메뉴 건너뛰기




Volumn 1838, Issue 3, 2014, Pages 968-977

RiDOM, a cell penetrating peptide. Interaction with phospholipid bilayers

Author keywords

Cell penetrating peptide; Melittin; Peptide membrane interaction; Pore formation; Thermodynamic; Transfection

Indexed keywords

1,2 DIOLEOYL SN GLYCERO 3 PHOSPHOETHANOLAMINE; GLYCEROPHOSPHOETHANOLAMINE; MELITTIN; NANOPARTICLE; UNCLASSIFIED DRUG;

EID: 84891762702     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.10.017     Document Type: Article
Times cited : (15)

References (52)
  • 1
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • E. Habermann Bee and wasp venoms Science 177 1972 314 322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 2
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation
    • G. Klocek, T. Schulthess, Y. Shai, and J. Seelig Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation Biochemistry 48 2009 2586 2596
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1    Schulthess, T.2    Shai, Y.3    Seelig, J.4
  • 3
    • 40149111869 scopus 로고    scopus 로고
    • Melittin interaction with sulfated cell surface sugars
    • DOI 10.1021/bi702258z
    • G. Klocek, and J. Seelig Melittin interaction with sulfated cell surface sugars Biochemistry 47 2008 2841 2849 (Pubitemid 351328835)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2841-2849
    • Klocek, G.1    Seelig, J.2
  • 5
    • 0019871670 scopus 로고
    • Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes
    • H. Vogel Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes FEBS Lett. 134 1981 37 42
    • (1981) FEBS Lett. , vol.134 , pp. 37-42
    • Vogel, H.1
  • 6
    • 84884528410 scopus 로고    scopus 로고
    • RiDOM, a cell penetrating peptide. Interaction with DNA and heparan sulfate
    • G. Québatte, E. Kitas, and J. Seelig riDOM, a cell penetrating peptide. Interaction with DNA and heparan sulfate J. Phys. Chem. B 117 2013 10807 10817
    • (2013) J. Phys. Chem. B , vol.117 , pp. 10807-10817
    • Québatte, G.1    Kitas, E.2    Seelig, J.3
  • 7
    • 33646152349 scopus 로고    scopus 로고
    • Melittin analogs with high lytic activity at endosomal pH enhance transfection with purified targeted PEI polyplexes
    • S. Boeckle, J. Fahrmeir, W. Roedl, M. Ogris, and E. Wagner Melittin analogs with high lytic activity at endosomal pH enhance transfection with purified targeted PEI polyplexes J. Control. Release 112 2006 240 248
    • (2006) J. Control. Release , vol.112 , pp. 240-248
    • Boeckle, S.1    Fahrmeir, J.2    Roedl, W.3    Ogris, M.4    Wagner, E.5
  • 8
    • 27644481173 scopus 로고    scopus 로고
    • C- versus N-terminally linked melittin-polyethylenimine conjugates: The site of linkage strongly influences activity of DNA polyplexes
    • DOI 10.1002/jgm.783
    • S. Boeckle, E. Wagner, and M. Ogris C- versus N-terminally linked melittin-polyethylenimine conjugates: the site of linkage strongly influences activity of DNA polyplexes J. Gene Med. 7 2005 1335 1347 (Pubitemid 41555439)
    • (2005) Journal of Gene Medicine , vol.7 , Issue.10 , pp. 1335-1347
    • Boeckle, S.1    Wagner, E.2    Ogris, M.3
  • 9
    • 0035861750 scopus 로고    scopus 로고
    • Melittin enables efficient vesicular escape and enhanced nuclear access of nonviral gene delivery vectors
    • M. Ogris, R.C. Carlisle, T. Bettinger, and L.W. Seymour Melittin enables efficient vesicular escape and enhanced nuclear access of nonviral gene delivery vectors J. Biol. Chem. 276 2001 47550 47555
    • (2001) J. Biol. Chem. , vol.276 , pp. 47550-47555
    • Ogris, M.1    Carlisle, R.C.2    Bettinger, T.3    Seymour, L.W.4
  • 10
    • 34548590395 scopus 로고    scopus 로고
