메뉴 건너뛰기




Volumn 1794, Issue 11, 2009, Pages 1700-1708

Kinetics and thermodynamics of the interaction of 1-anilino-naphthalene-8-sulfonate with proteins

Author keywords

Kinetic model; Ligand binding; Molecular docking; Multiple technique approach; Protein interaction

Indexed keywords

BOVINE SERUM ALBUMIN; PROTEIN; SULFONIC ACID DERIVATIVE; WATER;

EID: 70249089273     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.08.007     Document Type: Article
Times cited : (81)

References (42)
  • 1
    • 0041341891 scopus 로고    scopus 로고
    • Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine beta-lactoglobulin
    • Collini M., D'Alfonso L., Molinari H., Ragona L., Catalano M., and Baldini G. Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine beta-lactoglobulin. Protein Sci. 12 (2003) 1596-1603
    • (2003) Protein Sci. , vol.12 , pp. 1596-1603
    • Collini, M.1    D'Alfonso, L.2    Molinari, H.3    Ragona, L.4    Catalano, M.5    Baldini, G.6
  • 2
    • 67649101639 scopus 로고    scopus 로고
    • A competition assay for DNA binding using the fluorescent probe ANS
    • Taylor I.A., and Kneale G.G. A competition assay for DNA binding using the fluorescent probe ANS. Methods Mol. Biol. 543 (2009) 577-587
    • (2009) Methods Mol. Biol. , vol.543 , pp. 577-587
    • Taylor, I.A.1    Kneale, G.G.2
  • 3
    • 0042029724 scopus 로고    scopus 로고
    • The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism
    • Lartigue A., Gruez A., Spinelli S., Riviere S., Brossut R., Tegoni M., and Cambillau C. The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism. J. Biol. Chem. 278 (2003) 30213-30218
    • (2003) J. Biol. Chem. , vol.278 , pp. 30213-30218
    • Lartigue, A.1    Gruez, A.2    Spinelli, S.3    Riviere, S.4    Brossut, R.5    Tegoni, M.6    Cambillau, C.7
  • 4
    • 39749200245 scopus 로고    scopus 로고
    • Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus
    • Cattoni D.I., Flecha F.L.G., and Arguello J.M. Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus. Arch. Biochem. Biophys. 471 (2008) 198-206
    • (2008) Arch. Biochem. Biophys. , vol.471 , pp. 198-206
    • Cattoni, D.I.1    Flecha, F.L.G.2    Arguello, J.M.3
  • 6
    • 0013913906 scopus 로고
    • Cooperative Effects in Binding by Bovine Serum Albumin. I. The Binding of 1-Anilino-8-naphthalenesulfonate. Fluorimetric Titrations
    • E. Daniel, G. Weber, Cooperative Effects in Binding by Bovine Serum Albumin. I. The Binding of 1-Anilino-8-naphthalenesulfonate. Fluorimetric Titrations Biochemistry 5 (1966) 1893-1900.
    • (1966) Biochemistry , vol.5 , pp. 1893-1900
    • Daniel, E.1    Weber, G.2
  • 7
    • 0033135193 scopus 로고    scopus 로고
    • 1-anilino-8-naphthalene sulfonate as a protein conformational tightening agent
    • Matulis D., Baumann C.G., Bloomfield V.A., and Lovrien R.E. 1-anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 49 (1999) 451-458
    • (1999) Biopolymers , vol.49 , pp. 451-458
    • Matulis, D.1    Baumann, C.G.2    Bloomfield, V.A.3    Lovrien, R.E.4
  • 8
    • 33750726988 scopus 로고    scopus 로고
    • Photophysics of ANS. III: Circular dichroism of ANS and anilinonaphthalene in I-FABP
    • Kirk W., and Klimtchuk E. Photophysics of ANS. III: Circular dichroism of ANS and anilinonaphthalene in I-FABP. Biophys. Chem. 125 (2007) 24-31
    • (2007) Biophys. Chem. , vol.125 , pp. 24-31
    • Kirk, W.1    Klimtchuk, E.2
  • 9
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis D., and Lovrien R. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74 (1998) 422-429
    • (1998) Biophys. J. , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 10
    • 78651058006 scopus 로고
    • Polarization of the fluorescence of macromolecules. II. Fluorescent conjugates of ovalbumin and bovine serum albumin
    • Weber G. Polarization of the fluorescence of macromolecules. II. Fluorescent conjugates of ovalbumin and bovine serum albumin. Biochem. J. 51 (1952) 155-167
    • (1952) Biochem. J. , vol.51 , pp. 155-167
    • Weber, G.1
  • 11
    • 0032774245 scopus 로고    scopus 로고
    • Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate
    • Ory J.J., and Banaszak L.J. Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate. Biophys. J. 77 (1999) 1107-1116
