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Volumn 436, Issue 1-2, 2012, Pages 593-601

Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: Interaction with model membranes

Author keywords

Circular dichroism; Compression isotherms; Hepatitis GB virus C; HIV 1 FP; Lipid monolayer; Synthetic peptide

Indexed keywords

AMINO ACID DERIVATIVE; ANTIVIRUS AGENT; GLYCOPROTEIN E1; HEPATITIS G VIRUS E1 PROTEIN P10; HEPATITIS G VIRUS E1 PROTEIN P18; HEPATITIS G VIRUS E1 PROTEIN P7; HEPATITIS G VIRUS E1 PROTEIN P8; HUMAN IMMUNODEFICIENCY VIRUS 1 FUSION PROTEIN; LIPOSOME; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN;

EID: 84865285993     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2012.07.051     Document Type: Article
Times cited : (7)

References (31)
  • 1
    • 0033215173 scopus 로고    scopus 로고
    • Forming stable helical peptides using natural and artificial amino acids
    • M.J.I. Andrews, and A.B. Tabor Forming stable helical peptides using natural and artificial amino acids Tetrahedron 55 1999 11711 11743
    • (1999) Tetrahedron , vol.55 , pp. 11711-11743
    • Andrews, M.J.I.1    Tabor, A.B.2
  • 3
    • 0019816841 scopus 로고
    • Penetration of phospholipid monolayers by cardiotoxins
    • P. Bougis, H. Rochat, G. Pieroni, and R. Verger Penetration of phospholipid monolayers by cardiotoxins Biochemistry 20 1981 4915 4920
    • (1981) Biochemistry , vol.20 , pp. 4915-4920
    • Bougis, P.1    Rochat, H.2    Pieroni, G.3    Verger, R.4
  • 4
    • 0000050840 scopus 로고
    • The configuration of random polypeptide chains II. Theory
    • D.A. Brant, and P.J. Flory The configuration of random polypeptide chains II. Theory J. Am. Chem. Soc. 87 1965 2791 2800
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2791-2800
    • Brant, D.A.1    Flory, P.J.2
  • 5
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Y.H. Chen, J.T. Yang, and K.H. Chau Determination of the helix and beta form of proteins in aqueous solution by circular dichroism Biochemistry 13 1974 3350 3360
    • (1974) Biochemistry , vol.13 , pp. 3350-3360
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 6
    • 2942715203 scopus 로고    scopus 로고
    • Primary amphipathic cell-penetrating peptides: Structural requirements and interactions with model membranes
    • S. Deshayes, T. Plenat, G. Aldrian-Herrada, G. Divita, C. Le Grimellec, and F. Heitz Primary amphipathic cell-penetrating peptides: structural requirements and interactions with model membranes Biochemistry 43 2004 7698 7700
    • (2004) Biochemistry , vol.43 , pp. 7698-7700
    • Deshayes, S.1    Plenat, T.2    Aldrian-Herrada, G.3    Divita, G.4    Le Grimellec, C.5    Heitz, F.6
  • 7
    • 35848952075 scopus 로고    scopus 로고
    • Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus, conformational requirements for leakage
    • M. Fernández-Vidal, N. Rojo, E. Herrera, M.J. Gómara, and I. Haro Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus, conformational requirements for leakage Biophys. Chem. 132 2008 55 63
    • (2008) Biophys. Chem. , vol.132 , pp. 55-63
    • Fernández-Vidal, M.1    Rojo, N.2    Herrera, E.3    Gómara, M.J.4    Haro, I.5
  • 9
    • 0025745883 scopus 로고
    • A study of the miscibility of bile components in mixed monolayers at the air-liquid interface I. Cholesterol, lecithin, and lithocholic acid
    • M.J. Galvez, and M.A. Cabrerizo A study of the miscibility of bile components in mixed monolayers at the air-liquid interface I. Cholesterol, lecithin, and lithocholic acid Colloid. Polym. Sci. 269 1 1991 77 84
