메뉴 건너뛰기




Volumn 1818, Issue 2, 2012, Pages 212-218

Characterization of a potent antimicrobial lipopeptide via coarse-grained molecular dynamics

Author keywords

Antimicrobial peptides; Lipopeptides; Molecular dynamics

Indexed keywords

ANTIMICROBIAL PEPTIDE C16 KGGK; LIPOPEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84855447465     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.07.025     Document Type: Article
Times cited : (39)

References (50)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • H.G. Boman Peptide antibiotics and their role in innate immunity Annu. Rev. Immunol. 13 1995 61 92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 3
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • M. Zasloff Magainins, a class of antimicrobial peptides from xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor Proc. Natl. Acad. Sci. U. S. A. 84 1987 5449 5453 (Pubitemid 17129018)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.15 , pp. 5449-5453
    • Zasloff, M.1
  • 6
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Z. Wang, and G. Wang APD: the antimicrobial peptide database Nucleic Acids Res. 32 2004 D590 D592
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.2
  • 7
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • G. Wang, X. Li, and Z. Wang APD2: the updated antimicrobial peptide database and its application in peptide design Nucleic Acids Res. 37 2009 D933 D937
    • (2009) Nucleic Acids Res. , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 8
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanism of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanism of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 9
    • 0037282323 scopus 로고    scopus 로고
    • Antimicrobial peptides: Current status and therapeutic potential
    • DOI 10.2165/00003495-200363040-00005
    • A.R. Koczulla, and R. Bals Antimicrobial peptides: current status and therapeutic potential Drugs 63 2003 389 406 (Pubitemid 36259526)
    • (2003) Drugs , vol.63 , Issue.4 , pp. 389-406
    • Koczulla, A.R.1    Bals, R.2
  • 10
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 12
    • 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. Micro. 3 2005 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 13
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.07.001, PII S0005273606002616
    • B. Bechinger, and K. Lohner Detergent-like actions of linear amphipathic cationic antimicrobial peptides Biochimica et Biophysica Acta (BBA)Biomembranes 1758 2006 1529 1539 (Pubitemid 44436087)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 14
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • DOI 10.1016/S0196-9781(01)00498-3, PII S0196978101004983
    • Y. Shai, and Z. Oren From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides Peptides 22 2001 1629 1641 (Pubitemid 32918242)
    • (2001) Peptides , vol.22 , Issue.10 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 15
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • DOI 10.1038/nbt1267, PII NBT1267
    • R.E.W. Hancock, and H.-G. Sahl Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 24 2006 1551 1557 (Pubitemid 44967479)
    • (2006) Nature Biotechnology , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 16
    • 0347625845 scopus 로고    scopus 로고
    • Bestowing Antifungal and Antibacterial Activities by Lipophilic Acid Conjugation to D,L-Amino Acid-Containing Antimicrobial Peptides: A Plausible Mode of Action
    • DOI 10.1021/bi035142v
    • D. Avrahami, and Y. Shai Bestowing antifungal and antibacterial activities by lipophilic acid conjugation to D, L-amino acid-containing antimicrobial peptides: a plausible mode of action Biochemistry 42 2003 14946 14956 (Pubitemid 37553525)
    • (2003) Biochemistry , vol.42 , Issue.50 , pp. 14946-14956
    • Avrahami, D.1    Shai, Y.2
  • 17
    • 1842478127 scopus 로고    scopus 로고
    • A New Group of Antifungal and Antibacterial Lipopeptides Derived from Non-membrane Active Peptides Conjugated to Palmitic Acid
    • DOI 10.1074/jbc.M312260200
    • D. Avrahami, and Y. Shai A new group of antifungal and antibacterial lipopeptides derived from non-membrane active peptides conjugated to palmitic acid J. Biol. Chem. 279 2004 12277 12285 (Pubitemid 38445793)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12277-12285
    • Avrahami, D.1    Shai, Y.2
  • 19
