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Volumn 23, Issue 6, 2012, Pages 1252-1258

Design of a modular tetrameric scaffold for the synthesis of membrane-localized D-peptide inhibitors of HIV-1 entry

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; PEPTIDES; SCAFFOLDS;

EID: 84862699298     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc300076f     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection
    • Freed, E. O., and Martin, M. A. (1995) The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection. J. Biol. Chem. 270, 23883-6.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 2
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70, 777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 3
    • 0031962175 scopus 로고    scopus 로고
    • Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors
    • Jones, P. L., Korte, T., and Blumenthal, R. (1998) Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors. J. Biol. Chem. 273, 404-9.
    • (1998) J. Biol. Chem. , vol.273 , pp. 404-409
    • Jones, P.L.1    Korte, T.2    Blumenthal, R.3
  • 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 89, 263-73.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 6
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., Kay, M. S., and Kim, P. S. (2001) Protein design of an HIV-1 entry inhibitor. Science 291, 884-8.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 8
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C., Oas, T., McDanal, C., Bolognesi, D., and Matthews, T. (1992) A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. U. S. A. 89, 10537-41.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 9
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., Shugars, D. C., Greenwell, T. K., McDanal, C. B., and Matthews, T. J. (1994) Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U. S. A. 91, 9770-4.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 10
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., Shugars, D. C., and Matthews, T. J. (1998) Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72, 986-93.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 12
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan, D. C., Chutkowski, C. T., and Kim, P. S. (1998) Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. U. S. A. 95, 15613-7.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 13
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D. M., Malashkevich, V. N., Hong, L. H., Carr, P. A., and Kim, P. S. (1999) Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99, 103-15.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 15
    • 0034890660 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor
    • Derdeyn, C. A., Decker, J. M., Sfakianos, J. N., Zhang, Z., O'Brien, W. A., Ratner, L., Shaw, G. M., and Hunter, E. (2001) Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor. J. Virol. 75, 8605-14.
    • (2001) J. Virol. , vol.75 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Zhang, Z.4    O'Brien, W.A.5    Ratner, L.6    Shaw, G.M.7    Hunter, E.8
  • 17
    • 80055013474 scopus 로고    scopus 로고
    • Resistance of human immunodeficiency virus type 1 to a third-generation fusion inhibitor requires multiple mutations in gp41 and is accompanied by a dramatic loss of gp41 function
    • Eggink, D., Bontjer, I., Langedijk, J. P., Berkhout, B., and Sanders, R. W. (2011) Resistance of human immunodeficiency virus type 1 to a third-generation fusion inhibitor requires multiple mutations in gp41 and is accompanied by a dramatic loss of gp41 function. J. Virol. 85, 10785-97.
    • (2011) J. Virol. , vol.85 , pp. 10785-10797
    • Eggink, D.1    Bontjer, I.2    Langedijk, J.P.3    Berkhout, B.4    Sanders, R.W.5
  • 18
    • 33947417638 scopus 로고    scopus 로고
    • Clinical resistance to enfuvirtide does not affect susceptibility of human immunodeficiency virus type 1 to other classes of entry inhibitors
    • Ray, N., Harrison, J. E., Blackburn, L. A., Martin, J. N., Deeks, S. G., and Doms, R. W. (2007) Clinical resistance to enfuvirtide does not affect susceptibility of human immunodeficiency virus type 1 to other classes of entry inhibitors. J. Virol. 81, 3240-50.
    • (2007) J. Virol. , vol.81 , pp. 3240-3250
    • Ray, N.1    Harrison, J.E.2    Blackburn, L.A.3    Martin, J.N.4    Deeks, S.G.5    Doms, R.W.6
  • 19
    • 16244380203 scopus 로고    scopus 로고
    • Enfuvirtide resistance mutations: Impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization
    • Reeves, J. D., Lee, F. H., Miamidian, J. L., Jabara, C. B., Juntilla, M. M., and Doms, R. W. (2005) Enfuvirtide resistance mutations: impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization. J. Virol. 79, 4991-9.
    • (2005) J. Virol. , vol.79 , pp. 4991-4999
    • Reeves, J.D.1    Lee, F.H.2    Miamidian, J.L.3    Jabara, C.B.4    Juntilla, M.M.5    Doms, R.W.6
  • 23
    • 0026686436 scopus 로고
    • Total chemical synthesis of a D-enzyme: The enantiomers of HIV-1 protease show reciprocal chiral substrate specificity
    • Milton, R. C., Milton, S. C., and Kent, S. B. (1992) Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity. Science 256, 1445-8.
