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Volumn 50, Issue 23, 2011, Pages 5195-5207

Determinants of membrane activity from mutational analysis of the HIV fusion peptide

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR DELIVERY; FUSION PEPTIDES; HYDROPHOBIC PEPTIDES; LIPID MIXING; MEMBRANE ACTIVITY; MEMBRANE FUSION; MUTATIONAL ANALYSIS; SECONDARY STRUCTURES; SEQUENCE VARIATIONS; VIRAL INFECTIVITY;

EID: 79958793992     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200696s     Document Type: Article
Times cited : (10)

References (90)
  • 1
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • DOI 10.1038/387426a0
    • Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., and Wiley, D. C. (1997) Atomic structure of the ectodomain from HIV-1 gp41 Nature (London) 387, 426-430 (Pubitemid 27227210)
    • (1997) Nature , vol.387 , Issue.6631 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3    Skehel, J.J.4    Wiley, D.C.5
  • 4
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (1997) Core structure of gp41 from the HIV envelope glycoprotein Cell (Cambridge, MA, U. S.) 89, 263-273 (Pubitemid 27199898)
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 8
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • DOI 10.1038/nsb0498-276
    • Furuta, R. A., Wild, C. T., Weng, Y., and Weiss, C. D. (1998) Capture of an early fusion-active conformation of HIV-1 gp41 Nat. Struct. Biol. 5, 276-279 (Pubitemid 28164878)
    • (1998) Nature Structural Biology , vol.5 , Issue.4 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 9
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • DOI 10.1083/jcb.140.2.315
    • Munoz-Barroso, I., Durell, S., Sakaguchi, K., Appella, E., and Blumenthal, R. (1998) Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41 J. Cell Biol. 140, 315-323 (Pubitemid 28078395)
    • (1998) Journal of Cell Biology , vol.140 , Issue.2 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 10
    • 33646185493 scopus 로고    scopus 로고
    • Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells
    • Yang, X., Kurteva, S., Ren, X., Lee, S., and Sodroski, J. (2006) Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells J. Virol. 80, 4388-4395
    • (2006) J. Virol. , vol.80 , pp. 4388-4395
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 12
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • DOI 10.1146/annurev.biochem.70.1.777
    • Eckert, D. M. and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition Annu. Rev. Biochem. 70, 777-810 (Pubitemid 32662225)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 14
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • White, J. M., Delos, S. E., Brecher, M., and Schornberg, K. (2008) Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme Crit. Rev. Biochem. Mol. Biol. 43, 189-219 (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 15
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • DOI 10.1021/bi00486a020
    • Rafalski, M., Lear, J. D., and DeGrado, W. F. (1990) Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41 Biochemistry 29, 7917-7922 (Pubitemid 20281241)
    • (1990) Biochemistry , vol.29 , Issue.34 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, W.F.3
  • 16
    • 0026743982 scopus 로고
    • The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation
    • Gordon, L. M., Curtain, C. C., Zhong, Y. C., Kirkpatrick, A., Mobley, P. W., and Waring, A. J. (1992) The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation Biochim. Biophys. Acta, Mol. Basis Dis. 1139, 257-274
    • (1992) Biochim. Biophys. Acta, Mol. Basis Dis. , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 20
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • DOI 10.1038/nrm2417, PII NRM2417
    • Martens, S. and McMahon, H. T. (2008) Mechanisms of membrane fusion: disparate players and common principles Nat. Rev. Mol. Cell Biol. 9, 543-556 (Pubitemid 351881838)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.7 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 21
