메뉴 건너뛰기




Volumn 39, Issue 1, 2013, Pages 80-88

Membrane active antimicrobial activity and molecular dynamics study of a novel cationic antimicrobial peptide polybia-MPI, from the venom of Polybia paulista

Author keywords

Membrane perturbation; Molecular dynamics study; Polybia MPI; Resistant bacteria

Indexed keywords

POLYBIA MPI DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84871394570     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2012.11.002     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 0001585978 scopus 로고    scopus 로고
    • Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems
    • K. Anton, H. Feenstra Berk, and J.C.B. Herman Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems J Comput Chem 20 1999 786 798
    • (1999) J Comput Chem , vol.20 , pp. 786-798
    • Anton, K.1    Feenstra Berk, H.2    Herman, J.C.B.3
  • 3
    • 35848962760 scopus 로고    scopus 로고
    • Activity of an antimicrobial peptide mimetic against planktonic and biofilm cultures of oral pathogens
    • N. Beckloff, D. Laube, T. Castro, D. Furgang, S. Park, and D. Perlin Activity of an antimicrobial peptide mimetic against planktonic and biofilm cultures of oral pathogens Antimicrob Agents Chemther 51 2007 4125 4132
    • (2007) Antimicrob Agents Chemther , vol.51 , pp. 4125-4132
    • Beckloff, N.1    Laube, D.2    Castro, T.3    Furgang, D.4    Park, S.5    Perlin, D.6
  • 5
  • 6
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • O. Berger, O. Edholm, and F. Jähnig Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys J 72 1997 2002 2013
    • (1997) Biophys J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jähnig, F.3
  • 8
    • 54849405417 scopus 로고    scopus 로고
    • Self-assembly of a simple membrane protein: Coarse-grained molecular dynamics simulations of the influenza M2 channel
    • T. Carpenter, P.J. Bond, S. Khalid, and M.S.P. Sansom Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel Biophys J 95 2008 3790 3801
    • (2008) Biophys J , vol.95 , pp. 3790-3801
    • Carpenter, T.1    Bond, P.J.2    Khalid, S.3    Sansom, M.S.P.4
  • 9
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems J Chem Phys 98 1993 10089 10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 10
    • 0000112789 scopus 로고    scopus 로고
    • Molecular-dynamics simulations of a fully hydrated dipalmitoyl phosphatidylcholine bilayer with different macroscopic boundary-conditions and parameters
    • T. DP, and B. H.J Molecular-dynamics simulations of a fully hydrated dipalmitoyl phosphatidylcholine bilayer with different macroscopic boundary-conditions and parameters J Chem Phys 105 1996 4871 4880
    • (1996) J Chem Phys , vol.105 , pp. 4871-4880
    • Dp, T.1    B, H.J.2
  • 11
    • 0035646087 scopus 로고    scopus 로고
    • Implicit two-phase solvation model as a tool to assess conformation and energetics of proteins in membrane-mimetic media
    • R. Efremov, P. Volynsky, D. Nolde, G. Vergoten, and A. Arseniev Implicit two-phase solvation model as a tool to assess conformation and energetics of proteins in membrane-mimetic media Theor Chem Acc: Theor Comput Model 106 2001 48 54
    • (2001) Theor Chem Acc: Theor Comput Model , vol.106 , pp. 48-54
    • Efremov, R.1    Volynsky, P.2    Nolde, D.3    Vergoten, G.4    Arseniev, A.5
  • 13
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • G.B. Fields, and R.L. Noble 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
  • 14
    • 0019335817 scopus 로고
    • The amino acid sequence of the delta haemolysin of Staphylococcus aureus