    • (1992) Science , vol.256 , pp. 1445-1448
    • Milton, R.C.1    Milton, S.C.2    Kent, S.B.3
  • 24
    • 73549091727 scopus 로고    scopus 로고
    • Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding
    • Kahle, K. M., Steger, H. K., and Root, M. J. (2009) Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding. PLoS Pathog. 5, e1000674.
    • (2009) PLoS Pathog. , vol.5
    • Kahle, K.M.1    Steger, H.K.2    Root, M.J.3
  • 25
    • 15244356599 scopus 로고    scopus 로고
    • Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus
    • Platt, E. J., Durnin, J. P., and Kabat, D. (2005) Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus. J. Virol. 79, 4347-56.
    • (2005) J. Virol. , vol.79 , pp. 4347-4356
    • Platt, E.J.1    Durnin, J.P.2    Kabat, D.3
  • 26
    • 33748741296 scopus 로고    scopus 로고
    • Kinetic dependence to HIV-1 entry inhibition
    • Steger, H. K., and Root, M. J. (2006) Kinetic dependence to HIV-1 entry inhibition. J. Biol. Chem. 281, 25813-21.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25813-25821
    • Steger, H.K.1    Root, M.J.2
  • 31
    • 77958450463 scopus 로고    scopus 로고
    • Semisynthesis of a protein with cholesterol at the C-terminal, targeted to the cell membrane of live cells
    • Teruya, K., Nishizawa, K., and Doh-ura, K. (2010) Semisynthesis of a protein with cholesterol at the C-terminal, targeted to the cell membrane of live cells. Protein J. 29, 493-500.
    • (2010) Protein J. , vol.29 , pp. 493-500
    • Teruya, K.1    Nishizawa, K.2    Doh-ura, K.3
  • 32
    • 50349092134 scopus 로고    scopus 로고
    • Molecular dynamics studies of polyethylene oxide and polyethylene glycol: Hydrodynamic radius and shape anisotropy
    • Lee, H., Venable, R. M., Mackerell, A. D., Jr., and Pastor, R. W. (2008) Molecular dynamics studies of polyethylene oxide and polyethylene glycol: hydrodynamic radius and shape anisotropy. Biophys. J. 95, 1590-9.
    • (2008) Biophys. J. , vol.95 , pp. 1590-1599
    • Lee, H.1    Venable, R.M.2    Mackerell Jr., A.D.3    Pastor, R.W.4
  • 33
    • 78649829342 scopus 로고    scopus 로고
    • Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain
    • Wexler-Cohen, Y., Ashkenazi, A., Viard, M., Blumenthal, R., and Shai, Y. (2010) Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain. FASEB J. 24, 4196-202.
    • (2010) FASEB J. , vol.24 , pp. 4196-4202
    • Wexler-Cohen, Y.1    Ashkenazi, A.2    Viard, M.3    Blumenthal, R.4    Shai, Y.5
  • 34
    • 35948978102 scopus 로고    scopus 로고
    • Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition
    • Wexler-Cohen, Y., and Shai, Y. (2007) Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition. FASEB J. 21, 3677-84.
    • (2007) FASEB J. , vol.21 , pp. 3677-3684
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 35
    • 70049117718 scopus 로고    scopus 로고
    • Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action
    • Wexler-Cohen, Y., and Shai, Y. (2009) Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action. PLoS Pathog. 5, e1000509.
    • (2009) PLoS Pathog. , vol.5
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 36
    • 0034642495 scopus 로고    scopus 로고
    • Bioorganic synthesis of lipid-modified proteins for the study of signal transduction
    • Bader, B., Kuhn, K., Owen, D. J., Waldmann, H., Wittinghofer, A., and Kuhlmann, J. (2000) Bioorganic synthesis of lipid-modified proteins for the study of signal transduction. Nature 403, 223-6.