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • DOI 10.1126/science.1142614
    • Martens, S., Kozlov, M. M., and McMahon, H. T. (2007) How Synaptotagmin Promotes Membrane Fusion Science (Washington, D. C.) 316, 1205-1208 (Pubitemid 46877485)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 22
  • 24
    • 34548726186 scopus 로고    scopus 로고
    • HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates
    • DOI 10.1529/biophysj.107.109181
    • Tristram-Nagle, S. and Nagle, J. F. (2007) HIV-1 Fusion Peptide Decreases Bending Energy and Promotes Curved Fusion Intermediates Biophys. J. 93, 2048-2055 (Pubitemid 47437587)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 2048-2055
    • Tristram-Nagle, S.1    Nagle, J.F.2
  • 25
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptides and the mechanism of viral fusion
    • DOI 10.1016/S0005-2736(03)00169-X
    • Epand, R. M. (2003) Fusion peptides and the mechanism of viral fusion Biochim. Biophys. Acta, Biomembr. 1614, 116-121 (Pubitemid 36851609)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1614 , Issue.1 , pp. 116-121
    • Epand, R.M.1
  • 26
    • 0034462310 scopus 로고    scopus 로고
    • Modulation of membrane curvature by peptides
    • DOI 10.1002/1097-0282(2000)55:5<358::AID-BIP1009>3.0.CO;2-8
    • Epand, R. M. and Epand, R. F. (2001) Modulation of membrane curvature by peptides Biopolymers 55, 358-363 (Pubitemid 32246521)
    • (2000) Biopolymers - Peptide Science Section , vol.55 , Issue.5 , pp. 358-363
    • Epand, R.M.1    Epand, R.F.2
  • 28
    • 0019890491 scopus 로고
    • Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3.ANG. resolution
    • Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981) Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3.ANG. resolution Nature 289, 366-373
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 29
    • 0023915219 scopus 로고
    • Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid
    • Weis, W., Brown, J. H., Cusack, S., Paulson, J. C., Skehel, J. J., and Wiley, D. C. (1988) Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid Nature 333, 426-431
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 30
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • DOI 10.1038/371037a0
    • Bullough, P. A., Hughson, F. M., Skehel, J. J., and Wiley, D. C. (1994) Structure of influenza haemagglutinin at the pH of membrane fusion Nature 371, 37-43 (Pubitemid 24277462)
    • (1994) Nature , vol.371 , Issue.6492 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 31
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • DOI 10.1016/0092-8674(93)90260-W
    • Carr, C. M. and Kim, P. S. (1993) A spring-loaded mechanism for the conformational change of influenza hemagglutinin Cell 73, 823-832 (Pubitemid 23159019)
    • (1993) Cell , vol.73 , Issue.4 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 32
    • 0034700147 scopus 로고    scopus 로고
    • A host-guest system to study structure-function relationships of membrane fusion peptides
    • Han, X. and Tamm, L. K. (2000) A host-guest system to study structure-function relationships of membrane fusion peptides Proc. Natl. Acad. Sci. U. S. A. 97, 13097-13102
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13097-13102
    • Han, X.1    Tamm, L.K.2
  • 33
    • 34547652634 scopus 로고    scopus 로고
    • Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers
    • DOI 10.1529/biophysj.106.102335
    • Li, Y. and Tamm, L. K. (2007) Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers Biophys. J. 93, 876-885 (Pubitemid 47219779)
    • (2007) Biophysical Journal , vol.93 , Issue.3 , pp. 876-885
    • Li, Y.1    Tamm, L.K.2
  • 34
    • 42949163133 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries
    • DOI 10.1021/ja077302m
