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Volumn 109, Issue 5, 2015, Pages 936-947

PE and PS Lipids Synergistically Enhance Membrane Poration by a Peptide with Anticancer Properties

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; ANTINEOPLASTIC AGENT; LIPOSOME; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; POLYBIA-MPI, POLYBIA PAULISTA; WASP VENOM;

EID: 84940492448     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.07.033     Document Type: Article
Times cited : (108)

References (36)
  • 1
    • 67650421491 scopus 로고    scopus 로고
    • Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista
    • B.M. de Souza, and A.V. da Silva M.S. Palma Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista Peptides 30 2009 1387 1395
    • (2009) Peptides , vol.30 , pp. 1387-1395
    • De Souza, B.M.1    Da Silva, A.V.2    Palma, M.S.3
  • 2
    • 43049145799 scopus 로고    scopus 로고
    • Antitumor effects, cell selectivity and structure-activity relationship of a novel antimicrobial peptide polybia-MPI
    • K.R. Wang, and B.Z. Zhang 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    Wang, R.3
  • 3
    • 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, and J.X. Yan 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    Wang, R.3
  • 4
    • 84862580384 scopus 로고    scopus 로고
    • Influence of the bilayer composition on the binding and membrane disrupting effect of Polybia-MP1, an antimicrobial mastoparan peptide with leukemic T-lymphocyte cell selectivity
    • M.P. dos Santos Cabrera, and M. Arcisio-Miranda M.S. Palma Influence of the bilayer composition on the binding and membrane disrupting effect of Polybia-MP1, an antimicrobial mastoparan peptide with leukemic T-lymphocyte cell selectivity Biochemistry 51 2012 4898 4908
    • (2012) Biochemistry , vol.51 , pp. 4898-4908
    • Dos Santos Cabrera, M.P.1    Arcisio-Miranda, M.2    Palma, M.S.3
  • 5
    • 18544381354 scopus 로고    scopus 로고
    • Surface exposure of phosphatidylserine in pathological cells
    • R.F.A. Zwaal, P. Comfurius, and E.M. Bevers Surface exposure of phosphatidylserine in pathological cells Cell. Mol. Life Sci. 62 2005 971 988
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 971-988
    • Zwaal, R.F.A.1    Comfurius, P.2    Bevers, E.M.3
  • 6
    • 71749100398 scopus 로고    scopus 로고
    • Cationic amphiphilic peptides with cancer-selective toxicity
    • F. Schweizer Cationic amphiphilic peptides with cancer-selective toxicity Eur. J. Pharmacol. 625 2009 190 194
    • (2009) Eur. J. Pharmacol. , vol.625 , pp. 190-194
    • Schweizer, F.1
  • 7
    • 79953695111 scopus 로고    scopus 로고
    • Increased exposure of phosphatidylethanolamine on the surface of tumor vascular endothelium
    • J.H. Stafford, and P.E. Thorpe Increased exposure of phosphatidylethanolamine on the surface of tumor vascular endothelium Neoplasia 13 2011 299 308
    • (2011) Neoplasia , vol.13 , pp. 299-308
    • Stafford, J.H.1    Thorpe, P.E.2
  • 8
    • 79955669580 scopus 로고    scopus 로고
    • Antimicrobial peptides: Successes, challenges and unanswered questions
    • W.C. Wimley, and K. Hristova Antimicrobial peptides: successes, challenges and unanswered questions J. Membr. Biol. 239 2011 27 34
    • (2011) J. Membr. Biol. , vol.239 , pp. 27-34
    • Wimley, W.C.1    Hristova, K.2
  • 9
    • 84860601877 scopus 로고    scopus 로고
    • Antimicrobial peptides: Key components of the innate immune system
    • M. Pasupuleti, A. Schmidtchen, and M. Malmsten Antimicrobial peptides: key components of the innate immune system Crit. Rev. Biotechnol. 32 2012 143 171
    • (2012) Crit. Rev. Biotechnol. , vol.32 , pp. 143-171
    • Pasupuleti, M.1    Schmidtchen, A.2    Malmsten, M.3
  • 10
    • 84857411069 scopus 로고    scopus 로고
    • Designing antimicrobial peptides: Form follows function
    • C.D. Fjell, and J.A. Hiss G. Schneider Designing antimicrobial peptides: form follows function Nat. Rev. Drug Discov. 11 2012 37 51
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 37-51
    • Fjell, C.D.1    Hiss, J.A.2    Schneider, G.3
  • 11
    • 84878432085 scopus 로고    scopus 로고
    • Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers
    • P.D. Rakowska, and H. Jiang M.G. Ryadnov Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers Proc. Natl. Acad. Sci. USA 110 2013 8918 8923
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 8918-8923
    • Rakowska, P.D.1    Jiang, H.2    Ryadnov, M.G.3
  • 12
    • 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. de Souza, and M.A. Mendes M.S. Palma 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
    • De Souza, B.M.1    Mendes, M.A.2    Palma, M.S.3
  • 13
    • 0014779155 scopus 로고
    • Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • G. Rouser, S. Fkeischer, and A. Yamamoto Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots Lipids 5 1970 494 496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 14
    • 79952077574 scopus 로고    scopus 로고
    • A thermodynamic approach to the mechanism of cell-penetrating peptides in model membranes
    • A.N. McKeown, and J.L. Naro P.F. Almeida A thermodynamic approach to the mechanism of cell-penetrating peptides in model membranes Biochemistry 50 2011 654 662
    • (2011) Biochemistry , vol.50 , pp. 654-662
    • McKeown, A.N.1    Naro, J.L.2    Almeida, P.F.3
  • 15
    • 78650847371 scopus 로고    scopus 로고
    • Cationized albumin-biocoatings for the immobilization of lipid vesicles
    • S. Ritz, and K. Eisele E.K. Sinner Cationized albumin-biocoatings for the immobilization of lipid vesicles Biointerphases 5 2010 FA78 FA87
    • (2010) Biointerphases , vol.5 , pp. FA78-FA87
    • Ritz, S.1    Eisele, K.2    Sinner, E.K.3
  • 16
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • P. Schön, and A.J. García-Sáez P. Schwille Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence Biophys. J. 95 2008 691 698
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schön, P.1    García-Sáez, A.J.2    Schwille, P.3
  • 18
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching
    • A.S. Ladokhin, W.C. Wimley, and S.H. White Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching Biophys. J. 69 1995 1964 1971
    • (1995) Biophys. J. , vol.69 , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 19
    • 0032803785 scopus 로고    scopus 로고
    • Pore-forming action of mastoparan peptides on liposomes: A quantitative analysis
    • A. Arbuzova, and G. Schwarz Pore-forming action of mastoparan peptides on liposomes: a quantitative analysis Biochim. Biophys. Acta 1420 1999 139 152
    • (1999) Biochim. Biophys. Acta , vol.1420 , pp. 139-152
    • Arbuzova, A.1    Schwarz, G.2
  • 20
    • 0029731358 scopus 로고    scopus 로고
    • Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH-sensitive peptide
    • F. Nicol, S. Nir, and F.C. Szoka Jr. Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH-sensitive peptide Biophys. J. 71 1996 3288 3301
    • (1996) Biophys. J. , vol.71 , pp. 3288-3301
    • Nicol, F.1    Nir, S.2    Szoka, F.C.3
  • 21
    • 67049119439 scopus 로고    scopus 로고
    • Distinct mechanisms of lipid bilayer perturbation induced by peptides derived from the membrane-proximal external region of HIV-1 gp41
    • B. Apellániz, S. Nir, and J.L. Nieva Distinct mechanisms of lipid bilayer perturbation induced by peptides derived from the membrane-proximal external region of HIV-1 gp41 Biochemistry 48 2009 5320 5331
    • (2009) Biochemistry , vol.48 , pp. 5320-5331
    • Apellániz, B.1    Nir, S.2    Nieva, J.L.3
  • 22
    • 78649761049 scopus 로고    scopus 로고
    • All-or-none versus graded: Single-vesicle analysis reveals lipid composition effects on membrane permeabilization
    • B. Apellániz, and J.L. Nieva A.J. García-Sáez All-or-none versus graded: single-vesicle analysis reveals lipid composition effects on membrane permeabilization Biophys. J. 99 2010 3619 3628
    • (2010) Biophys. J. , vol.99 , pp. 3619-3628
    • Apellániz, B.1    Nieva, J.L.2    García-Sáez, A.J.3
  • 23
    • 78349267221 scopus 로고    scopus 로고
    • Pores formed by Baxα5 relax to a smaller size and keep at equilibrium
    • G. Fuertes, and A.J. García-Sáez J. Salgado Pores formed by Baxα5 relax to a smaller size and keep at equilibrium Biophys. J. 99 2010 2917 2925
    • (2010) Biophys. J. , vol.99 , pp. 2917-2925
    • Fuertes, G.1    García-Sáez, A.J.2    Salgado, J.3
  • 24
