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Volumn 261, Issue , 2012, Pages 369-374

In situ ATR-IR spectroscopy study of adsorbed protein: Visible light denaturation of bovine serum albumin on TiO 2

Author keywords

BSA adsorption; Denaturation; In situ spectroscopy; Protein structure; Visible light

Indexed keywords

BODY FLUIDS; CURVE FITTING; DENATURATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MAMMALS; POLYMER FILMS; PROTEINS; SPECTRUM ANALYSIS; SURFACE PLASMON RESONANCE; TITANIUM DIOXIDE;

EID: 84867745301     PISSN: 01694332     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.apsusc.2012.08.017     Document Type: Article
Times cited : (86)

References (50)
  • 1
    • 23444457779 scopus 로고    scopus 로고
    • Characterization of a dimeric unfolding intermediate of bovine serum albumin under mildly acidic condition
    • A. Brahma, C. Mandal, and D. Bhattacharyya Characterization of a dimeric unfolding intermediate of bovine serum albumin under mildly acidic condition Biochimica et Biophysica Acta - Proteins and Proteomics 1751 2 2005 159 169
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1751 , Issue.2 , pp. 159-169
    • Brahma, A.1    Mandal, C.2    Bhattacharyya, D.3
  • 2
    • 33748573272 scopus 로고    scopus 로고
    • Protein secondary structure controlled with light and photoresponsive surfactants
    • S. Wang, and C. Ted Lee Jr. Protein secondary structure controlled with light and photoresponsive surfactants Journal of Physical Chemistry B 110 2006 16117 16123
    • (2006) Journal of Physical Chemistry B , vol.110 , pp. 16117-16123
    • Wang, S.1    Ted Lee, Jr.C.2
  • 5
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • V. Militello, C. Casarino, A. Emanuele, A. Giostra, F. Pullara, and M. Leone Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering Biophysical Chemistry 107 2 2004 175 187
    • (2004) Biophysical Chemistry , vol.107 , Issue.2 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 6
    • 33645704194 scopus 로고    scopus 로고
    • Methods for measuring protein aggregation
    • S.E. Bondos Methods for measuring protein aggregation Current Analytical Chemistry 2 2 2006 157 170
    • (2006) Current Analytical Chemistry , vol.2 , Issue.2 , pp. 157-170
    • Bondos, S.E.1
  • 7
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • K. Nakanishi, T. Sakiyama, and K. Imamura On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon Journal of Bioscience and Bioengineering 91 3 2001 233 244
    • (2001) Journal of Bioscience and Bioengineering , vol.91 , Issue.3 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 8
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: Effect of topography at the nanometer scale and chemistry
    • P. Roach, D. Farrar, and C.C. Perry Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry Journal of the American Chemical Society 128 12 2006 3939 3945
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.12 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 9
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    • N. Brandes, P.B. Welzel, C. Werner, and L.W. Kroh Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis Journal of Colloid and Interface Science 299 1 2006 56 69
    • (2006) Journal of Colloid and Interface Science , vol.299 , Issue.1 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4
  • 10
    • 23844548026 scopus 로고    scopus 로고
    • Change of the zeta potential of biocompatible colloidal oxide particles upon adsorption of bovine serum albumin and lysozyme
    • K. Rezwan, A.R. Studart, J. Vörös, and L.J. Gauckler Change of the zeta potential of biocompatible colloidal oxide particles upon adsorption of bovine serum albumin and lysozyme Journal of Physical Chemistry B 109 30 2005 14469 14474
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.30 , pp. 14469-14474
    • Rezwan, K.1    Studart, A.R.2    Vörös, J.3    Gauckler, L.J.4
  • 11
    • 17444385644 scopus 로고    scopus 로고
    • A prediction method for the isoelectric point of binary protein mixtures of bovine serum albumin and lysozyme adsorbed on colloidal Titania and alumina particles