    • A dimethylmaleic acid - Melittin-polylysine conjugate with reduced toxicity, pH-triggered endosomolytic activity and enhanced gene transfer potential
    • DOI 10.1002/jgm.1075
    • M. Meyer, A. Zintchenko, M. Ogris, and E. Wagner A dimethylmaleic acid-melittin-polylysine conjugate with reduced toxicity, pH-triggered endosomolytic activity and enhanced gene transfer potential J. Gene Med. 9 2007 797 805 (Pubitemid 47386864)
    • (2007) Journal of Gene Medicine , vol.9 , Issue.9 , pp. 797-805
    • Meyer, M.1    Zintchenko, A.2    Ogris, M.3    Wagner, E.4
  • 12
    • 0029562430 scopus 로고
    • Short-chain phospholipids enhance amphipathic peptide-mediated gene transfer
    • DOI 10.1006/bbrc.1995.2761
    • J.Y. Legendre, and A. Supersaxo Short-chain phospholipids enhance amphipathic peptide-mediated gene transfer Biochem. Biophys. Res. Commun. 217 1995 179 185 (Pubitemid 26004777)
    • (1995) Biochemical and Biophysical Research Communications , vol.217 , Issue.1 , pp. 179-185
    • Legendre, J.-Y.1    Supersaxo, A.2
  • 13
    • 0031041965 scopus 로고    scopus 로고
    • Dioleoylmelittin as a novel serum-insensitive reagent for efficient transfection of mammalian cells
    • DOI 10.1021/bc960076d
    • J.Y. Legendre, A. Trzeciak, B. Bohrmann, U. Deuschle, E. Kitas, and A. Supersaxo Dioleoylmelittin as a novel serum-insensitive reagent for efficient transfection of mammalian cells Bioconjug. Chem. 8 1997 57 63 (Pubitemid 27064223)
    • (1997) Bioconjugate Chemistry , vol.8 , Issue.1 , pp. 57-63
    • Legendre, J.Y.1    Trzeciak, A.2    Bohrmann, B.3    Deuschle, U.4    Kitas, E.5    Supersaxo, A.6
  • 15
    • 77953631991 scopus 로고    scopus 로고
    • Hybrids of nonviral vectors for gene delivery
    • S. Zhang, Y. Zhao, B. Zhao, and B. Wang Hybrids of nonviral vectors for gene delivery Bioconjug. Chem. 21 2010 1003 1009
    • (2010) Bioconjug. Chem. , vol.21 , pp. 1003-1009
    • Zhang, S.1    Zhao, Y.2    Zhao, B.3    Wang, B.4
  • 16
    • 0242642132 scopus 로고    scopus 로고
    • SEAP expression in transiently transfected mammalian cells grown in serum-free suspension culture
    • DOI 10.1023/A:1026125016602
    • E.J. Schlaeger, E.A. Kitas, and A. Dorn SEAP expression in transiently transfected mammalian cells grown in serum-free suspension culture Cytotechnology 42 2003 47 55 (Pubitemid 37372945)
    • (2003) Cytotechnology , vol.42 , Issue.1 , pp. 47-55
    • Schlaeger, E.-J.1    Kitas, E.A.2    Dorn, A.3
  • 17
    • 0028875452 scopus 로고
    • Recent developments in retro peptides and proteins - An ongoing topochemical exploration
    • M. Chorev, and M. Goodman Recent developments in retro peptides and proteins - an ongoing topochemical exploration Trends Biotechnol. 13 1995 438 445
    • (1995) Trends Biotechnol. , vol.13 , pp. 438-445
    • Chorev, M.1    Goodman, M.2
  • 18
    • 0011822184 scopus 로고    scopus 로고
    • Partially modified retro-inverso peptides: Development, synthesis, and conformational behavior
    • M.D. Fletcher, and M.M. Campbell Partially modified retro-inverso peptides: development, synthesis, and conformational behavior Chem. Rev. 98 1998 763 796
    • (1998) Chem. Rev. , vol.98 , pp. 763-796
    • Fletcher, M.D.1    Campbell, M.M.2
  • 19
    • 77954312965 scopus 로고    scopus 로고
    • The synthesis and characterization of lipophilic peptide-based carriers for gene delivery
    • D.J. Coles, A. Esposito, H.T. Chuah, and I. Toth The synthesis and characterization of lipophilic peptide-based carriers for gene delivery Tetrahedron 66 2010 5435 5441
    • (2010) Tetrahedron , vol.66 , pp. 5435-5441
    • Coles, D.J.1    Esposito, A.2    Chuah, H.T.3    Toth, I.4
  • 20