    • 35448965554 scopus 로고    scopus 로고
    • Inhibition of fungal and bacterial plant pathogens in vitro and in planta with ultrashort cationic lipopeptides
    • DOI 10.1128/AEM.01334-07
    • A. Makovitzki, A. Viterbo, Y. Brotman, I. Chet, and Y. Shai Inhibition of fungal and bacterial plant pathogens in vitro and in planta with ultrashort cationic lipopeptides Appl. Environ. Microbiol. 73 2007 6629 6636 (Pubitemid 47623723)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.20 , pp. 6629-6636
    • Makovitzki, A.1    Viterbo, A.2    Brotman, Y.3    Chet, I.4    Shai, Y.5
  • 20
    • 0001008704 scopus 로고
    • Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid-crystal phases
    • H. Heller, M. Schaefer, and K. Schulten Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid-crystal phases J. Phys. Chem. 97 1993 8343 8360
    • (1993) J. Phys. Chem. , vol.97 , pp. 8343-8360
    • Heller, H.1    Schaefer, M.2    Schulten, K.3
  • 22
    • 49549083949 scopus 로고    scopus 로고
    • Membrane proteins: Molecular dynamics simulations
    • E. Lindahl, and M.S. Sansom Membrane proteins: molecular dynamics simulations Curr. Opin. Struct. Biol. 18 2008 425 431
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 425-431
    • Lindahl, E.1    Sansom, M.S.2
  • 23
    • 36248932202 scopus 로고    scopus 로고
    • Computer simulation of antimicrobial peptides
    • DOI 10.2174/092986707782360105
    • E. Mátyus, C. Kandt, and D.P. Tieleman Computer simulation of antimicrobial peptides Curr. Med. Chem. 14 2007 2789 2798 (Pubitemid 350130922)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.26 , pp. 2789-2798
    • Matyus, E.1    Kandt, C.2    Tieleman, D.P.3
  • 24
    • 70350238527 scopus 로고    scopus 로고
    • Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions
    • discussion 445-81
    • A.J. Rzepiela, D. Sengupta, N. Goga, and S.J. Marrink Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions Faraday Discuss 144 2010 431 443 discussion 445-81
    • (2010) Faraday Discuss , vol.144 , pp. 431-443
    • Rzepiela, A.J.1    Sengupta, D.2    Goga, N.3    Marrink, S.J.4
  • 26
    • 48149102003 scopus 로고    scopus 로고
    • Application of mean field boundary potentials in simulations of lipid vesicles
    • J.H. Risselada, A.E. Mark, and S.J. Marrink Application of mean field boundary potentials in simulations of lipid vesicles J. Phys. Chem. B 112 2008 7438 7447
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7438-7447
    • Risselada, J.H.1    Mark, A.E.2    Marrink, S.J.3
  • 30
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 31
    • 62349116492 scopus 로고    scopus 로고
    • On using a too large integration time step in molecular dynamics simulations of coarse-grained molecular models
    • M. Winger, D. Trzesniak, R. Baron, and W.F. van Gunsteren On using a too large integration time step in molecular dynamics simulations of coarse-grained molecular models Phys. Chem. Chem. Phys. 11 2009 1934 1941
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 1934-1941
    • Winger, M.1    Trzesniak, D.2    Baron, R.3    Van Gunsteren, W.F.4
  • 32
    • 77149124571 scopus 로고    scopus 로고
    • Comment on "on using a too large integration time step in molecular dynamics simulations of coarse-grained molecular models" by M. Winger, D. Trzesniak, R. Baron and W. F. van Gunsteren, Phys. Chem. Chem. Phys., 2009, 11, 1934
    • author reply 2257-8
    • S.J. Marrink, X. Periole, D.P. Tieleman, and A.H. de Vries Comment on "on using a too large integration time step in molecular dynamics simulations of coarse-grained molecular models" by M. Winger, D. Trzesniak, R. Baron and W. F. van Gunsteren, Phys. Chem. Chem. Phys., 2009, 11, 1934 Phys. Chem. Chem. Phys. 12 2010 2254 2256 author reply 2257-8
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 2254-2256
    • Marrink, S.J.1    Periole, X.2    Tieleman, D.P.3    De Vries, A.H.4
  • 33
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • S. Nose, and M.L. Klein Constant pressure molecular dynamics for molecular systems Mol. Phys. 50 1983 1055 1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 34
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 35
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • DOI 10.1063/1.328693
    • M. Parrinello, and A. Rahman Polymorphic transitions in single crystals: a new molecular dynamics method J. Appl. Phys. 52 1981 7182 7190 (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 36
