메뉴 건너뛰기




Volumn 26, Issue 6, 2008, Pages 1004-1013

Computational and experimental approaches assess the interactions between bovine β-lactoglobulin and synthetic compounds of pharmacological interest

Author keywords

Denaturant gradient gel electrophoresis; Fluorine nuclear magnetic resonance; Fluoroquinolones; Molecular docking; Monte Carlo; Statins; Steroids

Indexed keywords

ANNEALING PROTOCOLS; DENATURANT GRADIENT GEL ELECTROPHORESIS; FLUORINE NUCLEAR MAGNETIC RESONANCE; FLUOROQUINOLONES; MOLECULAR DOCKINGS; STEROIDS; SYNTHETIC COMPOUNDS;

EID: 37349056405     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2007.08.006     Document Type: Article
Times cited : (21)

References (55)
  • 1
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine β-lactoglobulin
    • Sawyer L., and Kontopidis G. The core lipocalin, bovine β-lactoglobulin. Biochim. Biophys. Acta 1482 (2000) 136-148
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 2
    • 0028102760 scopus 로고
    • The lipocalin protein family: a role in cell regulation
    • Flower D.R. The lipocalin protein family: a role in cell regulation. FEBS Lett. 354 (1994) 7-11
    • (1994) FEBS Lett. , vol.354 , pp. 7-11
    • Flower, D.R.1
  • 3
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: structure and function
    • Flower D.R. The lipocalin protein family: structure and function. Biochem. J. 318 (1996) 1-14
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 5
    • 0025155418 scopus 로고
    • Binding of ellipticine to β-lactoglobulin. A physico-chemical study of the specific interaction of an antitumor drug with a transport protein
    • Dodin G., Andrieux M., and al Kabbani H. Binding of ellipticine to β-lactoglobulin. A physico-chemical study of the specific interaction of an antitumor drug with a transport protein. Eur. J. Biochem. 193 (1990) 697-700
    • (1990) Eur. J. Biochem. , vol.193 , pp. 697-700
    • Dodin, G.1    Andrieux, M.2    al Kabbani, H.3
  • 6
    • 0025609431 scopus 로고
    • β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites
    • Dufour E., Marden M.C., and Haertle T. β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites. FEBS Lett. 277 (1990) 223-226
    • (1990) FEBS Lett. , vol.277 , pp. 223-226
    • Dufour, E.1    Marden, M.C.2    Haertle, T.3
  • 7
    • 0025784171 scopus 로고
    • Binding of retinoids and β-carotene to β-lactoglobulin: influence of protein modifications
    • Dufour E., and Haertle T. Binding of retinoids and β-carotene to β-lactoglobulin: influence of protein modifications. Biochim. Biophys. Acta 1079 (1991) 316-320
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 316-320
    • Dufour, E.1    Haertle, T.2
  • 9
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin
    • Creamer L.K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry 34 (1995) 7170-7176
    • (1995) Biochemistry , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 10
    • 0031035893 scopus 로고    scopus 로고
    • Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin
    • Narayan M., and Berliner L.J. Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 36 (1997) 1906-1911
    • (1997) Biochemistry , vol.36 , pp. 1906-1911
    • Narayan, M.1    Berliner, L.J.2
  • 11
    • 0031160714 scopus 로고    scopus 로고
    • Binding of vitamin D and cholesterol to β-lactoglobulin
    • Wang Q., Allen J.C., and Swaisgood H.E. Binding of vitamin D and cholesterol to β-lactoglobulin. J. Dairy Sci. 80 (1997) 1054-1059
    • (1997) J. Dairy Sci. , vol.80 , pp. 1054-1059
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 12
    • 0033049201 scopus 로고    scopus 로고
    • Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to β-lactoglobulin from fluorescence spectroscopy
    • D'Alfonso L., Collini M., and Baldini G. Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to β-lactoglobulin from fluorescence spectroscopy. Biochim. Biophys. Acta 1432 (1999) 194-202
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 194-202
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 13
    • 0345313659 scopus 로고    scopus 로고
    • β-Lactoglobulin binds palmitate within its central cavity