    • Qiang, W., Bodner, M. L., and Weliky, D. P. (2008) Solid-State NMR Spectroscopy of Human Immunodeficiency Virus Fusion Peptides Associated with Host-Cell-Like Membranes: 2D Correlation Spectra and Distance Measurements Support a Fully Extended Conformation and Models for Specific Antiparallel Strand Registries J. Am. Chem. Soc. 130, 5459-5471 (Pubitemid 351612954)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.16 , pp. 5459-5471
    • Qiang, W.1    Bodner, M.L.2    Weliky, D.P.3
  • 35
    • 77249112159 scopus 로고    scopus 로고
    • Comparative Analysis of Membrane-Associated Fusion Peptide Secondary Structure and Lipid Mixing Function of HIV gp41 Constructs that Model the Early Pre-Hairpin Intermediate and Final Hairpin Conformations
    • Sackett, K., Nethercott, M. J., Epand, R. F., Epand, R. M., Kindra, D. R., Shai, Y., and Weliky, D. P. (2010) Comparative Analysis of Membrane-Associated Fusion Peptide Secondary Structure and Lipid Mixing Function of HIV gp41 Constructs that Model the Early Pre-Hairpin Intermediate and Final Hairpin Conformations J. Mol. Biol. 397, 301-315
    • (2010) J. Mol. Biol. , vol.397 , pp. 301-315
    • Sackett, K.1    Nethercott, M.J.2    Epand, R.F.3    Epand, R.M.4    Kindra, D.R.5    Shai, Y.6    Weliky, D.P.7
  • 36
    • 65249174493 scopus 로고    scopus 로고
    • Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs
    • Sackett, K., Nethercott, M. J., Shai, Y., and Weliky, D. P. (2009) Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs Biochemistry 48, 2714-2722
    • (2009) Biochemistry , vol.48 , pp. 2714-2722
    • Sackett, K.1    Nethercott, M.J.2    Shai, Y.3    Weliky, D.P.4
  • 37
    • 78650317603 scopus 로고    scopus 로고
    • Major Antiparallel and Minor Parallel beta Sheet Populations Detected in the Membrane-Associated Human Immunodeficiency Virus Fusion Peptide
    • Schmick, S. D. and Weliky, D. P. (2010) Major Antiparallel and Minor Parallel beta Sheet Populations Detected in the Membrane-Associated Human Immunodeficiency Virus Fusion Peptide Biochemistry 49, 10623-10635
    • (2010) Biochemistry , vol.49 , pp. 10623-10635
    • Schmick, S.D.1    Weliky, D.P.2
  • 38
    • 4444320707 scopus 로고    scopus 로고
    • Oligomeric β-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers
    • DOI 10.1529/biophysj.103.028530
    • Yang, J., Prorok, M., Castellino, F. J., and Weliky, D. P. (2004) Oligomeric beta -structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers Biophys. J. 87, 1951-1963 (Pubitemid 39167049)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1951-1963
    • Yang, J.1    Prorok, M.2    Castellino, F.J.3    Weliky, D.P.4
  • 39
    • 34247209161 scopus 로고    scopus 로고
    • A critical evaluation of the conformational requirements of fusogenic peptides in membranes
    • DOI 10.1007/s00249-006-0106-2, Klaus Arnold Special Issue
    • Reichert, J., Grasnick, D., Afonin, S., Buerck, J., Wadhwani, P., and Ulrich, A. S. (2007) A critical evaluation of the conformational requirements of fusogenic peptides in membranes Eur. Biophys. J. 36, 405-413 (Pubitemid 46626198)
    • (2007) European Biophysics Journal , vol.36 , Issue.4-5 , pp. 405-413
    • Reichert, J.1    Grasnick, D.2    Afonin, S.3    Buerck, J.4    Wadhwani, P.5    Ulrich, A.S.6
  • 43
    • 75449102744 scopus 로고    scopus 로고
    • De novo design of antimicrobial polymers, foldamers, and small molecules: From discovery to practical applications
    • Tew, G. N., Scott, R. W., Klein, M. L., and Degrado, W. F. (2010) De novo design of antimicrobial polymers, foldamers, and small molecules: from discovery to practical applications Acc. Chem. Res. 43, 30-39
    • (2010) Acc. Chem. Res. , vol.43 , pp. 30-39
    • Tew, G.N.1    Scott, R.W.2    Klein, M.L.3    Degrado, W.F.4
  • 44
    • 77958085274 scopus 로고    scopus 로고
    • Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model
    • Wimley, W. C. (2010) Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model ACS Chem. Biol. 5, 905-917
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 46
    • 67849131062 scopus 로고    scopus 로고
    • Antimicrobial peptides and viral fusion peptides: How different they are?