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • K. Matsuzaki, and O. Murase K. Miyajima An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation Biochemistry 35 1996 11361 11368
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 25
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • K. Matsuzaki, and O. Murase K. Miyajima Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore Biochemistry 34 1995 6521 6526
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 26
    • 48249157851 scopus 로고    scopus 로고
    • Biomolecular engineering by combinatorial design and high-throughput screening: Small, soluble peptides that permeabilize membranes
    • R. Rathinakumar, and W.C. Wimley Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes J. Am. Chem. Soc. 130 2008 9849 9858
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9849-9858
    • Rathinakumar, R.1    Wimley, W.C.2
  • 27
    • 58849140539 scopus 로고    scopus 로고
    • Magainin 2 revisited: A test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles
    • S.M. Gregory, A. Pokorny, and P.F.F. Almeida Magainin 2 revisited: a test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles Biophys. J. 96 2009 116 131
    • (2009) Biophys. J. , vol.96 , pp. 116-131
    • Gregory, S.M.1    Pokorny, A.2    Almeida, P.F.F.3
  • 28
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles
    • S. Rex, and G. Schwarz Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles Biochemistry 37 1998 2336 2345
    • (1998) Biochemistry , vol.37 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 30
    • 77956761543 scopus 로고    scopus 로고
    • Kinetic pathway of antimicrobial peptide magainin 2-induced pore formation in lipid membranes
    • Y. Tamba, and H. Ariyama M. Yamazaki Kinetic pathway of antimicrobial peptide magainin 2-induced pore formation in lipid membranes J. Phys. Chem. B 114 2010 12018 12026
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12018-12026
    • Tamba, Y.1    Ariyama, H.2    Yamazaki, M.3
  • 31
    • 84880503720 scopus 로고    scopus 로고
    • Materials characterization of the low temperature sensitive liposome (LTSL): Effects of the lipid composition (lysolipid and DSPE-PEG2000) on the thermal transition and release of doxorubicin
    • 563-589
    • D. Needham, and J.Y. Park J. Tong Materials characterization of the low temperature sensitive liposome (LTSL): effects of the lipid composition (lysolipid and DSPE-PEG2000) on the thermal transition and release of doxorubicin Faraday Discuss. 161 2013 515 534 563-589
    • (2013) Faraday Discuss. , vol.161 , pp. 515-534
    • Needham, D.1    Park, J.Y.2    Tong, J.3
  • 32
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • H.W. Huang Action of antimicrobial peptides: two-state model Biochemistry 39 2000 8347 8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 33
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • D. Sengupta, and H. Leontiadou S.J. Marrink Toroidal pores formed by antimicrobial peptides show significant disorder Biochim. Biophys. Acta 1778 2008 2308 2317
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Marrink, S.J.3
  • 34
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • M.T. Lee, and W.C. Hung H.W. Huang Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides Proc. Natl. Acad. Sci. USA 105 2008 5087 5092
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5087-5092
    • Lee, M.T.1    Hung, W.C.2    Huang, H.W.3
  • 35
    • 84876274935 scopus 로고    scopus 로고
    • Cytochrome c causes pore formation in cardiolipin-containing membranes
    • C.L. Bergstrom, and P.A. Beales J.T. Groves Cytochrome c causes pore formation in cardiolipin-containing membranes Proc. Natl. Acad. Sci. USA 110 2013 6269 6274
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 6269-6274
    • Bergstrom, C.L.1    Beales, P.A.2    Groves, J.T.3
  • 36
    • 67649256037 scopus 로고    scopus 로고
    • Control of cell selectivity of antimicrobial peptides
    • K. Matsuzaki Control of cell selectivity of antimicrobial peptides Biochim. Biophys. Acta. 1788 2009 1687 1692
    • (2009) Biochim. Biophys. Acta. , vol.1788 , pp. 1687-1692
    • Matsuzaki, K.1


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