메뉴 건너뛰기




Volumn 168, Issue 2, 2009, Pages 250-258

Synthesis and antimicrobial activity of truncated fragments and analogs of citropin 1.1: The solution structure of the SDS micelle-bound citropin-like peptides

Author keywords

Antimicrobial activity; CD; Citropin 1.1; FTIR; NMR; SDS micelle

Indexed keywords

CITROPIN DERIVATIVE; DODECYL SULFATE SODIUM; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 70349560226     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.07.012     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 24144461618 scopus 로고    scopus 로고
    • Direct visualization of membrane leakage induced by the antibiotic peptides: maculation, citropin, and aurein
    • Ambroggio E.E., Separovic F., Bowie J.H., Gerardo D.F., and Bagatolli L.A. Direct visualization of membrane leakage induced by the antibiotic peptides: maculation, citropin, and aurein. Biophys. J. 89 (2005) 1874-1881
    • (2005) Biophys. J. , vol.89 , pp. 1874-1881
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.H.3    Gerardo, D.F.4    Bagatolli, L.A.5
  • 3
    • 0029047938 scopus 로고
    • Amphibian skin: a promising resource for antimicrobial peptides
    • Barra D., and Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol. 13 (1995) 205-209
    • (1995) Trends Biotechnol. , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 4
    • 0343459675 scopus 로고
    • The program XEASY for the computer-supported NMR spectral analysis of biological macromolecules
    • Bartles C., Xia T., Billeter M., Günter P., and Wüthrich K. The program XEASY for the computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 5 (1995) 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
  • 5
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax A., and Davis D.G. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63 (1985) 207-213
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 6
    • 0000161163 scopus 로고
    • Enhanced NMR resolution by restricting the effective sample volume
    • Bax A., and Freeman R. Enhanced NMR resolution by restricting the effective sample volume. J. Magn. Reson. 65 (1985) 355-360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Freeman, R.2
  • 8
    • 0020475305 scopus 로고
    • Sequential resonance assignments in protein (1)H nuclear magnetic resonance spectra: computation of sferically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations
    • Billeter M., Braun W., and Wüthrich K. Sequential resonance assignments in protein (1)H nuclear magnetic resonance spectra: computation of sferically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. J. Mol. Biol. 155 (1982) 321-346
    • (1982) J. Mol. Biol. , vol.155 , pp. 321-346
    • Billeter, M.1    Braun, W.2    Wüthrich, K.3
  • 9
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame
    • Bothner-By A.A., Stephens R.L., Lee J.M., Warren C.D., and Jeanloz R.W. Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. JACS 106 (1980) 811-813
    • (1980) JACS , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 10
    • 0037129516 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sodium dodecyl sulfate micelle in water: micellar structural characteristics and counterion distribution
    • Bruce C.D., Berkowitz M.L., Perera L., and Forbes M.D.E. Molecular dynamics simulation of sodium dodecyl sulfate micelle in water: micellar structural characteristics and counterion distribution. J. Phys. Chem. B 106 (2002) 3788-3793
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3788-3793
    • Bruce, C.D.1    Berkowitz, M.L.2    Perera, L.3    Forbes, M.D.E.4
  • 11
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvoluted FTIR spectra
    • Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers 25 (1986) 469-487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 13
    • 0034109713 scopus 로고    scopus 로고
    • Maculatin 1.1, an antimicrobial peptide from the Australian tree frog, Litoria genimaculata. Solution structure and biological activity
    • Chia B.C.S., Carver J.A., Mulhern T.D., and Bowie J.H. Maculatin 1.1, an antimicrobial peptide from the Australian tree frog, Litoria genimaculata. Solution structure and biological activity. Eur. J. Biochem. 267 (2000) 1894-1908