    • Joanne, P., Nicolas, P., and El Amri, C. (2009) Antimicrobial peptides and viral fusion peptides: how different they are? Protein Pept. Lett. 16, 743-750
    • (2009) Protein Pept. Lett. , vol.16 , pp. 743-750
    • Joanne, P.1    Nicolas, P.2    El Amri, C.3
  • 47
    • 79955669580 scopus 로고    scopus 로고
    • Antimicrobial Peptides: Successes, Challenges and Unanswered Questions
    • Wimley, W. and Hristova, K. (2011) Antimicrobial Peptides: Successes, Challenges and Unanswered Questions J. Membr. Biol. 239, 27-34-34
    • (2011) J. Membr. Biol. , vol.239 , pp. 27-34
    • Wimley, W.1    Hristova, K.2
  • 48
    • 67650566598 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: The importance of interfacial activity
    • Rathinakumar, R., Walkenhorst, W. F., and Wimley, W. C. (2009) Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: the importance of interfacial activity J. Am. Chem. Soc. 131, 7609-7617
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7609-7617
    • Rathinakumar, R.1    Walkenhorst, W.F.2    Wimley, W.C.3
  • 49
    • 48249157851 scopus 로고    scopus 로고
    • Biomolecular engineering by combinatorial design and high-throughput screening: Small, soluble peptides that permeabilize membranes
    • Rathinakumar, R. and Wimley, W. C. (2008) Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes J. Am. Chem. Soc. 130, 9849-9858
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9849-9858
    • Rathinakumar, R.1    Wimley, W.C.2
  • 50
    • 33646879586 scopus 로고    scopus 로고
    • PH-dependent lytic peptides discovered by phage display
    • DOI 10.1021/bi052488s
    • Hirosue, S. and Weber, T. (2006) pH-Dependent Lytic Peptides Discovered by Phage Display Biochemistry 45, 6476-6487 (Pubitemid 43787813)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6476-6487
    • Hirosue, S.1    Weber, T.2
  • 52
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • DOI 10.1038/90434
    • Han, X., Bushweller, J. H., Cafiso, D. S., and Tamm, L. K. (2001) Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin Nat. Struct. Biol. 8, 715-720 (Pubitemid 32757933)
    • (2001) Nature Structural Biology , vol.8 , Issue.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 53
    • 4444320707 scopus 로고    scopus 로고
    • Oligomeric β-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers
    • DOI 10.1529/biophysj.103.028530
    • Yang, J., Prorok, M., Castellino, F. J., and Weliky, D. P. (2004) Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers Biophys. J. 87, 1951-1963 (Pubitemid 39167049)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1951-1963
    • Yang, J.1    Prorok, M.2    Castellino, F.J.3    Weliky, D.P.4
  • 55
    • 34247209161 scopus 로고    scopus 로고
    • A critical evaluation of the conformational requirements of fusogenic peptides in membranes
    • DOI 10.1007/s00249-006-0106-2, Klaus Arnold Special Issue
    • Reichert, J., Grasnick, D., Afonin, S., Buerck, J., Wadhwani, P., and Ulrich, A. S. (2007) A critical evaluation of the conformational requirements of fusogenic peptides in membranes Eur. Biophys. J. 36, 405-413 (Pubitemid 46626198)
    • (2007) European Biophysics Journal , vol.36 , Issue.4-5 , pp. 405-413
    • Reichert, J.1    Grasnick, D.2    Afonin, S.3    Buerck, J.4    Wadhwani, P.5    Ulrich, A.S.6
  • 56
    • 1942438703 scopus 로고    scopus 로고
    • GALA: A designed synthetic pH-responsive amphipathic peptide with applications in drug and gene delivery
    • DOI 10.1016/j.addr.2003.10.041, PII S0169409X03002801
    • Li, W., Nicol, F., and Szoka, F. C. (2004) GALA: a designed synthetic pH-responsive amphipathic peptide with applications in drug and gene delivery Adv. Drug Delivery Rev. 56, 967-985 (Pubitemid 38520204)