    • (1991) Colloid. Polym. Sci. , vol.269 , Issue.1 , pp. 77-84
    • Galvez, M.J.1    Cabrerizo, M.A.2
  • 10
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • N.J. Greenfield Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 1 2006 2876 2880
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2880
    • Greenfield, N.J.1
  • 12
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • A. Lobley, L. Whitmore, and B.A. Wallace DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra Bioinformatics (Oxford England) 18 2002 211 220
    • (2002) Bioinformatics (Oxford England) , vol.18 , pp. 211-220
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 13
    • 0025902367 scopus 로고
    • Epifluorescence microscopic observation of monolayers of dipalmitoylphosphatidylcholine: Dependence of domain size on compression rates
    • K. Nag, C. Boland, N. Rich, and K.M. Keough Epifluorescence microscopic observation of monolayers of dipalmitoylphosphatidylcholine: dependence of domain size on compression rates Biochim. Biophys. Acta 1068 1991 157 160
    • (1991) Biochim. Biophys. Acta , vol.1068 , pp. 157-160
    • Nag, K.1    Boland, C.2    Rich, N.3    Keough, K.M.4
  • 14
    • 0029993251 scopus 로고    scopus 로고
    • Fluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayers
    • K. Nag, J. Perez-Gil, A. Cruz, and K.M. Keough Fluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayers Biophys. J. 71 1996 246 250
    • (1996) Biophys. J. , vol.71 , pp. 246-250
    • Nag, K.1    Perez-Gil, J.2    Cruz, A.3    Keough, K.M.4
  • 15
    • 0029185909 scopus 로고
    • Design of alpha-helical peptides: Their role in protein folding and molecular biology
    • R. Parthasarathy, S. Chaturvedi, and K. Go Design of alpha-helical peptides: their role in protein folding and molecular biology Prog. Biophys. Mol. Biol. 64 1995 1 54
    • (1995) Prog. Biophys. Mol. Biol. , vol.64 , pp. 1-54
    • Parthasarathy, R.1    Chaturvedi, S.2    Go, K.3
  • 17
    • 0026630978 scopus 로고
    • Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers
    • J. Perez-Gil, K. Nag, S. Taneva, and K.M. Keough Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers Biophys. J. 63 1992 197 200
    • (1992) Biophys. J. , vol.63 , pp. 197-200
    • Perez-Gil, J.1    Nag, K.2    Taneva, S.3    Keough, K.M.4
  • 18
    • 0032104778 scopus 로고    scopus 로고
    • Conformational behavior of the HAV-VP3 (110-121) peptidic sequence and synthetic analogs in membrane environments studied by CD and computational methods
    • J.A. Pérez, J. Cantó, F. Reig, J.J. Pérez, and I. Haro Conformational behavior of the HAV-VP3 (110-121) peptidic sequence and synthetic analogs in membrane environments studied by CD and computational methods Biopolymers 45 1998 479 480
    • (1998) Biopolymers , vol.45 , pp. 479-480
    • Pérez, J.A.1    Cantó, J.2    Reig, F.3    Pérez, J.J.4    Haro, I.5
  • 19
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • M. Rafalski, J.D. Lear, and W.F. DeGrado Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41 Biochemistry 29 1990 7917 7920
    • (1990) Biochemistry , vol.29 , pp. 7917-7920
    • Rafalski, M.1    Lear, J.D.2    Degrado, W.F.3
  • 20
    • 0031558811 scopus 로고    scopus 로고
    • Role of beta-turn residues in beta-hairpin formation and stability in designed peptides
    • M. Ramirez-Alvarado, F.J. Blanco, H. Niemann, and L. Serrano Role of beta-turn residues in beta-hairpin formation and stability in designed peptides J. Mol. Biol. 273 1997 898 900