    • Wu S.Y., Perez M.D., Puyol P., and Sawyer L. β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 274 (1999) 170-174
    • (1999) J. Biol. Chem. , vol.274 , pp. 170-174
    • Wu, S.Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 16
    • 0000125782 scopus 로고
    • β-Lactoglobulins
    • McKenzie H.A. (Ed), Academic Press, New York
    • McKenzie H.A. β-Lactoglobulins. In: McKenzie H.A. (Ed). Milk Proteins (1971), Academic Press, New York 257-330
    • (1971) Milk Proteins , pp. 257-330
    • McKenzie, H.A.1
  • 18
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., and Eliopoulos E.E. Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 197 (1987) 695-706
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 22
    • 0030635208 scopus 로고    scopus 로고
    • Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2
    • Ragona L., Pusterla F., Zetta L., Monaco H.L., and Molinari H. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Fold. Des. 2 (1997) 281-290
    • (1997) Fold. Des. , vol.2 , pp. 281-290
    • Ragona, L.1    Pusterla, F.2    Zetta, L.3    Monaco, H.L.4    Molinari, H.5
  • 24
    • 0032110129 scopus 로고    scopus 로고
    • 15N chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form
    • 15N chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 12 (1998) 89-107
    • (1998) J. Biomol. NMR , vol.12 , pp. 89-107
    • Uhrinova, S.1    Uhrin, D.2    Denton, H.3    Smith, M.4    Sawyer, L.5    Barlow, P.N.6
  • 25
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer
    • Uhrinova S., Smith M.H., Jameson G.B., Urhin D., Sawyer L., and Barlow P.N. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 39 (2000) 3565-3574
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Urhin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 26
    • 0029398314 scopus 로고
    • Susceptibility of β-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin
    • Guo M.R., Fox P.F., and Kindstedt P.S. Susceptibility of β-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. J. Dairy Sci. 78 (1995) 2336-2344
    • (1995) J. Dairy Sci. , vol.78 , pp. 2336-2344
    • Guo, M.R.1    Fox, P.F.2    Kindstedt, P.S.3
  • 27
    • 0030100299 scopus 로고    scopus 로고
    • Purification of β-lactoglobulin from whey protein concentrate by pepsin treatment
    • Kinekawa Y., and Kitabatake N. Purification of β-lactoglobulin from whey protein concentrate by pepsin treatment. J. Dairy Sci. 79 (1996) 350-356
    • (1996) J. Dairy Sci. , vol.79 , pp. 350-356
    • Kinekawa, Y.1    Kitabatake, N.2
  • 30
    • 0025013513 scopus 로고
    • β-Lactoglobulin: a protein drug carrier?
    • McAlpine A.S., and Sawyer L. β-Lactoglobulin: a protein drug carrier?. Biochem. Soc. Trans. 18 (1990) 879
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 879
    • McAlpine, A.S.1    Sawyer, L.2
  • 32
    • 84986450183 scopus 로고
    • Hybrid Monte Carlo: an efficient algorithm for condensed matter simulation
    • Clamp M.E., Baker P.G., Stirling C.J., and Brass A. Hybrid Monte Carlo: an efficient algorithm for condensed matter simulation. J. Comput. Chem. 15 (1994) 838-846
    • (1994) J. Comput. Chem. , vol.15 , pp. 838-846
    • Clamp, M.E.1    Baker, P.G.2    Stirling, C.J.3    Brass, A.4
  • 33
    • 0000167458 scopus 로고
    • A Smart Monte Carlo technique for free energy simulations of multiconformational molecules: direct calculations of the conformational populations of organic molecules
    • Senderowitz H., Guarnieri F., and Still W.C. A Smart Monte Carlo technique for free energy simulations of multiconformational molecules: direct calculations of the conformational populations of organic molecules. J. Am. Chem. Soc. 117 (1995) 8211-8219
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8211-8219
    • Senderowitz, H.1    Guarnieri, F.2    Still, W.C.3
  • 37
    • 0018781995 scopus 로고
    • Electrophoretic analysis of the unfolding of proteins by urea
    • Creighton T.E. Electrophoretic analysis of the unfolding of proteins by urea. J. Mol. Biol. 129 (1979) 235-264
    • (1979) J. Mol. Biol. , vol.129 , pp. 235-264
    • Creighton, T.E.1
  • 38
