메뉴 건너뛰기




Volumn 101, Issue 5, 2011, Pages 1193-1201

Solution and solid-state NMR structural studies of antimicrobial peptides LPcin-I and LPcin-II

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 80052509416     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.06.067     Document Type: Article
Times cited : (24)

References (32)
  • 1
    • 1542315480 scopus 로고    scopus 로고
    • In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin
    • DOI 10.1016/j.peptides.2003.12.009, PII S0196978103004236
    • H. Saido-Sakanaka, and J. Ishibashi M. Yamakawa In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin Peptides 25 2004 19 27 (Pubitemid 38299283)
    • (2004) Peptides , vol.25 , Issue.1 , pp. 19-27
    • Saido-Sakanaka, H.1    Ishibashi, J.2    Momotani, E.3    Amano, F.4    Yamakawa, M.5
  • 2
    • 2942592590 scopus 로고    scopus 로고
    • Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides
    • DOI 10.1016/j.virol.2004.02.029, PII S0042682204001722
    • V.G. Chinchar, and L. Bryan L. Rollins-Smith Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides Virology 323 2004 268 275 (Pubitemid 38748474)
    • (2004) Virology , vol.323 , Issue.2 , pp. 268-275
    • Chinchar, V.G.1    Bryan, L.2    Silphadaung, U.3    Noga, E.4    Wade, D.5    Rollins-Smith, L.6
  • 3
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • DOI 10.1016/S0140-6736(97)80051-7
    • R.E.W. Hancock Peptide antibiotics Lancet 349 1997 418 422 (Pubitemid 27077684)
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.W.1
  • 4
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 2005 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 5
    • 0347755460 scopus 로고    scopus 로고
    • APD: The Antimicrobial Peptide Database
    • Database Issue
    • Z. Wang, and G. Wang APD: the Antimicrobial Peptide Database Nucleic Acids Res. 32 Database issue 2004 D590 D592
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.2
  • 6
    • 0018798032 scopus 로고
    • Physicochemical studies of the protein-lipid interactions in melittin-containing micelles
    • J. Lauterwein, and C. Bösch K. Wüthrich Physicochemical studies of the protein-lipid interactions in melittin-containing micelles Biochim. Biophys. Acta 556 1979 244 264
    • (1979) Biochim. Biophys. Acta , vol.556 , pp. 244-264
    • Lauterwein, J.1    Bösch, C.2    Wüthrich, K.3
  • 7
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • G.D. Henry, and B.D. Sykes Methods to study membrane protein structure in solution Methods Enzymol. 239 1994 515 535
    • (1994) Methods Enzymol. , vol.239 , pp. 515-535
    • Henry, G.D.1    Sykes, B.D.2
  • 8
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • J. Gesell, M. Zasloff, and S.J. Opella Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution J. Biomol. NMR 9 1997 127 135 (Pubitemid 127715704)
    • (1997) Journal of Biomolecular NMR , vol.9 , Issue.2 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 9
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • DOI 10.1021/bi000714m
    • A. Rozek, C.L. Friedrich, and R.E. Hancock Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles Biochemistry 39 2000 15765 15774 (Pubitemid 32040945)
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.W.3
  • 10
    • 0036343921 scopus 로고    scopus 로고
    • Dimer structure of magainin 2 bound to phospholipid vesicles
    • K. Wakamatsu, and A. Takeda K. Matsuzaki Dimer structure of magainin 2 bound to phospholipid vesicles Biopolymers 64 2002 314 327
    • (2002) Biopolymers , vol.64 , pp. 314-327
    • Wakamatsu, K.1    Takeda, A.2    Matsuzaki, K.3
  • 11
    • 0031903306 scopus 로고    scopus 로고
    • Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy
    • B. Bechinger, M. Zasloff, and S.J. Opella Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy Biophys. J. 74 1998 981 987 (Pubitemid 28345291)
    • (1998) Biophysical Journal , vol.74 , Issue.2 , pp. 981-987
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 13
    • 3142527103 scopus 로고    scopus 로고
    • Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose peptone
    • S. Campagna, and A.G. Mathot J.L. Gaillard Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose peptone J. Dairy Sci. 87 2004 1621 1626 (Pubitemid 38893292)
    • (2004) Journal of Dairy Science , vol.87 , Issue.6 , pp. 1621-1626
    • Campagna, S.1    Mathot, A.-G.2    Fleury, Y.3    Girardet, J.-M.4    Gaillard, J.-L.5
  • 14
    • 0033049369 scopus 로고    scopus 로고
    • Specific interaction between anionic phospholipids and milk bovine component PP3 and its 119-135 C-terminal fragment
    • DOI 10.1016/S0927-7765(99)00044-2, PII S0927776599000442