    • J.E. Fitton, A. Dell, and W.V. Shaw The amino acid sequence of the delta haemolysin of Staphylococcus aureus FEBS Lett 115 1980 209 212
    • (1980) FEBS Lett , vol.115 , pp. 209-212
    • Fitton, J.E.1    Dell, A.2    Shaw, W.V.3
  • 15
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • B. Pullman, D. Reidel Publishing Company Dordrecht
    • H.J.C. Berendsen, J.P.M. Postma, W.Fv. Gunsteren, and J. Hermans Interaction models for water in relation to protein hydration B. Pullman, Intermolecular forces 1981 D. Reidel Publishing Company Dordrecht 331 342
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Gunsteren, W.Fv.3    Hermans, J.4
  • 20
    • 33748908201 scopus 로고    scopus 로고
    • Chitosan derivatives killed bacteria by disrupting the outer and inner membrane
    • J.-Y. Je, and S.-K. Kim Chitosan derivatives killed bacteria by disrupting the outer and inner membrane J Agric Food Chem 54 2006 6629 6633
    • (2006) J Agric Food Chem , vol.54 , pp. 6629-6633
    • Je, J.-Y.1    Kim, S.-K.2
  • 21
    • 58749101895 scopus 로고    scopus 로고
    • Pore formation induced by an antimicrobial peptide: Electrostatic effects
    • F. Jean-François, J. Elezgaray, P. Berson, P. Vacher, and E.J. Dufourc Pore formation induced by an antimicrobial peptide: electrostatic effects Biophys J 95 2008 5748 5756
    • (2008) Biophys J , vol.95 , pp. 5748-5756
    • Jean-François, F.1    Elezgaray, J.2    Berson, P.3    Vacher, P.4    Dufourc, E.J.5
  • 22
    • 1042267271 scopus 로고    scopus 로고
    • Implicit solvent model estimates of the stability of model structures of the alamethicin channel
    • A. Kessel, D.P. Tieleman, and N. Ben-Tal Implicit solvent model estimates of the stability of model structures of the alamethicin channel Eur Biophys J 33 2004 16 28
    • (2004) Eur Biophys J , vol.33 , pp. 16-28
    • Kessel, A.1    Tieleman, D.P.2    Ben-Tal, N.3
  • 23
    • 3042737827 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptides for cancer treatments
    • C. Leuschner, and W. Hansel Membrane disrupting lytic peptides for cancer treatments Curr Pharm Des 10 2004 2299 2310
    • (2004) Curr Pharm des , vol.10 , pp. 2299-2310
    • Leuschner, C.1    Hansel, W.2
  • 24
    • 0031880829 scopus 로고    scopus 로고
    • Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations
    • S.-J. Marrink, O. Berger, P. Tieleman, and F. Jähnig Adhesion forces of lipids in a phospholipid membrane studied by molecular dynamics simulations Biophys J 74 1998 931 943
    • (1998) Biophys J , vol.74 , pp. 931-943
    • Marrink, S.-J.1    Berger, O.2    Tieleman, P.3    Jähnig, F.4
  • 25
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: A unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • M. Miteva, M. Andersson, A. Karshikoff, and G. Otting Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin FEBS Lett 462 1999 155 158
    • (1999) FEBS Lett , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 26
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • S. Miyamoto, and P.A. Kollman Settle: an analytical version of the SHAKE and RATTLE algorithm for rigid water models J Comput Chem 13 1992 952 962
    • (1992) J Comput Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 27
    • 0037157179 scopus 로고    scopus 로고
    • Production of a recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system
    • C. Morassutti, F. De Amicis, B. Skerlavaj, M. Zanetti, and S. Marchetti Production of a recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system FEBS Lett 519 2002 141 146
    • (2002) FEBS Lett , vol.519 , pp. 141-146
    • Morassutti, C.1    De Amicis, F.2    Skerlavaj, B.3    Zanetti, M.4    Marchetti, S.5