    • 77950991422 scopus 로고    scopus 로고
    • LOOS: An extensible platform for the structural analysis of simulations
    • T.D. Romo, and A. Grossfield LOOS: an extensible platform for the structural analysis of simulations Conf. Proc. IEEE Eng. Med. Biol. Soc. 2009 2009 2332 2335
    • (2009) Conf. Proc. IEEE Eng. Med. Biol. Soc. , vol.2009 , pp. 2332-2335
    • Romo, T.D.1    Grossfield, A.2
  • 38
    • 50549097744 scopus 로고    scopus 로고
    • Assessing atomistic and coarse-grained force fields for protein-lipid interactions: The formidable challenge of an ionizable side chain in a membrane
    • I. Vorobyov, L. Li, and T.W. Allen Assessing atomistic and coarse-grained force fields for protein-lipid interactions: the formidable challenge of an ionizable side chain in a membrane J. Phys. Chem. B 112 2008 9588 9602
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9588-9602
    • Vorobyov, I.1    Li, L.2    Allen, T.W.3
  • 40
    • 33747241994 scopus 로고    scopus 로고
    • Generalized coarse-grained model based on point multipole and Gay-Berne potentials
    • P.A. Golubkov, and P. Ren Generalized coarse-grained model based on point multipole and Gay-Berne potentials J. Chem. Phys. 125 2006 64103
    • (2006) J. Chem. Phys. , vol.125 , pp. 64103
    • Golubkov, P.A.1    Ren, P.2
  • 41
    • 41549097838 scopus 로고    scopus 로고
    • A transferable coarse-grained model for hydrogen-bonding liquids
    • P.A. Golubkov, J.C. Wu, and P. Ren A transferable coarse-grained model for hydrogen-bonding liquids Phys. Chem. Chem. Phys. 10 2008 2050 2057
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2050-2057
    • Golubkov, P.A.1    Wu, J.C.2    Ren, P.3
  • 42
    • 45749113323 scopus 로고    scopus 로고
    • Aggregation of cateslytin β-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides?
    • DOI 10.1021/bi800448h
    • F. Jean-François, S. Castano, B. Desbat, B. Odaert, M. Roux, M.-H. Metz-Boutigue, and E.J. Dufourc Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. a new mode of action for antimicrobial peptides? Biochemistry 47 2008 6394 6402 (Pubitemid 351874231)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6394-6402
    • Jean-Francois, F.1    Castano, S.2    Desbat, B.3    Odaert, B.4    Roux, M.5    Metz-Boutigue, M.-H.6    Dufourc, E.J.7
  • 43
    • 77952362863 scopus 로고    scopus 로고
    • Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: Lipid clustering in anionic membranes
    • R.F. Epand, L. Maloy, A. Ramamoorthy, and R.M. Epand Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: lipid clustering in anionic membranes Biophys. J. 98 2010 2564 2573
    • (2010) Biophys. J. , vol.98 , pp. 2564-2573
    • Epand, R.F.1    Maloy, L.2    Ramamoorthy, A.3    Epand, R.M.4
  • 44
    • 60549086215 scopus 로고    scopus 로고
    • Peptide induced demixing in PG/PE lipid mixtures: A mechanism for the specificity of antimicrobial peptides towards bacterial membranes?
    • A. Arouri, M. Dathe, and A. Blume Peptide induced demixing in PG/PE lipid mixtures: a mechanism for the specificity of antimicrobial peptides towards bacterial membranes? Biochim. Biophys. Acta 1788 2009 650 659
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 650-659
    • Arouri, A.1    Dathe, M.2    Blume, A.3
  • 47
    • 79953790729 scopus 로고    scopus 로고
    • Bacterial membrane lipids in the action of antimicrobial agents
    • R.M. Epand, and R.F. Epand Bacterial membrane lipids in the action of antimicrobial agents J. Pept. Sci. 17 2011 298 305
    • (2011) J. Pept. Sci. , vol.17 , pp. 298-305
    • Epand, R.M.1    Epand, R.F.2
  • 48
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • R.M. Epand, and R.F. Epand Lipid domains in bacterial membranes and the action of antimicrobial agents Biochim. Biophys. Acta 1788 2009 289 294
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 50
    • 77955486396 scopus 로고    scopus 로고
    • Atomic-resolution simulations predict a transition state for vesicle fusion defined by contact of a few lipid tails
    • P.M. Kasson, E. Lindahl, and V.S. Pande Atomic-resolution simulations predict a transition state for vesicle fusion defined by contact of a few lipid tails PLoS Comput. Biol. 6 2010 e1000829
    • (2010) PLoS Comput. Biol. , vol.6 , pp. 1000829
    • Kasson, P.M.1    Lindahl, E.2    Pande, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.