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1894-1908
    • Chia, B.C.S.1    Carver, J.A.2    Mulhern, T.D.3    Bowie, J.H.4
  • 14
    • 0033634645 scopus 로고    scopus 로고
    • A 31P NMR study of the interaction of amphibian antimicrobial peptides with the membranes of live bacteria
    • Chia B.C.S., Lam Y.H., Dyall-Smith M., Separovic F., and Bowie J.H. A 31P NMR study of the interaction of amphibian antimicrobial peptides with the membranes of live bacteria. Lett. Pept. Sci. 7 (2000) 151-156
    • (2000) Lett. Pept. Sci. , vol.7 , pp. 151-156
    • Chia, B.C.S.1    Lam, Y.H.2    Dyall-Smith, M.3    Separovic, F.4    Bowie, J.H.5
  • 15
    • 0035215289 scopus 로고    scopus 로고
    • Amide proton temperature coefficients as hydrogen bond indicators in proteins
    • Cierpicki T., and Otlewski J. Amide proton temperature coefficients as hydrogen bond indicators in proteins. J. Biomol. NMR 21 (2001) 249-261
    • (2001) J. Biomol. NMR , vol.21 , pp. 249-261
    • Cierpicki, T.1    Otlewski, J.2
  • 16
    • 0344875561 scopus 로고    scopus 로고
    • A cyclic CCK8 analogue selective for the cholecystokin type A receptor: design, synthesis, NMR structure and binding measurements
    • De Luca S., Ragone R., Bracco C., Digilio G., Aloj L., Tesauro D., Saviano M., Pedone C., and Morelli G. A cyclic CCK8 analogue selective for the cholecystokin type A receptor: design, synthesis, NMR structure and binding measurements. ChemBioChem 4 (2003) 1176-1187
    • (2003) ChemBioChem , vol.4 , pp. 1176-1187
    • De Luca, S.1    Ragone, R.2    Bracco, C.3    Digilio, G.4    Aloj, L.5    Tesauro, D.6    Saviano, M.7    Pedone, C.8    Morelli, G.9
  • 17
    • 0344211838 scopus 로고    scopus 로고
    • NNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1
    • Doyle J., Brinkworth C.S., Wegener K.L., Carver J.A., Llewellyn L.E., Olver I.N., Bowie J.H., Wabnitz P.A., and Tyler M.J. NNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1. Eur. J. Biochem. 270 (2003) 1141-1153
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1141-1153
    • Doyle, J.1    Brinkworth, C.S.2    Wegener, K.L.3    Carver, J.A.4    Llewellyn, L.E.5    Olver, I.N.6    Bowie, J.H.7    Wabnitz, P.A.8    Tyler, M.J.9
  • 18
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields G.B., and Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35 (1990) 161-214
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 19
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P., Mumenthaler C., and Wüthrich 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
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 20
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., and Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. JACS 114 (1992) 10663-10665
    • (1992) JACS , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 21
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong J., and Shaoning Y. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim. Biophys. Sin. 39 (2007) 549-559
    • (2007) Acta Biochim. Biophys. Sin. , vol.39 , pp. 549-559
    • Kong, J.1    Shaoning, Y.2
  • 22
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 52-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 52-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 23
    • 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. Biochim. Biophys. Res. Commun. 95 (1980) 1-10
    • (1980) Biochim. Biophys. Res. Commun. , vol.95 , pp. 1-10
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 24
    • 0027328548 scopus 로고
    • The toad, ugly and venomous, wears yet a precious jewel in his skin
    • Lazarus L.H., and Attil M. The toad, ugly and venomous, wears yet a precious jewel in his skin. Prog. Neurobiol. 41 (1993) 473-507
    • (1993) Prog. Neurobiol. , vol.41 , pp. 473-507
    • Lazarus, L.H.1    Attil, M.2
  • 25
    • 0032558088 scopus 로고    scopus 로고
    • 10-helix contents of a helical peptide
    • 10-helix contents of a helical peptide. JACS 120 (1998) 7039-7048
    • (1998) JACS , vol.120 , pp. 7039-7048
    • Long, H.W.1    Tycko, R.2
  • 27
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation spectroscopy