  • 28
    • 0031005930 scopus 로고    scopus 로고
    • A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity
    • Z. Oren, J. Hong, and Y. Shai A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity J Biol Chem 272 1997 14643 14649
    • (1997) J Biol Chem , vol.272 , pp. 14643-14649
    • Oren, Z.1    Hong, J.2    Shai, Y.3
  • 29
    • 0035913957 scopus 로고    scopus 로고
    • Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata
    • S. Park, S.-H. Park, H.-C. Ahn, S. Kim, S.S. Kim, and B.J. Lee Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata FEBS Lett 507 2001 95 100
    • (2001) FEBS Lett , vol.507 , pp. 95-100
    • Park, S.1    Park, S.-H.2    Ahn, H.-C.3    Kim, S.4    Kim, S.S.5    Lee, B.J.6
  • 30
    • 0036286655 scopus 로고    scopus 로고
    • Computer simulation studies of model biological membranes
    • L. Saiz, and M.L. Klein Computer simulation studies of model biological membranes Acc Chem Res 35 2002 482 489
    • (2002) Acc Chem Res , vol.35 , pp. 482-489
    • Saiz, L.1    Klein, M.L.2
  • 31
    • 27744473974 scopus 로고    scopus 로고
    • Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista
    • B.M. Souza, M.A. Mendes, L.D. Santos, M.R. Marques, L.M.M. César, and R.N.A. Almeida Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista Peptides 26 2005 2157 2164
    • (2005) Peptides , vol.26 , pp. 2157-2164
    • Souza, B.M.1    Mendes, M.A.2    Santos, L.D.3    Marques, M.R.4    César, L.M.M.5    Almeida, R.N.A.6
  • 32
    • 62549111695 scopus 로고    scopus 로고
    • Interaction of MDpep9, a novel antimicrobial peptide from Chinese traditional edible larvae of housefly, with Escherichia coli genomic DNA
    • Y.-L. Tang, Y.-H. Shi, W. Zhao, G. Hao, and G.-W. Le Interaction of MDpep9, a novel antimicrobial peptide from Chinese traditional edible larvae of housefly, with Escherichia coli genomic DNA Food Chem 115 2009 867 872
    • (2009) Food Chem , vol.115 , pp. 867-872
    • Tang, Y.-L.1    Shi, Y.-H.2    Zhao, W.3    Hao, G.4    Le, G.-W.5
  • 33
    • 0025743796 scopus 로고
    • Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes
    • T. Utsugi, A.J. Schroit, J. Connor, C.D. Bucana, and I.J. Fidler Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes Cancer Res 51 1991 3062 3066
    • (1991) Cancer Res , vol.51 , pp. 3062-3066
    • Utsugi, T.1    Schroit, A.J.2    Connor, J.3    Bucana, C.D.4    Fidler, I.J.5
  • 34
    • 0025952233 scopus 로고
    • Occurrence and stability of insertion sequences in Mycobacterium tuberculosis complex strains: Evaluation of an insertion sequence-dependent DNA polymorphism as a tool in the epidemiology of tuberculosis
    • D. van Soolingen, P.W. Hermans, P.E. de Haas, D.R. Soll, and J.D. van Embden Occurrence and stability of insertion sequences in Mycobacterium tuberculosis complex strains: evaluation of an insertion sequence-dependent DNA polymorphism as a tool in the epidemiology of tuberculosis J Clin Microbiol 29 1991 2578 2586
    • (1991) J Clin Microbiol , vol.29 , pp. 2578-2586
    • Van Soolingen, D.1    Hermans, P.W.2    De Haas, P.E.3    Soll, D.R.4    Van Embden, J.D.5
  • 35
    • 63649150812 scopus 로고    scopus 로고
    • Novel mode of action of polybia-MPI, a novel antimicrobial peptide, in multi-drug resistant leukemic cells
    • K.R. Wang, J.X. Yan, B.Z. Zhang, J.J. Song, P.F. Jia, and R. Wang Novel mode of action of polybia-MPI, a novel antimicrobial peptide, in multi-drug resistant leukemic cells Cancer Lett 278 2009 65 72
    • (2009) Cancer Lett , vol.278 , pp. 65-72
    • Wang, K.R.1    Yan, J.X.2    Zhang, B.Z.3    Song, J.J.4    Jia, P.F.5    Wang, R.6
