DERIVATIVE; UNCLASSIFIED DRUG;

EID: 34248352027     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.844     Document Type: Article
Times cited : (5)

References (32)
  • 2
    • 1242306544 scopus 로고    scopus 로고
    • Antimicrobial peptides from ranid frogs: Taxonomic and phylogenetic markers and a potential source of new therapeutic agents
    • Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochem. Biophys. Acta 2004; 1696: 1-14.
    • (2004) Biochem. Biophys. Acta , vol.1696 , pp. 1-14
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3
  • 3
    • 0034106918 scopus 로고    scopus 로고
    • Structure-function relationships of temporins, small antimicrobialpeptides from amphibian skin
    • Mangoni ML, Rinaldi AC, Giulio AD, Mignogna G, Bozii A, Barra D. Structure-function relationships of temporins, small antimicrobialpeptides from amphibian skin. Eur. J. Biochem. 2000; 267: 1447-1454.
    • (2000) Eur. J. Biochem , vol.267 , pp. 1447-1454
    • Mangoni, M.L.1    Rinaldi, A.C.2    Giulio, A.D.3    Mignogna, G.4    Bozii, A.5    Barra, D.6
  • 5
    • 0037113168 scopus 로고    scopus 로고
    • Temporin L: Antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles
    • Rinaldi AC, Mangoni ML, Rufo A, Luzi C, Barra D, Zhao H. Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles. Biochem. J. 2002; 368: 91-100.
    • (2002) Biochem. J , vol.368 , pp. 91-100
    • Rinaldi, A.C.1    Mangoni, M.L.2    Rufo, A.3    Luzi, C.4    Barra, D.5    Zhao, H.6
  • 6
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z, Shai Y. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 1998; 47: 451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 7
    • 0026354984 scopus 로고
    • Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers
    • Rapaport D, Shai Y. Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers. J. Biol. Chem. 1991; 266: 23769-23775.
    • (1991) J. Biol. Chem , vol.266 , pp. 23769-23775
    • Rapaport, D.1    Shai, Y.2
  • 8
    • 0037165196 scopus 로고    scopus 로고
    • Animicrobial peptides of multicellular organism
    • Zasloff M. Animicrobial peptides of multicellular organism. Nature 2002; 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 10
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defece? Magainins and tachyplesins as archetypes
    • Matsuzaki K, Biochim M. Why and how are peptide-lipid interactions utilized for self-defece? Magainins and tachyplesins as archetypes. Biophys. Acta-Biomem. 1999; 1462: 1-10.
    • (1999) Biophys. Acta-Biomem , vol.1462 , pp. 1-10
    • Matsuzaki, K.1    Biochim, M.2
  • 11
    • 0026969265 scopus 로고
    • Interactions of antimicrobial dermaseptin and its fluorescently labeled analogs with phospholipid-membranes
    • Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y. Interactions of antimicrobial dermaseptin and its fluorescently labeled analogs with phospholipid-membranes. Biochemistry 1992; 31: 12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 14
    • 0032412381 scopus 로고    scopus 로고
    • Antimicrobial peptides
    • Andreu D, Rivas L. Antimicrobial peptides. Biopolymers 1998; 47: 415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 16
    • 34248332653 scopus 로고    scopus 로고
    • Conformational behaviour of temporin a and temporin L by NMR spectroscopy in different environmental conditions
    • Auriemma L, Carotenuto M, Mazella di Bosco A, Mangowi ML, Campiglia P, Grieco P. Conformational behaviour of temporin a and temporin L by NMR spectroscopy in different environmental conditions. J. Pept. Sci. 2006; 12(Suppl. S): 192.
    • (2006) J. Pept. Sci , vol.12 , Issue.SUPPL. S , pp. 192
    • Auriemma, L.1    Carotenuto, M.2    Mazella di Bosco, A.3    Mangowi, M.L.4    Campiglia, P.5    Grieco, P.6
  • 17
    • 33747241354 scopus 로고    scopus 로고
    • Conformational behaviour of temporis A and temporis L by NMR spectroscopy in different environmental conditions
    • Kamysz W, Mickjewicz B, Rodziewicz-Motowidlo S, Greber K, Okrój M. Conformational behaviour of temporis A and temporis L by NMR spectroscopy in different environmental conditions. J. Pept. Sci. 2006; 12: 533-537.
    • (2006) J. Pept. Sci , vol.12 , pp. 533-537
    • Kamysz, W.1    Mickjewicz, B.2    Rodziewicz-Motowidlo, S.3    Greber, K.4    Okrój, M.5
  • 18
    • 34248374886 scopus 로고    scopus 로고
    • Varian, nuclear magnetic resonance instruments. VnmrTM Software, Revision 5.3B 1/97.
    • Varian, nuclear magnetic resonance instruments. VnmrTM Software, Revision 5.3B 1/97.