    • Palmer A.G., Cavanagh J., Wright P.E., and Rance M. Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation spectroscopy. J. Magn. Reson. 93 (1991) 151-170
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 30
    • 38849197910 scopus 로고    scopus 로고
    • Conformational studies of vasopressin and mesotocin using NMR spectroscopy and molecular modelling methods. Part II: studies in the SDS micelle
    • Rodziewicz-Motowidło S., Sikorska E., Oleszczuk M., and Czapiewski C. Conformational studies of vasopressin and mesotocin using NMR spectroscopy and molecular modelling methods. Part II: studies in the SDS micelle. J. Pept. Sci. 14 (2008) 85-96
    • (2008) J. Pept. Sci. , vol.14 , pp. 85-96
    • Rodziewicz-Motowidło, S.1    Sikorska, E.2    Oleszczuk, M.3    Czapiewski, C.4
  • 31
    • 0030185518 scopus 로고    scopus 로고
    • Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: a monitor of intramolecular hydrogen bonds in helical peptides?
    • Rothemund S., Weißhoff H., Beyermann M., Krause E., Bienert M., Mügge C., Sykes B.D., and Sönnichsen F.D. Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: a monitor of intramolecular hydrogen bonds in helical peptides?. J. Biomol. NMR 8 (1996) 93-97
    • (1996) J. Biomol. NMR , vol.8 , pp. 93-97
    • Rothemund, S.1    Weißhoff, H.2    Beyermann, M.3    Krause, E.4    Bienert, M.5    Mügge, C.6    Sykes, B.D.7    Sönnichsen, F.D.8
  • 32
    • 0028989666 scopus 로고
    • Software for viewing biomolecules in three dimensions on the Internet
    • Sanchez-Ferrer A., Nunez-Delicado E., and Bru R. Software for viewing biomolecules in three dimensions on the Internet. Trends Biochem. Sci. 20 (1995) 286-288
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 286-288
    • Sanchez-Ferrer, A.1    Nunez-Delicado, E.2    Bru, R.3
  • 35
    • 0001480302 scopus 로고    scopus 로고
    • Simulation of sodium dodecyl sulfate at the water-vapor and water-carbon tetrachloride interfaces at low surface coverage
    • Schweighofer K.J., Essman U., and Berkowitz M. Simulation of sodium dodecyl sulfate at the water-vapor and water-carbon tetrachloride interfaces at low surface coverage. J. Phys. Chem. B 101 (1997) 3793-3799
    • (1997) J. Phys. Chem. B , vol.101 , pp. 3793-3799
    • Schweighofer, K.J.1    Essman, U.2    Berkowitz, M.3
  • 36
    • 35848930156 scopus 로고    scopus 로고
    • Interactions of the Australian tree frog antimicrobial peptides aurein 1.2, citropin 1.1 and maculatin 1.1 with lipid model membranes: differential scanning calorimetric and Fourier transform infrared spectroscopic studies
    • Seto G.W.J., Marwaha S., Kobewka D.M., Lewis N.A.H., Separovic F., and McElhaney R.N. Interactions of the Australian tree frog antimicrobial peptides aurein 1.2, citropin 1.1 and maculatin 1.1 with lipid model membranes: differential scanning calorimetric and Fourier transform infrared spectroscopic studies. Biochim. Biophys. Acta 1768 (2007) 2787-2800
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2787-2800
    • Seto, G.W.J.1    Marwaha, S.2    Kobewka, D.M.3    Lewis, N.A.H.4    Separovic, F.5    McElhaney, R.N.6
  • 37
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 38
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 39
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 952 (1988) 115-130
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 40
    • 0025613794 scopus 로고
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 30 (1990) 1243-1257
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 41
    • 0033569805 scopus 로고    scopus 로고
    • Host defense peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1
    • Wegener K.L., Wabnitz P.A., Carver J.A., Bowie J.H., Chia B.C.S., Wallace J.C., and Tyler M.J. Host defense peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. Eur. J. Biochem. 265 (1999) 627-637
    • (1999) Eur. J. Biochem. , vol.265 , pp. 627-637
    • Wegener, K.L.1    Wabnitz, P.A.2    Carver, J.A.3    Bowie, J.H.4    Chia, B.C.S.5    Wallace, J.C.6    Tyler, M.J.7
  • 42
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5 (1995) 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.