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Volumn 28, Issue 14, 2012, Pages 5913-5920

Synthesis of three novel anionic gemini surfactants and comparative studies of their assemble behavior in the presence of bovine serum albumin

Author keywords

[No Author keywords available]

Indexed keywords

ANIONIC GEMINI SURFACTANT; BOVINE SERUM ALBUMINS; CD SPECTRA; COMPARATIVE STUDIES; CONCENTRATION REGION; FLUORESCENCE SPECTRA; GEMINI SURFACTANT; HIGH CONCENTRATION; HYDROPHOBIC TAILS; LOW CONCENTRATIONS; MICROENVIRONMENTS; PHYSIOLOGICAL PH; SECONDARY STRUCTURES; SPECTRAL METHODS; SURFACE TENSION MEASUREMENTS; SURFACTANT CONCENTRATIONS; TAIL LENGTH;

EID: 84859562768     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la204212s     Document Type: Article
Times cited : (72)

References (35)
  • 4
    • 84878113803 scopus 로고    scopus 로고
    • Synthesis and Some Properties of Fluorinated Cationic Surfactants
    • Mohamed, M. Z.; Mohamed, A. S. Synthesis and Some Properties of Fluorinated Cationic Surfactants J. Surfactants Deterg. 2009, 13, 521-528
    • (2009) J. Surfactants Deterg. , vol.13 , pp. 521-528
    • Mohamed, M.Z.1    Mohamed, A.S.2
  • 5
    • 0013112779 scopus 로고    scopus 로고
    • Gemini surfactants: A distinct class of self-assembling molecules [Review]
    • Hait, S. K.; Moulik, S. P. Gemini surfactants: A distinct class of self-assembling molecules [Review] Curr. Sci. 2002, 82, 1101-1111
    • (2002) Curr. Sci. , vol.82 , pp. 1101-1111
    • Hait, S.K.1    Moulik, S.P.2
  • 6
    • 84861538974 scopus 로고    scopus 로고
    • Anionic Gemini Surfactants: A Distinct Class of Surfactants
    • Shukla, D.; Tyagi, V. K. Anionic Gemini Surfactants: A Distinct Class of Surfactants J. Oleo. Sci. 2006, 55, 215-226
    • (2006) J. Oleo. Sci. , vol.55 , pp. 215-226
    • Shukla, D.1    Tyagi, V.K.2
  • 7
    • 3042686687 scopus 로고    scopus 로고
    • Synthesis and surface properties of anionic gemini surfactants with amide groups
    • Yoshimura, T.; Esumi, K. Synthesis and surface properties of anionic gemini surfactants with amide groups J. Colloid Interface Sci. 2004, 276, 231-238
    • (2004) J. Colloid Interface Sci. , vol.276 , pp. 231-238
    • Yoshimura, T.1    Esumi, K.2
  • 8
    • 36649034484 scopus 로고    scopus 로고
    • New anionic gemini surfactant based on EDTA accessible by convenient synthesis
    • Wattebled, L.; Laschewsky, A. New anionic gemini surfactant based on EDTA accessible by convenient synthesis Colloid Polym. Sci. 2007, 285, 1387-1393
    • (2007) Colloid Polym. Sci. , vol.285 , pp. 1387-1393
    • Wattebled, L.1    Laschewsky, A.2
  • 9
    • 0001684352 scopus 로고
    • Surfactant interaction with biomembranes and proteins
    • Jones, M. N. Surfactant interaction with biomembranes and proteins Chem. Soc. Rev. 1992, 21, 127-136
    • (1992) Chem. Soc. Rev. , vol.21 , pp. 127-136
    • Jones, M.N.1
  • 10
    • 70349923640 scopus 로고    scopus 로고
    • Interaction of Bovine (BSA), Rabbit (RSA), and Porcine (PSA) Serum Albumins with Cationic Single-Chain/Gemini Surfactants: A Comparative Study
    • Gull, N.; Sen, P.; Khan, R. H.; Kabir-ud-Din Interaction of Bovine (BSA), Rabbit (RSA), and Porcine (PSA) Serum Albumins with Cationic Single-Chain/Gemini Surfactants: A Comparative Study Langmuir 2009, 25, 11686-11691
    • (2009) Langmuir , vol.25 , pp. 11686-11691
    • Gull, N.1    Sen, P.2    Khan, R.H.3    Kabir-Ud-Din4
  • 11
    • 33751155438 scopus 로고
    • Spectroscopic Probe Analysis of Protein-Surfactant Interactions: The BSA/SDS System
    • Turro, N. J.; Lei, X. G. Spectroscopic Probe Analysis of Protein-Surfactant Interactions: The BSA/SDS System Langmuir 1995, 11, 2525-2533
    • (1995) Langmuir , vol.11 , pp. 2525-2533
    • Turro, N.J.1    Lei, X.G.2
  • 12
    • 0036165334 scopus 로고    scopus 로고