    • (2004) Advanced Drug Delivery Reviews , vol.56 , Issue.7 , pp. 967-985
    • Li, W.1    Nicol, F.2    Szoka Jr., F.C.3
  • 57
    • 42949119657 scopus 로고    scopus 로고
    • Application of an HIV gp41-derived peptide for enhanced intracellular trafficking of synthetic gene and siRNA delivery vehicles
    • DOI 10.1021/bc700448h
    • Kwon, E. J., Bergen, J. M., and Pun, S. H. (2008) Application of an HIV gp41-Derived Peptide for Enhanced Intracellular Trafficking of Synthetic Gene and siRNA Delivery Vehicles Bioconjugate Chem. 19, 920-927 (Pubitemid 351614546)
    • (2008) Bioconjugate Chemistry , vol.19 , Issue.4 , pp. 920-927
    • Kwon, E.J.1    Bergen, J.M.2    Pun, S.H.3
  • 58
    • 0032487377 scopus 로고    scopus 로고
    • Application of membrane-active peptides for drug and gene delivery across cellular membranes
    • DOI 10.1016/S0169-409X(98)00005-2, PII S0169409X98000052
    • Plank, C., Zauner, W., and Wagner, E. (1998) Application of membrane-active peptides for drug and gene delivery across cellular membranes Adv. Drug Delivery Rev. 34, 21-35 (Pubitemid 28464476)
    • (1998) Advanced Drug Delivery Reviews , vol.34 , Issue.1 , pp. 21-35
    • Plank, C.1    Zauner, W.2    Wagner, E.3
  • 59
    • 33646152349 scopus 로고    scopus 로고
    • Melittin analogs with high lytic activity at endosomal pH enhance transfection with purified targeted PEI polyplexes
    • Boeckle, S., Fahrmeir, J., Roedl, W., Ogris, M., and Wagner, E. (2006) Melittin analogs with high lytic activity at endosomal pH enhance transfection with purified targeted PEI polyplexes J. Controlled Release 112, 240-248
    • (2006) J. Controlled Release , vol.112 , pp. 240-248
    • Boeckle, S.1    Fahrmeir, J.2    Roedl, W.3    Ogris, M.4    Wagner, E.5
  • 60
    • 34248680739 scopus 로고    scopus 로고
    • Exogenous siRNA delivery using peptide transduction domains/cell penetrating peptides
    • DOI 10.1016/j.addr.2007.03.004, PII S0169409X0700021X, Opportunities and Challenges for Therapeutic Gene Silencing using RNAi and microRNA Technologies
    • Meade, B. R. and Dowdy, S. F. (2007) Exogenous siRNA delivery using peptide transduction domains/cell penetrating peptides Adv. Drug Delivery Rev. 59, 134-140 (Pubitemid 46770904)
    • (2007) Advanced Drug Delivery Reviews , vol.59 , Issue.2-3 , pp. 134-140
    • Meade, B.R.1    Dowdy, S.F.2
  • 61
    • 39149093340 scopus 로고    scopus 로고
    • Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides
    • Meade, B. R. and Dowdy, S. F. (2008) Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides Adv. Drug Delivery Rev. 60, 530-536
    • (2008) Adv. Drug Delivery Rev. , vol.60 , pp. 530-536
    • Meade, B.R.1    Dowdy, S.F.2
  • 62
    • 0035523593 scopus 로고    scopus 로고
    • A powerful cooperative interaction between a fusogenic peptide and lipofectamine for the enhancement of receptor-targeted, non-viral gene delivery via integrin receptors
    • DOI 10.1002/jgm.224
    • Zhang, X., Collins, L., and Fabre, J. W. (2001) A powerful cooperative interaction between a fusogenic peptide and lipofectamine for the enhancement of receptor-targeted, non-viral gene delivery via integrin receptors J. Gene Med. 3, 560-568 (Pubitemid 33685086)
    • (2001) Journal of Gene Medicine , vol.3 , Issue.6 , pp. 560-568
    • Zhang, X.1    Collins, L.2    Fabre, J.W.3
  • 63
    • 29744464073 scopus 로고    scopus 로고
    • Exploration of peptide motifs for potent non-viral gene delivery highly selective for dividing cells
    • DOI 10.1002/jgm.809