  • 36
    • 43049145799 scopus 로고    scopus 로고
    • Antitumor effects, cell selectivity and structure-activity relationship of a novel antimicrobial peptide polybia-MPI
    • K.R. Wang, B.Z. Zhang, W. Zhang, J.X. Yan, J. Li, and R. Wang Antitumor effects, cell selectivity and structure-activity relationship of a novel antimicrobial peptide polybia-MPI Peptides 29 2008 963 968
    • (2008) Peptides , vol.29 , pp. 963-968
    • Wang, K.R.1    Zhang, B.Z.2    Zhang, W.3    Yan, J.X.4    Li, J.5    Wang, R.6
  • 37
    • 84861148326 scopus 로고    scopus 로고
    • Membrane-active action mode of polybia-CP, a novel antimicrobial peptide isolated from the venom of Polybia paulista
    • K.R. Wang, J.X. Yan, R. Chen, W. Dang, B.Z. Zhang, and W. Zhang Membrane-active action mode of polybia-CP, a novel antimicrobial peptide isolated from the venom of Polybia paulista Antimicrob Agents Chemother 56 2012 3318 3323
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 3318-3323
    • Wang, K.R.1    Yan, J.X.2    Chen, R.3    Dang, W.4    Zhang, B.Z.5    Zhang, W.6
  • 38
    • 79961029521 scopus 로고    scopus 로고
    • Novel cytotoxity exhibition mode of polybia-CP, a novel antimicrobial peptide from the venom of the social wasp Polybia paulista
    • K.R. Wang, J.X. Yan, X. Liu, J.D. Zhang, R. Chen, and B.Z. Zhang Novel cytotoxity exhibition mode of polybia-CP, a novel antimicrobial peptide from the venom of the social wasp Polybia paulista Toxicology 288 2011 27 33
    • (2011) Toxicology , vol.288 , pp. 27-33
    • Wang, K.R.1    Yan, J.X.2    Liu, X.3    Zhang, J.D.4    Chen, R.5    Zhang, B.Z.6
  • 39
    • 70349495710 scopus 로고    scopus 로고
    • Interactions of antimicrobial peptide from C-terminus of myotoxin II with phospholipid mono- and bilayers
    • A. Won, and A. Ianoul Interactions of antimicrobial peptide from C-terminus of myotoxin II with phospholipid mono- and bilayers Biochim Biophys Acta: Biomembr 1788 2009 2277 2283
    • (2009) Biochim Biophys Acta: Biomembr , vol.1788 , pp. 2277-2283
    • Won, A.1    Ianoul, A.2
  • 40
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 41
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • L. Zhang, A. Rozek, and R.E.W. Hancock Interaction of cationic antimicrobial peptides with model membranes J Biol Chem 276 2001 35714 35722
    • (2001) J Biol Chem , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.W.3
  • 42
    • 77956665511 scopus 로고    scopus 로고
    • A novel analog of antimicrobial peptide polybia-MPI, with thioamide bond substitution, exhibits increased therapeutic efficacy against cancer and diminished toxicity in mice
    • W. Zhang, J. Li, L. Liu, K. Wang, J. Song, and J. Yan A novel analog of antimicrobial peptide polybia-MPI, with thioamide bond substitution, exhibits increased therapeutic efficacy against cancer and diminished toxicity in mice Peptides 31 2010 1832 1838
    • (2010) Peptides , vol.31 , pp. 1832-1838
    • Zhang, W.1    Li, J.2    Liu, L.3    Wang, K.4    Song, J.5    Yan, J.6
  • 43
    • 33846846337 scopus 로고    scopus 로고
    • Atomic-scale structure and electrostatics of anionic palmitoyloleoylphosphatidylglycerol lipid bilayers with Na+ counterions
    • W. Zhao, T. Róg, A.A. Gurtovenko, I. Vattulainen, and M. Karttunen Atomic-scale structure and electrostatics of anionic palmitoyloleoylphosphatidylglycerol lipid bilayers with Na+ counterions Biophys J 92 2007 1114 1124
    • (2007) Biophys J , vol.92 , pp. 1114-1124
    • Zhao, W.1    Róg, T.2    Gurtovenko, A.A.3    Vattulainen, I.4    Karttunen, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.