    • A Multitechnique Approach in Protein/Surfactant Interaction Study: Physicochemical Aspects of Sodium Dodecyl Sulfate in the Presence of Trypsin in Aqueous Medium
    • Ghosh, S.; Banerjee, A. A Multitechnique Approach in Protein/Surfactant Interaction Study: Physicochemical Aspects of Sodium Dodecyl Sulfate in the Presence of Trypsin in Aqueous Medium Biomacromolecules 2002, 3, 9-16
    • (2002) Biomacromolecules , vol.3 , pp. 9-16
    • Ghosh, S.1    Banerjee, A.2
  • 13
    • 58249132510 scopus 로고    scopus 로고
    • Comparative studies of interactions of hemoglobin with single-chain and with gemini surfactants
    • Wang, Y. S.; Guo, R.; Xi, J. Comparative studies of interactions of hemoglobin with single-chain and with gemini surfactants J. Colloid Interface Sci. 2009, 331, 470-475
    • (2009) J. Colloid Interface Sci. , vol.331 , pp. 470-475
    • Wang, Y.S.1    Guo, R.2    Xi, J.3
  • 14
    • 33646405452 scopus 로고    scopus 로고
    • Comparative Studies on Interactions of Bovine Serum Albumin with Cationic Gemini and Single-Chain Surfactants
    • Li, Y. J.; Wang, X. Y.; Wang, Y. L. Comparative Studies on Interactions of Bovine Serum Albumin with Cationic Gemini and Single-Chain Surfactants J. Phys. Chem. B 2006, 110, 8499-8505
    • (2006) J. Phys. Chem. B , vol.110 , pp. 8499-8505
    • Li, Y.J.1    Wang, X.Y.2    Wang, Y.L.3
  • 15
    • 59049102515 scopus 로고    scopus 로고
    • Comparative study on interaction of bovine serum albumin with dissymmetric and symmetric gemini surfactant by spectral method
    • Wu, Dan.; Xu, G. Y.; Feng, Y. J.; Wang, Y. J.; Zhu, Y. Y. Comparative study on interaction of bovine serum albumin with dissymmetric and symmetric gemini surfactant by spectral method Colloid Polym. Sci. 2009, 287, 225-230
    • (2009) Colloid Polym. Sci. , vol.287 , pp. 225-230
    • Wu, D.1    Xu, G.Y.2    Feng, Y.J.3    Wang, Y.J.4    Zhu, Y.Y.5
  • 16
    • 33947481423 scopus 로고
    • Surfactant Adsorption at the Solid-Liquid Interface-Dependence of Mechanism on Chain Length
    • Somasundaran, P.; Healy, T. W.; Fuerstenau, D. W. Surfactant Adsorption at the Solid-Liquid Interface-Dependence of Mechanism on Chain Length J. Phys. Chem. 1964, 68, 3562-3566
    • (1964) J. Phys. Chem. , vol.68 , pp. 3562-3566
    • Somasundaran, P.1    Healy, T.W.2    Fuerstenau, D.W.3
  • 17
    • 20444481737 scopus 로고    scopus 로고
    • Gemini surfactants, the effect of hydrophobic chain length and dissymmetry
    • Oda, R.; Huc, I.; Candau, S. J. Gemini surfactants, the effect of hydrophobic chain length and dissymmetry Chem. Commun. 1997, 21, 2105-2106
    • (1997) Chem. Commun. , vol.21 , pp. 2105-2106
    • Oda, R.1    Huc, I.2    Candau, S.J.3
  • 18
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • Huang, B. X.; Kim, H. Y.; Dass, C. Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry J. Am. Soc. Mass. Spectrom. 2004, 15, 1237-1247
    • (2004) J. Am. Soc. Mass. Spectrom. , vol.15 , pp. 1237-1247
    • Huang, B.X.1    Kim, H.Y.2    Dass, C.3
  • 20
    • 0001221576 scopus 로고
    • Fluorescence spectra of anthracene and pyrene in water and in aqueous surfactant solution
    • Nakajima, A. Fluorescence spectra of anthracene and pyrene in water and in aqueous surfactant solution J. Lumin. 1977, 15, 277-282
    • (1977) J. Lumin. , vol.15 , pp. 277-282
    • Nakajima, A.1
  • 21
    • 84859620788 scopus 로고    scopus 로고
    • v 8.1; Tripos Associates Inc. St. Louis, MO, USA
    • SYBYL v 8.1; Tripos Associates Inc., St. Louis, MO, USA, 2008.
    • (2008) SYBYL
  • 22
    • 0027136282 scopus 로고
    • Comparative Protein Modelling by Satisfaction of Spatial Restraints
    • Sali, A.; Blundell, T. L. Comparative Protein Modelling by Satisfaction of Spatial Restraints J. Mol. Biol. 1993, 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 23
    • 58749084516 scopus 로고    scopus 로고
    • Using AutoDock for ligand-receptor docking
    • John Wiley & Sons: New York, Chapter 8, Unit 8.14