    • 58149187340 scopus 로고    scopus 로고
    • The characterization of a novel dendritic system for gene delivery by isothermal titration calorimetry
    • D.J. Coles, S. Yang, R.F. Minchin, and I. Toth The characterization of a novel dendritic system for gene delivery by isothermal titration calorimetry Biopolymers 90 2008 651 654
    • (2008) Biopolymers , vol.90 , pp. 651-654
    • Coles, D.J.1    Yang, S.2    Minchin, R.F.3    Toth, I.4
  • 21
    • 0037178127 scopus 로고    scopus 로고
    • Thermodynamics of cationic lipid binding to DNA and DNA condensation: Roles of electrostatics and hydrophobicity
    • DOI 10.1021/ja0124055
    • D. Matulis, I. Rouzina, and V.A. Bloomfield Thermodynamics of cationic lipid binding to DNA and DNA condensation: roles of electrostatics and hydrophobicity J. Am. Chem. Soc. 124 2002 7331 7342 (Pubitemid 34670442)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.25 , pp. 7331-7342
    • Matulis, D.1    Rouzina, I.2    Bloomfield, V.A.3
  • 22
    • 0344981527 scopus 로고    scopus 로고
    • Lipoplex Thermodynamics: Determination of DNA-Cationic Lipoid Interaction Energies
    • E. Pozharski, and R.C. MacDonald Lipoplex thermodynamics: determination of DNA-cationic lipoid interaction energies Biophys. J. 85 2003 3969 3978 (Pubitemid 37490306)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3969-3978
    • Pozharski, E.1    MacDonald, R.C.2
  • 23
    • 34447323868 scopus 로고    scopus 로고
    • High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA
    • DOI 10.1021/bi700416h
    • A. Ziegler, and J. Seelig High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA Biochemistry 46 2007 8138 8145 (Pubitemid 47051649)
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 8138-8145
    • Ziegler, A.1    Seelig, J.2
  • 24
    • 79958093000 scopus 로고    scopus 로고
    • Contributions of glycosaminoglycan binding and clustering to the biological uptake of the nonamphipathic cell-penetrating peptide WR9
    • A. Ziegler, and J. Seelig Contributions of glycosaminoglycan binding and clustering to the biological uptake of the nonamphipathic cell-penetrating peptide WR9 Biochemistry 50 2011 4650 4664
    • (2011) Biochemistry , vol.50 , pp. 4650-4664
    • Ziegler, A.1    Seelig, J.2
  • 25
    • 0242576091 scopus 로고    scopus 로고
    • Thermodynamic analysis of polycation-DNA interaction applying titration microcalorimetry
    • T. Ehtezazi, U. Rungsardthong, and S. Stolnik Thermodynamic analysis of polycation-DNA interaction applying titration microcalorimetry Langmuir 19 2003 9387 9394
    • (2003) Langmuir , vol.19 , pp. 9387-9394
    • Ehtezazi, T.1    Rungsardthong, U.2    Stolnik, S.3
  • 27
    • 79952197490 scopus 로고    scopus 로고
    • Thermodynamics of lipid interactions with cell-penetrating peptides
    • R. Sauder, J. Seelig, and A. Ziegler Thermodynamics of lipid interactions with cell-penetrating peptides Methods Mol. Biol. 683 2011 129 155
    • (2011) Methods Mol. Biol. , vol.683 , pp. 129-155
    • Sauder, R.1    Seelig, J.2    Ziegler, A.3
  • 28
    • 1542327642 scopus 로고    scopus 로고
    • Pathway for Polyarginine Entry into Mammalian Cells
    • DOI 10.1021/bi035933x
    • S.M. Fuchs, and R.T. Raines Pathway for polyarginine entry into mammalian cells Biochemistry 43 2004 2438 2444 (Pubitemid 38327839)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2438-2444
    • Fuchs, S.M.1    Raines, R.T.2
  • 29
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • M. Tyagi, M. Rusnati, M. Presta, and M. Giacca Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans J. Biol. Chem. 276 2001 3254 3261
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 30