    • S. Campagna, and N. Van Mau J.L. Gaillard Specific interaction between anionic phospholipids and milk bovine component PP3 and its 119-135 C-terminal fragment Colloids Surf. B Biointerfaces 13 1999 299 309 (Pubitemid 29281557)
    • (1999) Colloids and Surfaces B: Biointerfaces , vol.13 , Issue.6 , pp. 299-309
    • Campagna, S.1    Van Mau, N.2    Heitz, F.3    Humbert, G.4    Gaillard, J.-L.5
  • 16
    • 0035817238 scopus 로고    scopus 로고
    • Evidence for membrane affinity of the C-terminal domain of bovine milk PP3 component
    • DOI 10.1016/S0005-2736(01)00360-1, PII S0005273601003601
    • S. Campagna, and P. Cosette J.L. Gaillard Evidence for membrane affinity of the C-terminal domain of bovine milk PP3 component Biochim. Biophys. Acta 1513 2001 217 222 (Pubitemid 32706419)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1513 , Issue.2 , pp. 217-222
    • Campagna, S.1    Cosette, P.2    Molle, G.3    Gaillard, J.-L.4
  • 17
    • 60349118324 scopus 로고    scopus 로고
    • Cloning, expression, isotope labeling, purification, and characterization of bovine antimicrobial peptide, lactophoricin in Escherichia coli
    • T.J. Park, and J.S. Kim Y. Kim Cloning, expression, isotope labeling, purification, and characterization of bovine antimicrobial peptide, lactophoricin in Escherichia coli Protein Expr. Purif. 65 2009 23 29
    • (2009) Protein Expr. Purif. , vol.65 , pp. 23-29
    • Park, T.J.1    Kim, J.S.2    Kim, Y.3
  • 18
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 19
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • B.A. Johnson Using NMRView to visualize and analyze the NMR spectra of macromolecules Methods Mol. Biol. 278 2004 313 352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 20
    • 0034919240 scopus 로고    scopus 로고
    • Automated assignment of ambiguous nuclear overhauser effects with ARIA
    • DOI 10.1016/S0076-6879(01)39310-2
    • J.P. Linge, S.I. O'Donoghue, and M. Nilges Automated assignment of ambiguous nuclear overhauser effects with ARIA Methods Enzymol. 339 2001 71 90 (Pubitemid 32666557)
    • (2001) Methods in Enzymology , vol.339 , pp. 71-90
    • Linge, J.P.1    O'Donoghue, S.I.2    Nilges, M.3
  • 21
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • A.T. Brünger, and P.D. Adams G.L. Warren Crystallography & NMR system: a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54 1998 905 921
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Warren, G.L.3
  • 23
    • 36849106840 scopus 로고
    • Proton-enhanced NMR of dilute spins in solids
    • A. Pines, M.G. Gibby, and J.S. Waugh Proton-enhanced NMR of dilute spins in solids J. Chem. Phys. 59 1973 569 571
    • (1973) J. Chem. Phys. , vol.59 , pp. 569-571
    • Pines, A.1    Gibby, M.G.2    Waugh, J.S.3
  • 24
    • 0041993680 scopus 로고    scopus 로고
    • Phase-modulated heteronuclear decoupling in NMR of solids
    • A.K. Khitrin, T. Fujiwara, and H.J. Akutsu Phase-modulated heteronuclear decoupling in NMR of solids J. Magn. Reson. 162 2003 46 53
    • (2003) J. Magn. Reson. , vol.162 , pp. 46-53
    • Khitrin, A.K.1    Fujiwara, T.2    Akutsu, H.J.3
  • 25
    • 0042468159 scopus 로고    scopus 로고
    • A "magic sandwich" pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy
    • A.A. Nevzorov, and S.J. Opella A "magic sandwich" pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy J. Magn. Reson. 164 2003 182 186
    • (2003) J. Magn. Reson. , vol.164 , pp. 182-186
    • Nevzorov, A.A.1    Opella, S.J.2
  • 26
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • R. Koradi, M. Billeter, and K. Wüthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 29-32 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 29
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • F.M. Marassi, and S.J. Opella A solid-state NMR index of helical membrane protein structure and topology J. Magn. Reson. 144 2000 150 155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 30
    • 0034184852 scopus 로고    scopus 로고
    • Imaging membrane protein helical wheels
    • J. Wang, and J. Denny T.A. Cross Imaging membrane protein helical wheels J. Magn. Reson. 144 2000 162 167
    • (2000) J. Magn. Reson. , vol.144 , pp. 162-167
    • Wang, J.1    Denny, J.2    Cross, T.A.3
  • 31
    • 20444366208 scopus 로고    scopus 로고
    • Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch
    • DOI 10.1016/j.jmb.2005.05.004, PII S0022283605005243
    • S.H. Park, and S.J. Opella Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch J. Mol. Biol. 350 2005 310 318 (Pubitemid 40805465)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.2 , pp. 310-318
    • Sang, H.P.1    Opella, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.