    • Morris, G. M.; Huey, R.; Olson, A. J. Using AutoDock for ligand-receptor docking. In Current Protocols in Bioinformatics; John Wiley & Sons: New York, 2008; Chapter 8, Unit 8.14.
    • (2008) Current Protocols in Bioinformatics
    • Morris, G.M.1    Huey, R.2    Olson, A.J.3
  • 24
    • 33847310205 scopus 로고    scopus 로고
    • Daidzein interaction with human serum albumin studied using optical spectroscopy and molecular modeling methods
    • Li, Y.; He, W.; Liu, H.; Yao, X.; Hu, Z. Daidzein interaction with human serum albumin studied using optical spectroscopy and molecular modeling methods J. Mol. Struct. 2007, 831, 144-150
    • (2007) J. Mol. Struct. , vol.831 , pp. 144-150
    • Li, Y.1    He, W.2    Liu, H.3    Yao, X.4    Hu, Z.5
  • 26
    • 34547331164 scopus 로고    scopus 로고
    • Surfactant-induced protein unfolding as studied by small-angle neutron scattering and dynamic light scattering
    • Chodankar, S.; Aswal, V. K.; Kohlbrecher, J.; Vavrin, R.; Wagh, A. G. Surfactant-induced protein unfolding as studied by small-angle neutron scattering and dynamic light scattering J. Phys.: Condens. Matter 2007, 19, 326102-326114
    • (2007) J. Phys.: Condens. Matter , vol.19 , pp. 326102-326114
    • Chodankar, S.1    Aswal, V.K.2    Kohlbrecher, J.3    Vavrin, R.4    Wagh, A.G.5
  • 27
    • 0035960767 scopus 로고    scopus 로고
    • The Lysozyme-Dodecyl Sulfate System: An Example of Protein-Surfactant Aggregation
    • Stenstam, A.; Khan, A.; Wennerström, H. The Lysozyme-Dodecyl Sulfate System: An Example of Protein-Surfactant Aggregation Langmuir 2001, 17, 7513-7520
    • (2001) Langmuir , vol.17 , pp. 7513-7520
    • Stenstam, A.1    Khan, A.2    Wennerström, H.3
  • 29
    • 0026373840 scopus 로고
    • Theory of surfactant self-assembly: A predictive molecular thermodynamic approach
    • Nagarajan, R.; Ruckenstein, E. Theory of surfactant self-assembly: a predictive molecular thermodynamic approach Langmuir 1991, 7, 2934-2969
    • (1991) Langmuir , vol.7 , pp. 2934-2969
    • Nagarajan, R.1    Ruckenstein, E.2
  • 30
    • 0037456021 scopus 로고    scopus 로고
    • Quenching of BSA intrinsic fluorescence by alkylpyridinium cations: Its relationship to surfactant-protein association
    • Diaz, X.; Abuin, E.; Lissi, E. Quenching of BSA intrinsic fluorescence by alkylpyridinium cations: Its relationship to surfactant-protein association J. Photochem. Photobiol. A: Chem. 2003, 155, 157-162
    • (2003) J. Photochem. Photobiol. A: Chem. , vol.155 , pp. 157-162
    • Diaz, X.1    Abuin, E.2    Lissi, E.3
  • 31
    • 33749343561 scopus 로고    scopus 로고
    • Interactions between Bovine Serum Albumin and Gemini Surfactant Alkanediyl-a, w-Bis(Dimethyldodecyl- Ammonium Bromide)
    • Pi, Y. Y.; Shang, Y. Z.; Peng, C. J.; Liu, H. L.; Hu, Y.; Jiang, J. W. Interactions between Bovine Serum Albumin and Gemini Surfactant Alkanediyl-a, w-Bis(Dimethyldodecyl- Ammonium Bromide) Biopolymers 2006, 83, 243-249
    • (2006) Biopolymers , vol.83 , pp. 243-249
    • Pi, Y.Y.1    Shang, Y.Z.2    Peng, C.J.3    Liu, H.L.4    Hu, Y.5    Jiang, J.W.6
  • 32
    • 33746529856 scopus 로고    scopus 로고
    • The Unusual Micelle Micropolarity of Partially Fluorinated Gemini Surfactants Sensed by Pyrene Fluorescence
    • Asakawa, T.; Okada, T.; Hayasaka, T.; Kuwamoto, K.; Ohta, A.; Miyagishi, S. The Unusual Micelle Micropolarity of Partially Fluorinated Gemini Surfactants Sensed by Pyrene Fluorescence Langmuir 2006, 22, 6053-6055
    • (2006) Langmuir , vol.22 , pp. 6053-6055
    • Asakawa, T.1    Okada, T.2    Hayasaka, T.3    Kuwamoto, K.4    Ohta, A.5    Miyagishi, S.6
  • 33
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
    • Sreerama, N.; Woody, R. W. Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set Anal. Biochem. 2000, 287, 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2


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