    • 0037159193 scopus 로고    scopus 로고
    • Evidence for a plasma membrane-mediated permeability barrier to Tat basic domain in well-differentiated epithelial cells: Lack of correlation with heparan sulfate
    • DOI 10.1021/bi026097e
    • S. Violini, V. Sharma, J.L. Prior, M. Dyszlewski, and D. Piwnica-Worms Evidence for a plasma membrane-mediated permeability barrier to Tat basic domain in well-differentiated epithelial cells: lack of correlation with heparan sulfate Biochemistry 41 2002 12652 12661 (Pubitemid 35192494)
    • (2002) Biochemistry , vol.41 , Issue.42 , pp. 12652-12661
    • Violini, S.1    Sharma, V.2    Prior, J.L.3    Dyszlewski, M.4    Piwnica-Worms, D.5
  • 31
    • 11844293998 scopus 로고    scopus 로고
    • TAT derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: Optical, biophysical, and metabolic evidence
    • DOI 10.1021/bi0491604
    • A. Ziegler, P. Nervi, M. Durrenberger, and J. Seelig The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: optical, biophysical, and metabolic evidence Biochemistry 44 2005 138 148 (Pubitemid 40095715)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 138-148
    • Ziegler, A.1    Nervi, P.2    Durrenberger, M.3    Seelig, J.4
  • 32
    • 0031543338 scopus 로고    scopus 로고
    • A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism
    • DOI 10.1006/abio.1997.2355
    • J. Reed, and T.A. Reed A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism Anal. Biochem. 254 1997 36 40 (Pubitemid 27523226)
    • (1997) Analytical Biochemistry , vol.254 , Issue.1 , pp. 36-40
    • Reed, J.1    Reed, T.A.2
  • 33
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • DOI 10.1016/S0304-4157(97)00002-6, PII S0304415797000026
    • J. Seelig Titration calorimetry of lipid-peptide interactions Biochim. Biophys. Acta 1331 1997 103 116 (Pubitemid 27168150)
    • (1997) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1331 , Issue.1 , pp. 103-116
    • Seelig, J.1
  • 35
    • 77957067380 scopus 로고
    • Electrostatic potentials at membrane-solution interfaces
    • S.A. McLaughlin Electrostatic potentials at membrane-solution interfaces Curr. Top. Membr. Transp. 9 1977 71 144
    • (1977) Curr. Top. Membr. Transp. , vol.9 , pp. 71-144
    • McLaughlin, S.A.1
  • 36
    • 0024328774 scopus 로고
    • Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation
    • DOI 10.1021/bi00436a014
    • E. Kuchinka, and J. Seelig Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation Biochemistry 28 1989 4216 4221 (Pubitemid 19141622)
    • (1989) Biochemistry , vol.28 , Issue.10 , pp. 4216-4221
    • Kuchinka, E.1    Seelig, J.2
  • 37
    • 0025061113 scopus 로고
    • Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes
    • DOI 10.1021/bi00453a007
    • G. Beschiaschvili, and J. Seelig Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes Biochemistry 29 1990 52 58 (Pubitemid 20033706)
    • (1990) Biochemistry , vol.29 , Issue.1 , pp. 52-58
    • Beschiaschvili, G.1    Seelig, J.2
  • 38
    • 0027525276 scopus 로고
    • Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = +1 to z = +3
    • J. Seelig, S. Nebel, P. Ganz, and C. Bruns Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = + 1 to z = + 3 Biochemistry 32 1993 9714 9721 (Pubitemid 23296817)
    • (1993) Biochemistry , vol.32 , Issue.37 , pp. 9714-9721
    • Seelig, J.1    Nebel, S.2    Ganz, P.3    Bruns, C.4
  • 39
    • 0032539980 scopus 로고    scopus 로고
    • Magainin 2 amide interaction with lipid membranes: Calorimetric detection of peptide binding and pore formation
    • DOI 10.1021/bi972615n