    • (1999) Biophys. J. , vol.77 , pp. 1107-1116
    • Ory, J.J.1    Banaszak, L.J.2
  • 12
    • 0034612339 scopus 로고    scopus 로고
    • Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA
    • Schonbrunn E., Eschenburg S., Luger K., Kabsch W., and Amrhein N. Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 6345-63499
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6345-63499
    • Schonbrunn, E.1    Eschenburg, S.2    Luger, K.3    Kabsch, W.4    Amrhein, N.5
  • 13
    • 0021095677 scopus 로고
    • Intramolecular donor-acceptor systems. 10. Multiple fluorescences from 8-(N-phenylamino)-1-naphthalenesulfonates
    • Kosower E.M., and Kanety H. Intramolecular donor-acceptor systems. 10. Multiple fluorescences from 8-(N-phenylamino)-1-naphthalenesulfonates. J. Am. Chem. Soc. 105 (1983) 6236-6243
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6236-6243
    • Kosower, E.M.1    Kanety, H.2
  • 14
    • 0001198146 scopus 로고
    • Electron hydration dynamics using the 2-anilinonaphthalene precursor
    • Lee J., and Robinson G.W. Electron hydration dynamics using the 2-anilinonaphthalene precursor. J. Am. Chem. Soc. 107 (1985) 6153-6156
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6153-6156
    • Lee, J.1    Robinson, G.W.2
  • 15
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45 (1994) 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 16
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G., Birkett D.J., and Wade D.N. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11 (1975) 824-832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 17
    • 9144248624 scopus 로고    scopus 로고
    • Determination of the molecular size of BSA by fluorescence anisotropy
    • González Flecha F.L., and Levi V. Determination of the molecular size of BSA by fluorescence anisotropy. Biochem. Mol. Biol. Educ. 31 (2003) 319-322
    • (2003) Biochem. Mol. Biol. Educ. , vol.31 , pp. 319-322
    • González Flecha, F.L.1    Levi, V.2
  • 19
    • 0000478993 scopus 로고
    • Fragmentation of bovine serum albumin by pepsin. I. The origin of the acid expansion of the albumin molecule
    • Weber G., and Young L.B. Fragmentation of bovine serum albumin by pepsin. I. The origin of the acid expansion of the albumin molecule. J. Biol. Chem. 239 (1964) 1415-1423
    • (1964) J. Biol. Chem. , vol.239 , pp. 1415-1423
    • Weber, G.1    Young, L.B.2
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 21
    • 19544369340 scopus 로고    scopus 로고
    • Direct characterization of the folded, unfolded and urea-denatured states of the c-terminal domain of the ribosomal protein L9
    • Li Y., Picart F., and Raleigh D.P. Direct characterization of the folded, unfolded and urea-denatured states of the c-terminal domain of the ribosomal protein L9. J. Mol. Biol. 349 (2005) 839-846
    • (2005) J. Mol. Biol. , vol.349 , pp. 839-846
    • Li, Y.1    Picart, F.2    Raleigh, D.P.3
  • 22
    • 0016205019 scopus 로고
    • Kinetic studies on binding of bovine serum albumin with 1-anilino-8-naphthalene sulfonate
    • Nakatani H., Haga M., and Hiromi K. Kinetic studies on binding of bovine serum albumin with 1-anilino-8-naphthalene sulfonate. FEBS Lett. 43 (1974) 293-296
    • (1974) FEBS Lett. , vol.43 , pp. 293-296
    • Nakatani, H.1    Haga, M.2    Hiromi, K.3
  • 25
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 26
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G.M., Halliday R.S., Huey R., Hart W.E., Belew R.K., Olson A.J., and G.S. D. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comp. Chem. 19 (1998) 1639-1662
    • (1998) J. Comp. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Halliday, R.S.2    Huey, R.3    Hart, W.E.4    Belew, R.K.5    Olson, A.J.6    G.S., D.7
  • 27
    • 0033397980 scopus 로고    scopus 로고
    • Python: a programming language for software integration and development
    • Sanner M.F. Python: a programming language for software integration and development. J. Mol. Graphics Mod. 17 (1999) 57-61
    • (1999) J. Mol. Graphics Mod. , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 28
    • 0018091195 scopus 로고
    • Application of Akaike's information criterion (AIC) in the evaluation of linear pharmacokinetic equations