    • K. Rezwan, L.P. Meier, and L.J. Gauckler A prediction method for the isoelectric point of binary protein mixtures of bovine serum albumin and lysozyme adsorbed on colloidal Titania and alumina particles Langmuir 21 8 2005 3493 3497
    • (2005) Langmuir , vol.21 , Issue.8 , pp. 3493-3497
    • Rezwan, K.1    Meier, L.P.2    Gauckler, L.J.3
  • 12
    • 34047244215 scopus 로고    scopus 로고
    • Enhanced immunoresponse of antibody/mixed-PEG co-immobilized surface construction of highperformance immunomagnetic ELISA system
    • Y. Nagasaki, H. Kobayashi, Y. Katsuyama, T. Jomura, and T. Sakura Enhanced immunoresponse of antibody/mixed-PEG co-immobilized surface construction of highperformance immunomagnetic ELISA system Journal of Colloid and Interface Science 309 2 2007 524 530
    • (2007) Journal of Colloid and Interface Science , vol.309 , Issue.2 , pp. 524-530
    • Nagasaki, Y.1    Kobayashi, H.2    Katsuyama, Y.3    Jomura, T.4    Sakura, T.5
  • 13
    • 33846670266 scopus 로고    scopus 로고
    • Blocking agents for ELISA quantification of compounds coming from bovine muscle crude extracts
    • M.A. Sentandreu, L. Aubry, F. Toldra, and A. Ouali Blocking agents for ELISA quantification of compounds coming from bovine muscle crude extracts European Food Research and Technology 224 5 2007 623 628
    • (2007) European Food Research and Technology , vol.224 , Issue.5 , pp. 623-628
    • Sentandreu, M.A.1    Aubry, L.2    Toldra, F.3    Ouali, A.4
  • 17
    • 26444619077 scopus 로고    scopus 로고
    • 2 -based photocatalysis: Surface defects, oxygen and charge transfer
    • 2 -based photocatalysis: surface defects, oxygen and charge transfer Topics in Catalysis 35 3-4 2005 197 210
    • (2005) Topics in Catalysis , vol.35 , Issue.34 , pp. 197-210
    • Thompson, T.L.1    Yates, Jr.J.T.2
  • 19
    • 0036295717 scopus 로고    scopus 로고
    • Optimization of immunogold labeling TEM: An ELISA-based method for evaluation of blocking agents for quantitative detection of antigen
    • R. Kaur, K.L. Dikshit, and M. Raje Optimization of immunogold labeling TEM: an ELISA-based method for evaluation of blocking agents for quantitative detection of antigen Journal of Histochemistry & Cytochemistry 50 6 2002 863 873
    • (2002) Journal of Histochemistry & Cytochemistry , vol.50 , Issue.6 , pp. 863-873
    • Kaur, R.1    Dikshit, K.L.2    Raje, M.3
  • 20
  • 22
    • 4444344985 scopus 로고    scopus 로고
    • Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy
    • K. Murayama, and M. Tomida Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy Biochemistry 43 2004 11526 11532
    • (2004) Biochemistry , vol.43 , pp. 11526-11532
    • Murayama, K.1    Tomida, M.2
  • 26
    • 4444246648 scopus 로고    scopus 로고
    • Protein Data Bank, Department of Chemistry, Brookhaven National Laboratory, Upton, NY 11973
    • Structure Explore-1AO6, Protein Data Bank, Department of Chemistry, Brookhaven National Laboratory, Upton, NY 11973, http://www.pdb.bnl.gov/index. html.
    • Structure Explore-1AO6
  • 27
    • 0016724114 scopus 로고
    • Fragment of bovine serum albumin produced by limited proteolysis
    • R.G. Reed, R.C. Feldhoff, O.L. Clute, and T. Peters Jr. Fragment of bovine serum albumin produced by limited proteolysis Biochemistry 14 1975 4578 4583
    • (1975) Biochemistry , vol.14 , pp. 4578-4583
    • Reed, R.G.1    Feldhoff, R.C.2    Clute, O.L.3    Peters, Jr.T.4
  • 29
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • J.T. Pelton, and L.R. McLean Spectroscopic methods for analysis of protein secondary structure Analytical Biochemistry 277 2000 167 176
    • (2000) Analytical Biochemistry , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 31
    • 0000536553 scopus 로고
    • In situ attenuated total reflection Fourier-transform infrared studies of the goethite (alpha-FeOOH)-aqueous solution interface
    • M.I. Tejedor-Tejedor, and M.A. Anderson In situ attenuated total reflection Fourier-transform infrared studies of the goethite (alpha-FeOOH)-aqueous solution interface Langmuir 2 1986 203 210
    • (1986) Langmuir , vol.2 , pp. 203-210
    • Tejedor-Tejedor, M.I.1    Anderson, M.A.2
  • 32
    • 0026923272 scopus 로고