    • M.R. Wenk, and J. Seelig Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation Biochemistry 37 1998 3909 3916 (Pubitemid 28162948)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3909-3916
    • Wenk, M.R.1    Seelig, J.2
  • 40
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium J. Mol. Biol. 294 1999 785 794
    • (1999) J. Mol. Biol. , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 41
    • 0034681140 scopus 로고    scopus 로고
    • Membrane binding and pore formation of the antibacterial peptide PGLa: Thermodynamic and mechanistic aspects
    • DOI 10.1021/bi992146k
    • T. Wieprecht, O. Apostolov, M. Beyermann, and J. Seelig Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects Biochemistry 39 2000 442 452 (Pubitemid 30056480)
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 442-452
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 42
    • 0033935281 scopus 로고    scopus 로고
    • Binding of the antibacterial peptide magainin 2 amide to small and large unilamellar vesicles
    • DOI 10.1016/S0301-4622(00)00120-4, PII S0301462200001204
    • T. Wieprecht, O. Apostolov, and J. Seelig Binding of the antibacterial peptide magainin 2 amide to small and large unilamellar vesicles Biophys. Chem. 85 2000 187 198 (Pubitemid 30445262)
    • (2000) Biophysical Chemistry , vol.85 , Issue.2-3 , pp. 187-198
    • Wieprecht, T.1    Apostolov, O.2    Seelig, J.3
  • 45
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • J. Seelig 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes Biochim. Biophys. Acta 515 1978 105 140 (Pubitemid 8398025)
    • (1978) Biochimica et Biophysica Acta , vol.515 , Issue.2 , pp. 105-140
    • Seelig, J.1
  • 46
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction
    • S.C. Quay, and C.C. Condie Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction Biochemistry 22 1983 695 700
    • (1983) Biochemistry , vol.22 , pp. 695-700
    • Quay, S.C.1    Condie, C.C.2
  • 47
    • 0027056421 scopus 로고
    • Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding
    • W. Wilcox, and D. Eisenberg Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding Protein Sci. 1 1992 641 653 (Pubitemid 23009199)
    • (1992) Protein Science , vol.1 , Issue.5 , pp. 641-653
    • Wilcox, W.1    Eisenberg, D.2
  • 48
    • 0026602028 scopus 로고
    • Mechanism of the conformational transition of melittin
    • Y. Goto, and Y. Hagihara Mechanism of the conformational transition of melittin Biochemistry 31 1992 732 738
    • (1992) Biochemistry , vol.31 , pp. 732-738
    • Goto, Y.1    Hagihara, Y.2
  • 49
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles
    • DOI 10.1021/bi971009p
    • S. Rex, and G. Schwarz Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles Biochemistry 37 1998 2336 2345 (Pubitemid 28119307)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 51
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • DOI 10.1021/bi00090a020
    • R.M. Peitzsch, and S. McLaughlin Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins Biochemistry 32 1993 10436 10443 (Pubitemid 23320168)
    • (1993) Biochemistry , vol.32 , Issue.39 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 52
    • 0029034233 scopus 로고
    • Thermodynamics of fatty acid binding to fatty acid-binding proteins and fatty acid partition between water and membranes measured using the fluorescent probe ADIFAB
    • G.V. Richieri, R.T. Ogata, and A.M. Kleinfeld Thermodynamics of fatty acid binding to fatty acid-binding proteins and fatty acid partition between water and membranes measured using the fluorescent probe ADIFAB J. Biol. Chem. 270 1995 15076 15084
    • (1995) J. Biol. Chem. , vol.270 , pp. 15076-15084
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.