    • Parker, A. L., Collins, L., Zhang, X., and Fabre, J. W. (2005) Exploration of peptide motifs for potent non-viral gene delivery highly selective for dividing cells J. Gene Med. 7, 1545-1554 (Pubitemid 43025515)
    • (2005) Journal of Gene Medicine , vol.7 , Issue.12 , pp. 1545-1554
    • Parker, A.L.1    Collins, L.2    Zhang, X.3    Fabre, J.W.4
  • 64
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • Wimley, W. C. and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 3, 842-848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 65
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D., and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion Biochemistry 20, 4093-4099
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 66
    • 79958814246 scopus 로고    scopus 로고
    • Rantosomes and ravosomes
    • Szoka, F. C. (1998) Rantosomes and ravosomes J. Liposome Res. 8, vii-ix
    • (1998) J. Liposome Res. , vol.8
    • Szoka, F.C.1
  • 67
    • 0018719041 scopus 로고
    • Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes
    • Olson, F., Hunt, C. A., Szoka, F. C., Vail, W. J., and Papahadjopoulos, D. (1979) Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes Biochim. Biophys. Acta 557, 9-23 (Pubitemid 10245657)
    • (1979) Biochimica et Biophysica Acta , vol.557 , Issue.1 , pp. 9-23
    • Olson, F.1    Hunt, C.A.2    Szoka, F.C.3
  • 68
    • 0021340434 scopus 로고
    • PH-induced destabilization of phosphatidylethanolamine-containing liposomes: Role of bilayer contact
    • Ellens, H., Bentz, J., and Szoka, F. C. (1984) pH-Induced destabilization of phosphatidylethanolamine-containing liposomes: role of bilayer contact Biochemistry 23, 1532-1538 (Pubitemid 14137550)
    • (1984) Biochemistry , vol.23 , Issue.7 , pp. 1532-1538
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 69
    • 0029752766 scopus 로고    scopus 로고
    • Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope
    • Akashi, K.-I., Miyata, H., Itoh, H., and Kinosita, K., Jr. (1996) Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope Biophys. J. 71, 3242-3250 (Pubitemid 26422366)
    • (1996) Biophysical Journal , vol.71 , Issue.6 , pp. 3242-3250
    • Akashi, K.-I.1    Miyata, H.2    Itoh, H.3    Kinosita Jr., K.4
  • 70
    • 8844279069 scopus 로고    scopus 로고
    • A trimeric HIV-1 fusion peptide construct which does not self-associate in aqueous solution and which has 15-fold higher membrane fusion rate
    • DOI 10.1021/ja045612o
    • Yang, R., Prorok, M., Castellino, F. J., and Weliky, D. P. (2004) A Trimeric HIV-1 Fusion Peptide Construct Which Does Not Self-Associate in Aqueous Solution and Which Has 15-Fold Higher Membrane Fusion Rate J. Am. Chem. Soc. 126, 14722-14723 (Pubitemid 39532144)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.45 , pp. 14722-14723
    • Yang, R.1    Prorok, M.2    Castellino, F.J.3    Weliky, D.P.4
  • 71
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • DOI 10.1021/ja072511s
    • Tang, M., Waring, A. J., and Hong, M. (2007) Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR J. Am. Chem. Soc. 129, 11438-11446 (Pubitemid 47555563)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.37 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 72
    • 45549085024 scopus 로고    scopus 로고
    • Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy
    • Tang, M., Waring, A. J., Lehrer, R. I., and Hong, M. (2008) Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy Angew. Chem., Int. Ed. 47, 3202-3205
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 3202-3205
    • Tang, M.1    Waring, A.J.2    Lehrer, R.I.3    Hong, M.4
  • 73
    • 13344250452 scopus 로고    scopus 로고
    • Noncovalent binding between guanidinium and anionic groups: Focus on biological- and synthetic-based arginine/guanidinium interactions with phosph[on]ate and sulf[on]ate residues