    • (1997) J. Mol. Biol. , vol.273 , pp. 898-900
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Niemann, H.3    Serrano, L.4
  • 21
    • 67349158245 scopus 로고    scopus 로고
    • Fluorescence study of the dynamic interaction between E1 (145-162) sequence of hepatitis GB virus C and liposomes
    • M. Sánchez-Martín, J. Amigo, M. Pujol, I. Haro, M. Alsina, and M. Busquets Fluorescence study of the dynamic interaction between E1 (145-162) sequence of hepatitis GB virus C and liposomes Anal. Bioanal. Chem. 394 2009 1003 1010
    • (2009) Anal. Bioanal. Chem. , vol.394 , pp. 1003-1010
    • Sánchez-Martín, M.1    Amigo, J.2    Pujol, M.3    Haro, I.4    Alsina, M.5    Busquets, M.6
  • 22
    • 75649122919 scopus 로고    scopus 로고
    • A Langmuir monolayer study of the interaction of E1 (145-162) hepatitis G virus peptide with phospholipid membranes
    • M.J. Sánchez-Martín, I. Haro, M.A. Alsina, M.A. Busquets, and M. Pujol A Langmuir monolayer study of the interaction of E1 (145-162) hepatitis G virus peptide with phospholipid membranes J. Phys. Chem. B 114 2010 448 450
    • (2010) J. Phys. Chem. B , vol.114 , pp. 448-450
    • Sánchez-Martín, M.J.1    Haro, I.2    Alsina, M.A.3    Busquets, M.A.4    Pujol, M.5
  • 24
    • 80054757875 scopus 로고    scopus 로고
    • Biophysical Investigations of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide
    • M.J. Sánchez-Martín, P. Urbán, M. Pujol, I. Haro, M.A. Alsina, and M.A. Busquets Biophysical Investigations of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide ChemPhysChem 12 2011 2816 2820
    • (2011) ChemPhysChem , vol.12 , pp. 2816-2820
    • Sánchez-Martín, M.J.1    Urbán, P.2    Pujol, M.3    Haro, I.4    Alsina, M.A.5    Busquets, M.A.6
  • 26
    • 0034769199 scopus 로고    scopus 로고
    • GB virus-C infection in patients infected with the human immunodeficiency virus
    • H.L. Tillmann, and M.P. Manns GB virus-C infection in patients infected with the human immunodeficiency virus Antiviral Res. 52 2001 83 90
    • (2001) Antiviral Res. , vol.52 , pp. 83-90
    • Tillmann, H.L.1    Manns, M.P.2
  • 27
    • 34248329071 scopus 로고    scopus 로고
    • Langmuir-Blodgett films formed by continuously varying surface pressure, characterization by IR spectroscopy and epifluorescence microscopy
    • L. Wang, A. Cruz, C.R. Flach, J. Perez-Gil, and R. Mendelsohn Langmuir-Blodgett films formed by continuously varying surface pressure, characterization by IR spectroscopy and epifluorescence microscopy Langmuir 23 2007 4950 4960
    • (2007) Langmuir , vol.23 , pp. 4950-4960
    • Wang, L.1    Cruz, A.2    Flach, C.R.3    Perez-Gil, J.4    Mendelsohn, R.5
  • 28
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 2004 668 670
    • (2004) Nucleic Acids Res. , vol.32 , pp. 668-670
    • Whitmore, L.1    Wallace, B.A.2
  • 29
  • 30
    • 2942659318 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by GB virus C infection through increases in RANTES, MIP-1alpha, MIP-1beta, and SDF-1
    • J. Xiang, S.L. George, S. Wunschmann, Q. Chang, D. Klinzman, and J.T. Stapleton Inhibition of HIV-1 replication by GB virus C infection through increases in RANTES, MIP-1alpha, MIP-1beta, and SDF-1 Lancet 363 2004 2040 2050
    • (2004) Lancet , vol.363 , pp. 2040-2050
    • Xiang, J.1    George, S.L.2    Wunschmann, S.3    Chang, Q.4    Klinzman, D.5    Stapleton, J.T.6


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