    • (2000) Nature , vol.403 , pp. 223-226
    • Bader, B.1    Kuhn, K.2    Owen, D.J.3    Waldmann, H.4    Wittinghofer, A.5    Kuhlmann, J.6
  • 37
    • 0037936885 scopus 로고    scopus 로고
    • C-terminal octylation rescues an inactive T20 mutant: Implications for the mechanism of HIV/SIMIAN immunodeficiency virus-induced membrane fusion
    • Peisajovich, S. G., Gallo, S. A., Blumenthal, R., and Shai, Y. (2003) C-terminal octylation rescues an inactive T20 mutant: implications for the mechanism of HIV/SIMIAN immunodeficiency virus-induced membrane fusion. J. Biol. Chem. 278, 21012-7.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21012-21017
    • Peisajovich, S.G.1    Gallo, S.A.2    Blumenthal, R.3    Shai, Y.4
  • 38
    • 47049106121 scopus 로고    scopus 로고
    • The functional roles of lipid rafts in T cell activation, immune diseases and HIV infection and prevention
    • Luo, C., Wang, K., Liu de, Q., Li, Y., and Zhao, Q. S. (2008) The functional roles of lipid rafts in T cell activation, immune diseases and HIV infection and prevention. Cell Mol. Immunol. 5, 1-7.
    • (2008) Cell Mol. Immunol. , vol.5 , pp. 1-7
    • Luo, C.1    Wang, K.2    De Liu, Q.3    Li, Y.4    Zhao, Q.S.5
  • 39
    • 79952088584 scopus 로고    scopus 로고
    • The Role of Lipids in Retrovirus Replication
    • Waheed, A. A., and Freed, E. O. (2010) The Role of Lipids in Retrovirus Replication. Viruses 2, 1146-1180.
    • (2010) Viruses , vol.2 , pp. 1146-1180
    • Waheed, A.A.1    Freed, E.O.2
  • 40
    • 0037164705 scopus 로고    scopus 로고
    • Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups
    • Vincent, N., Genin, C., and Malvoisin, E. (2002) Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups. Biochim. Biophys. Acta 1567, 157-64.
    • (2002) Biochim. Biophys. Acta , vol.1567 , pp. 157-164
    • Vincent, N.1    Genin, C.2    Malvoisin, E.3
  • 42
    • 80051955323 scopus 로고    scopus 로고
    • Fatty acid and peptide profiles in plasma membrane and membrane rafts of PUFA supplemented RAW264.7 macrophages
    • Schumann, J., Leichtle, A., Thiery, J., and Fuhrmann, H. (2011) Fatty acid and peptide profiles in plasma membrane and membrane rafts of PUFA supplemented RAW264.7 macrophages. PLoS One 6, e24066.
    • (2011) PLoS One , vol.6
    • Schumann, J.1    Leichtle, A.2    Thiery, J.3    Fuhrmann, H.4
  • 43
    • 0016691920 scopus 로고
    • Fatty acid binding to plasma albumin
    • Spector, A. A. (1975) Fatty acid binding to plasma albumin. J. Lipid Res. 16, 165-79.
    • (1975) J. Lipid Res. , vol.16 , pp. 165-179
    • Spector, A.A.1
  • 44
    • 0032739854 scopus 로고    scopus 로고
    • Acyl and alkyl chain length of GPI-anchors is critical for raft association in vitro
    • Benting, J., Rietveld, A., Ansorge, I., and Simons, K. (1999) Acyl and alkyl chain length of GPI-anchors is critical for raft association in vitro. FEBS Lett. 462, 47-50.
    • (1999) FEBS Lett. , vol.462 , pp. 47-50
    • Benting, J.1    Rietveld, A.2    Ansorge, I.3    Simons, K.4
  • 45
    • 43549094436 scopus 로고    scopus 로고
    • The interaction between cholesterol and human serum albumin
    • Peng, L., Minbo, H., Fang, C., Xi, L., and Chaocan, Z. (2008) The interaction between cholesterol and human serum albumin. Protein Pept. Lett. 15, 360-4.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 360-364
    • Peng, L.1    Minbo, H.2    Fang, C.3    Xi, L.4    Chaocan, Z.5
  • 46
    • 75649126908 scopus 로고    scopus 로고
    • Study on the interaction of cationic lipids with bovine serum albumin
    • Charbonneau, D. M., and Tajmir-Riahi, H. A. (2010) Study on the interaction of cationic lipids with bovine serum albumin. J. Phys. Chem. B 114, 1148-55.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 1148-1155
    • Charbonneau, D.M.1    Tajmir-Riahi, H.A.2
  • 47
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics
    • Fishburn, C. S. (2008) The pharmacology of PEGylation: balancing PD with PK to generate novel therapeutics. J. Pharm. Sci. 97, 4167-83.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4167-4183
    • Fishburn, C.S.1


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