    • DOI 10.1021/cr040603j
    • Schug, K. A. and Lindner, W. (2005) Noncovalent Binding between Guanidinium and Anionic Groups: Focus on Biological- and Synthetic-Based Arginine/Guanidinium Interactions with Phosph[on]ate and Sulf[on]ate Residues Chem. Rev. (Washington, D. C.) 105, 67-113 (Pubitemid 40195930)
    • (2005) Chemical Reviews , vol.105 , Issue.1 , pp. 67-113
    • Schug, K.A.1    Lindner, W.2
  • 74
    • 44949104715 scopus 로고    scopus 로고
    • HIV TAT forms pores in membranes by inducing saddle-splay curvature: Potential role of bidentate hydrogen bonding
    • Mishra, A., Gordon, V. D., Yang, L., Coridan, R., and Wong, G. C. L. (2008) HIV TAT forms pores in membranes by inducing saddle-splay curvature: potential role of bidentate hydrogen bonding Angew. Chem., Int. Ed. 47, 2986-2989
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 2986-2989
    • Mishra, A.1    Gordon, V.D.2    Yang, L.3    Coridan, R.4    Wong, G.C.L.5
  • 75
    • 77951902057 scopus 로고    scopus 로고
    • Arginine-rich cell-penetrating peptides
    • Schmidt, N., Mishra, A., Lai, G. H., and Wong, G. C. L. (2010) Arginine-rich cell-penetrating peptides FEBS Lett. 584, 1806-1813
    • (2010) FEBS Lett. , vol.584 , pp. 1806-1813
    • Schmidt, N.1    Mishra, A.2    Lai, G.H.3    Wong, G.C.L.4
  • 76
    • 79955650131 scopus 로고    scopus 로고
    • A Look at Arginine in Membranes
    • Hristova, K. and Wimley, W. (2011) A Look at Arginine in Membranes J. Membr. Biol. 239, 49-56-56
    • (2011) J. Membr. Biol. , vol.239 , pp. 49-56
    • Hristova, K.1    Wimley, W.2
  • 77
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • Boggs, J. M. (1987) Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function Biochim. Biophys. Acta 906, 353-404 (Pubitemid 17140656)
    • (1987) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.906 , Issue.3 , pp. 353-404
    • Boggs, J.M.1
  • 78
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • DOI 10.1006/jmbi.1999.2829
    • Tsai, J., Taylor, R., Chothia, C., and Gerstein, M. (1999) The packing density in proteins: standard radii and volumes J. Mol. Biol. 290, 253-266 (Pubitemid 29308589)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.1 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 79
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.07.001, PII S0005273606002616
    • Bechinger, B. and Lohner, K. (2006) Detergent-like actions of linear amphipathic cationic antimicrobial peptides Biochim. Biophys. Acta, Biomembr. 1758, 1529-1539 (Pubitemid 44436087)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 80
    • 3242701305 scopus 로고    scopus 로고
    • Antimicrobial 14-helical β-peptides: Potent bilayer disrupting agents
    • DOI 10.1021/bi049414l
    • Epand, R. F., Raguse, T. L., Gellman, S. H., and Epand, R. M. (2004) Antimicrobial 14-helical beta-peptides: potent bilayer disrupting agents Biochemistry 43, 9527-9535 (Pubitemid 38955486)
    • (2004) Biochemistry , vol.43 , Issue.29 , pp. 9527-9535
    • Epand, R.F.1    Raguse, T.L.2    Gellman, S.H.3    Epand, R.M.4
  • 81
    • 0141888597 scopus 로고    scopus 로고
    • Helical peptoid mimics of magainin-2 amide
    • DOI 10.1021/ja037320d
    • Patch, J. A. and Barron, A. E. (2003) Helical Peptoid Mimics of Magainin-2 Amide J. Am. Chem. Soc. 125, 12092-12093 (Pubitemid 37238834)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.40 , pp. 12092-12093
    • Patch, J.A.1    Barron, A.E.2
  • 82
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren, Z. and Shai, Y. (1998) Mode of action of linear amphipathic alpha-helical antimicrobial peptides Biopolymers 47, 451-463