    • 0032547692 scopus 로고    scopus 로고
    • Denaturant-gradient gel electrophoresis: technical aspects and practical applications
    • Gianazza E., Eberini I., Santi O., and Vignati M. Denaturant-gradient gel electrophoresis: technical aspects and practical applications. Anal. Chim. Acta 372 (1998) 99-120
    • (1998) Anal. Chim. Acta , vol.372 , pp. 99-120
    • Gianazza, E.1    Eberini, I.2    Santi, O.3    Vignati, M.4
  • 39
    • 0036037132 scopus 로고    scopus 로고
    • The ligand-binding site of bovine β-lactoglobulin: evidence for a function
    • Kontopidis G., Holt C., and Sawyer L. The ligand-binding site of bovine β-lactoglobulin: evidence for a function. J. Mol. Biol. 318 (2002) 1043-1055
    • (2002) J. Mol. Biol. , vol.318 , pp. 1043-1055
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 40
    • 0028234099 scopus 로고
    • Structural modeling and electrostatic properties of aspartate transcarbamylase from Saccharomyces cerevisiae
    • Villoutreix B.O., Spassov V.Z., Atanasov B.P., Herve G., and Ladjimi M.M. Structural modeling and electrostatic properties of aspartate transcarbamylase from Saccharomyces cerevisiae. Proteins 19 (1994) 230-243
    • (1994) Proteins , vol.19 , pp. 230-243
    • Villoutreix, B.O.1    Spassov, V.Z.2    Atanasov, B.P.3    Herve, G.4    Ladjimi, M.M.5
  • 41
    • 0028246854 scopus 로고
    • Probing the retinol-binding site of bovine β-lactoglobulin
    • Cho Y., Batt C.A., and Sawyer L. Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269 (1994) 11102-11107
    • (1994) J. Biol. Chem. , vol.269 , pp. 11102-11107
    • Cho, Y.1    Batt, C.A.2    Sawyer, L.3
  • 42
    • 0028454828 scopus 로고
    • The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure
    • Böhm H.J. The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure. J. Comp. Aided Mol. Des. 8 (1994) 243-256
    • (1994) J. Comp. Aided Mol. Des. , vol.8 , pp. 243-256
    • Böhm, H.J.1
  • 43
    • 0001471515 scopus 로고    scopus 로고
    • The Nosé-Poincaré method for constant temperature molecular dynamics
    • Bond S.D., Benedict J.L., and Laird B.B. The Nosé-Poincaré method for constant temperature molecular dynamics. J. Comp. Phys. 151 (1999) 114-134
    • (1999) J. Comp. Phys. , vol.151 , pp. 114-134
    • Bond, S.D.1    Benedict, J.L.2    Laird, B.B.3
  • 44
    • 0022555881 scopus 로고
    • Detection of folding intermediates using urea-gradient electrophoresis
    • Creighton T.E. Detection of folding intermediates using urea-gradient electrophoresis. Methods Enzymol. 131 (1986) 156-172
    • (1986) Methods Enzymol. , vol.131 , pp. 156-172
    • Creighton, T.E.1
  • 45
    • 0019324834 scopus 로고
    • Kinetic study of protein unfolding and refolding using urea gradient electrophoresis
    • Creighton T.E. Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J. Mol. Biol. 137 (1980) 61-80
    • (1980) J. Mol. Biol. , vol.137 , pp. 61-80
    • Creighton, T.E.1
  • 46
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins
    • Binkowski T.A., Naghibzadeh S., and Liang J. CASTp: computed atlas of surface topography of proteins. Nucleic Acids Res. 31 (2003) 3352-3355
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 50
    • 37349014211 scopus 로고    scopus 로고
    • A.M. Masel, K.T. Bell, Comparison of equine I and II β-lactoglobulin genes, submitted to EMBL/GenBank/DDBJ databases, 1996.
  • 53
    • 33748276474 scopus 로고    scopus 로고
    • Protein-ligand docking: current status and future challenges
    • Sousa S.F., Fernandes P.A., and Ramos M.J. Protein-ligand docking: current status and future challenges. Proteins 65 (2006) 15-26
    • (2006) Proteins , vol.65 , pp. 15-26
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 54
    • 33845335781 scopus 로고    scopus 로고
    • Towards predictive ligand design with free-energy based computational methods?
    • Foloppe N., and Hubbard R. Towards predictive ligand design with free-energy based computational methods?. Curr. Med. Chem. 13 (2006) 3583-3608
    • (2006) Curr. Med. Chem. , vol.13 , pp. 3583-3608
    • Foloppe, N.1    Hubbard, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.