  • 19
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartles C, Xia T, Billeter M, Günter P, Wüthrich K. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J. Biomol. NMR 1995; 5: 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartles, C.1    Xia, T.2    Billeter, M.3    Günter, P.4    Wüthrich, K.5
  • 20
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U, Sorrensen OW, Ernst KR. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 1982; 104: 6800-6810.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 6800-6810
    • Piantini, U.1    Sorrensen, O.W.2    Ernst, K.R.3
  • 21
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985; 65: 355-360.
    • (1985) J. Magn. Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 22
    • 0343359244 scopus 로고
    • Investigation of exchange processes by 2-dimensional NMR-spectroscopy
    • Jeener J, Meier BH, Bachmann P, Ernst RR. Investigation of exchange processes by 2-dimensional NMR-spectroscopy. J. Chem. Phys. 1979; 71: 4546-4553.
    • (1979) J. Chem. Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 23
    • 5144229966 scopus 로고
    • Practical aspectrs of two-dimensional transverse NOE spectroscopy
    • Bax A, Davis DG. Practical aspectrs of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 1985; 63: 207-213.
    • (1985) J. Magn. Reson , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 24
    • 33745356391 scopus 로고
    • Contact electron-spin coupling of nuclear magnetic moments
    • Karplus M. Contact electron-spin coupling of nuclear magnetic moments. J. Chem. Phys. 1959; 30: 11-15.
    • (1959) J. Chem. Phys , vol.30 , pp. 11-15
    • Karplus, M.1
  • 25
    • 0026089657 scopus 로고
    • Efficient computation of 3-dimensional protein structures in solution from nuclear-magnetic-resonance data using the program DIANA and the supporting programs CALIBA, HABAS ans GLOMSA
    • Güntert P, Braun W, Wüthrich K. Efficient computation of 3-dimensional protein structures in solution from nuclear-magnetic-resonance data using the program DIANA and the supporting programs CALIBA, HABAS ans GLOMSA. J. Mol. Biol. 1991; 217: 517-530.
    • (1991) J. Mol. Biol , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 26
    • 0021764813 scopus 로고
    • HNα for identification of helical secondary structure
    • HNα for identification of helical secondary structure. J. Mol. Biol. 1984; 180: 741-751.
    • (1984) J. Mol. Biol , vol.180 , pp. 741-751
    • Pardi, A.1    Billeter, M.2    Wüthrich, K.3
  • 27
    • 0003905053 scopus 로고
    • Version 3.1. Yale University Press: New Haven, CT
    • Brünger AT. The X-PLOR Software Manual. Version 3.1. Yale University Press: New Haven, CT, 1992.
    • (1992) The X-PLOR Software Manual
    • Brünger, A.T.1
  • 28
    • 84986512474 scopus 로고    scopus 로고
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 1983; 4: 187-217.
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 1983; 4: 187-217.
  • 29
    • 33846446220 scopus 로고
    • Restart procedures for conjugate gradient method
    • Powell MJD. Restart procedures for conjugate gradient method. Math. Prog. 1977; 12: 241-254.
    • (1977) Math. Prog , vol.12 , pp. 241-254
    • Powell, M.J.D.1
  • 30
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi K, Billeter M, Wütrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 1996; 15: 51.
    • (1996) J. Mol. Graph , vol.15 , pp. 51
    • Koradi, K.1    Billeter, M.2    Wütrich, K.3
  • 31
    • 0026597879 scopus 로고
    • The chemical-shift index-a fast and simple method for the assignment of protein secondary structure through NMR-spectroscopy
    • Wishart DS, Sykes BD, Richards FM. The chemical-shift index-a fast and simple method for the assignment of protein secondary structure through NMR-spectroscopy. Biochemistry 1992; 31: 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 32
    • 33644531547 scopus 로고    scopus 로고
    • Conformational bahaviour of Temporin A and Temporin L in aqueous solution: A computational/experimental study
    • D'Abramo D, Rinaldi AC, Bozzi A, Amadei A, Mignogna G, Di Nola A, Aschi M. Conformational bahaviour of Temporin A and Temporin L in aqueous solution: a computational/experimental study. Biopolymers 2006; 81: 215-224.
    • (2006) Biopolymers , vol.81 , pp. 215-224
    • D'Abramo, D.1    Rinaldi, A.C.2    Bozzi, A.3    Amadei, A.4    Mignogna, G.5    Di Nola, A.6    Aschi, M.7


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