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 83
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., Zasloff, M., and Opella, S. J. (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy Protein Sci. 2, 2077-2084 (Pubitemid 23354711)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 84
    • 67849104242 scopus 로고    scopus 로고
    • The "tilted peptide theory" links membrane insertion properties and fusogenicity of viral fusion peptides
    • Charloteaux, B., Lorin, A., Brasseur, R., and Lins, L. (2009) The "tilted peptide theory" links membrane insertion properties and fusogenicity of viral fusion peptides Protein Pept. Lett. 16, 718-725
    • (2009) Protein Pept. Lett. , vol.16 , pp. 718-725
    • Charloteaux, B.1    Lorin, A.2    Brasseur, R.3    Lins, L.4
  • 85
    • 77957709364 scopus 로고    scopus 로고
    • Studies on viral fusion peptides: The distribution of lipophilic and electrostatic potential over the peptide determines the angle of insertion into a membrane
    • Taylor, A. and Sansom, M. S. (2010) Studies on viral fusion peptides: the distribution of lipophilic and electrostatic potential over the peptide determines the angle of insertion into a membrane Eur. Biophys. J. 39, 1537-1545
    • (2010) Eur. Biophys. J. , vol.39 , pp. 1537-1545
    • Taylor, A.1    Sansom, M.S.2
  • 86
    • 33646138957 scopus 로고    scopus 로고
    • Evaluating tilt angles of membrane-associated helices: Comparison of computational and NMR techniques
    • Ulmschneider, M. B., Sansom, M. S., and Di Nola, A. (2006) Evaluating tilt angles of membrane-associated helices: comparison of computational and NMR techniques Biophys. J. 90, 1650-1660
    • (2006) Biophys. J. , vol.90 , pp. 1650-1660
    • Ulmschneider, M.B.1    Sansom, M.S.2    Di Nola, A.3
  • 87
    • 0026328559 scopus 로고
    • Fluorescence assay for phospholipid membrane asymmetry
    • McIntyre, J. C. and Sleight, R. G. (1991) Fluorescence assay for phospholipid membrane asymmetry Biochemistry 30, 11819-11827
    • (1991) Biochemistry , vol.30 , pp. 11819-11827
    • McIntyre, J.C.1    Sleight, R.G.2
  • 88
    • 0018653707 scopus 로고
    • 2+-induced fusion of phospholipid vesicles monitored by mixing of aqueous contents
    • DOI 10.1038/281690a0
    • Wilschut, J. and Papahadjopoulos, D. (1979) Ca2+-induced fusion of phospholipid vesicles monitored by mixing of aqueous contents Nature 281, 690-692 (Pubitemid 10249051)
    • (1979) Nature , vol.281 , Issue.5733 , pp. 690-692
    • Wilschut, J.1    Papahadjopoulos, D.2
  • 89
    • 0026576543 scopus 로고
    • Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: Importance of interbilayer separation
    • Burgess, S. W., McIntosh, T. J., and Lentz, B. R. (1992) Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: importance of interbilayer separation Biochemistry 31, 2653-2661
    • (1992) Biochemistry , vol.31 , pp. 2653-2661
    • Burgess, S.W.1    McIntosh, T.J.2    Lentz, B.R.3
  • 90
    • 59849106607 scopus 로고    scopus 로고
    • HIV Fusion Peptide and Its Cross-Linked Oligomers: Efficient Syntheses, Significance of the Trimer in Fusion Activity, Correlation of beta Strand Conformation with Membrane Cholesterol, and Proximity to Lipid Headgroups
    • Qiang, W. and Weliky, D. P. (2009) HIV Fusion Peptide and Its Cross-Linked Oligomers: Efficient Syntheses, Significance of the Trimer in Fusion Activity, Correlation of beta Strand Conformation with Membrane Cholesterol, and Proximity to Lipid Headgroups Biochemistry 48, 289-301
    • (2009) Biochemistry , vol.48 , pp. 289-301
    • Qiang, W.1    Weliky, D.P.2


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