    • Yamaoka K., Nakagawa T., and Uno T. Application of Akaike's information criterion (AIC) in the evaluation of linear pharmacokinetic equations. J. Pharm. Biopharm. 6 (1978) 165-175
    • (1978) J. Pharm. Biopharm. , vol.6 , pp. 165-175
    • Yamaoka, K.1    Nakagawa, T.2    Uno, T.3
  • 30
    • 10744230472 scopus 로고    scopus 로고
    • Reversible fast-dimerization of bovine serum albumin detected by fluorescence resonance energy transfer
    • Levi V., and González Flecha F.L. Reversible fast-dimerization of bovine serum albumin detected by fluorescence resonance energy transfer. Biochim. Biophys. Acta 1599 (2002) 141-148
    • (2002) Biochim. Biophys. Acta , vol.1599 , pp. 141-148
    • Levi, V.1    González Flecha, F.L.2
  • 31
    • 0032545025 scopus 로고    scopus 로고
    • Induced circular dichroism and UV-vis absorption spectroscopy of cyclodextrin inclusion complexes: structural elucidation of supramolecular azi-adamantane (spiro[adamantane-2, 3′-diazirine])
    • Krois D., and Brinker U.H. Induced circular dichroism and UV-vis absorption spectroscopy of cyclodextrin inclusion complexes: structural elucidation of supramolecular azi-adamantane (spiro[adamantane-2, 3′-diazirine]). J. Am. Chem. Soc. 120 (1998) 11627-11632
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11627-11632
    • Krois, D.1    Brinker, U.H.2
  • 32
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya A.A., Grune T., and Curry S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 303 (2000) 721-732
    • (2000) J. Mol. Biol. , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grune, T.2    Curry, S.3
  • 35
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt S., and Freire E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 11 (2001) 560-566
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 36
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: insights for ligand design
    • Olsson T.S., Williams M.A., Pitt W.R., and Ladbury J.E. The thermodynamics of protein-ligand interaction and solvation: insights for ligand design. J. Mol. Biol. 384 (2008) 1002-1017
    • (2008) J. Mol. Biol. , vol.384 , pp. 1002-1017
    • Olsson, T.S.1    Williams, M.A.2    Pitt, W.R.3    Ladbury, J.E.4
  • 37
    • 33646359689 scopus 로고    scopus 로고
    • Binding of 8-anilinonaphthalene sulfonate to dimeric and tetrameric concanavalin A: energetics and its implications on saccharide binding studied by isothermal titration calorimetry and spectroscopy
    • Banerjee T., and Kishore N. Binding of 8-anilinonaphthalene sulfonate to dimeric and tetrameric concanavalin A: energetics and its implications on saccharide binding studied by isothermal titration calorimetry and spectroscopy. J. Phys. Chem. B 110 (2006) 7022-7028
    • (2006) J. Phys. Chem. B , vol.110 , pp. 7022-7028
    • Banerjee, T.1    Kishore, N.2
  • 39
    • 0038309550 scopus 로고    scopus 로고
    • Protein stability induced by ligand binding correlates with changes in protein flexibility
    • Celej M.S., Montich G.G., and Fidelio G.D. Protein stability induced by ligand binding correlates with changes in protein flexibility. Protein. Sci. 12 (2003) 1496-1506
    • (2003) Protein. Sci. , vol.12 , pp. 1496-1506
    • Celej, M.S.1    Montich, G.G.2    Fidelio, G.D.3
  • 40
    • 0014640053 scopus 로고
    • The circular dichroism spectra of the complexes of 1-anilino-8-naphthalenesulfonate with bovine serum albumin. Evidence for heterogeneity of binding
    • Anderson S. The circular dichroism spectra of the complexes of 1-anilino-8-naphthalenesulfonate with bovine serum albumin. Evidence for heterogeneity of binding. Biochemistry 12 (1969) 4838-4842
    • (1969) Biochemistry , vol.12 , pp. 4838-4842
    • Anderson, S.1
  • 41
    • 40549127817 scopus 로고    scopus 로고
    • A fluorescence analysis of ANS bound to bovine serum albumin: binding properties revisited by using energy transfer
    • Togashi D., and Ryder A. A fluorescence analysis of ANS bound to bovine serum albumin: binding properties revisited by using energy transfer. J. Fluoresc. 18 (2008) 519-526
    • (2008) J. Fluoresc. , vol.18 , pp. 519-526
    • Togashi, D.1    Ryder, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.