    • Fourier transform infrared attenuated total reflection spectroscopy linear dichroism study of sodium dodecyl sulfate adsorption at the Al%Os/water interface using A1203-coated optics
    • R.P. Sperline, Y. Song, and H. Freiser Fourier transform infrared attenuated total reflection spectroscopy linear dichroism study of sodium dodecyl sulfate adsorption at the Al%Os/water interface using A1203-coated optics Langmuir 8 1992 2183 2191
    • (1992) Langmuir , vol.8 , pp. 2183-2191
    • Sperline, R.P.1    Song, Y.2    Freiser, H.3
  • 33
    • 0042344948 scopus 로고    scopus 로고
    • In situ attenuated total reflection infrared spectroscopy: A sensitive tool for the investigation of reduction-oxidation processes on heterogeneous Pd metal catalysts
    • T. Burgi, R. Wirz, and A. Baiker In situ attenuated total reflection infrared spectroscopy: a sensitive tool for the investigation of reduction-oxidation processes on heterogeneous Pd metal catalysts Journal of Physical Chemistry B 107 28 2003 6774 6781
    • (2003) Journal of Physical Chemistry B , vol.107 , Issue.28 , pp. 6774-6781
    • Burgi, T.1    Wirz, R.2    Baiker, A.3
  • 34
    • 33646140556 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of solid catalysts functioning in the presence of liquid-phase reactants
    • H. Knözinger, Academic Press
    • T. Bürgi, and A. Baiker Attenuated total reflection infrared spectroscopy of solid catalysts functioning in the presence of liquid-phase reactants H. Knözinger, Advances in Catalysis vol. 50 2006 Academic Press 227 283
    • (2006) Advances in Catalysis , vol.50 , pp. 227-283
    • Bürgi, T.1    Baiker, A.2
  • 35
    • 0028521727 scopus 로고
    • 2 in the aqueous-phase
    • 2 in the aqueous-phase Langmuir 10 10 1994 3587 3597
    • (1994) Langmuir , vol.10 , Issue.10 , pp. 3587-3597
    • Hug, S.J.1    Sulzberger, B.2
  • 36
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochimica et Biophysica Sinica 39 8 2007 549 559
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 37
    • 0025613794 scopus 로고
    • 2 O) solution. I. Spectral parameters of amino acid residue absorption bands
    • 2 O) solution. I. Spectral parameters of amino acid residue absorption bands Biopolymers 30 1990 1243 1257
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 38
    • 0025648652 scopus 로고
    • 2 O) solution. II. Amide absorption bands of polypeptide and fibrous protein in α-, β- And random coil conformations
    • 2 O) solution. II. Amide absorption bands of polypeptide and fibrous protein in α-, β- and random coil conformations Biopolymers 30 1990 1259 1271
    • (1990) Biopolymers , vol.30 , pp. 1259-1271
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 39
    • 0025693227 scopus 로고
    • 2 O) solution. III. Estimation of the protein secondary structure
    • 2 O) solution. III. Estimation of the protein secondary structure Biopolymer 30 1990 1273 1280
    • (1990) Biopolymer , vol.30 , pp. 1273-1280
    • Kalnin, B.I.1    Venyaminov, S.Y.2
  • 40
    • 0025357111 scopus 로고
    • Protein secondary structure in water from second-derivative amide i infrared spectra
    • A. Dong, P. Huang, and W.S. Caughey Protein secondary structure in water from second-derivative amide I infrared spectra Biochemistry 29 1990 3303 3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 41
    • 0036114440 scopus 로고    scopus 로고
    • Effect of heavy water on protein flexibility
    • C. Patrizia, and B.S. Giovanni Effect of heavy water on protein flexibility Biophysical Journal 82 2002 3246 3253
    • (2002) Biophysical Journal , vol.82 , pp. 3246-3253
    • Patrizia, C.1    Giovanni, B.S.2
  • 43
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra
    • H. Susi, and D.M. Byler Protein structure by Fourier transform infrared spectroscopy: second derivative spectra Biochemical and Biophysical Research Communications 115 1983 391 397
    • (1983) Biochemical and Biophysical Research Communications , vol.115 , pp. 391-397
    • Susi, H.1    Byler, D.M.2
  • 44
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymer 25 1986 469 487
    • (1986) Biopolymer , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 45
    • 0026529046 scopus 로고
    • Redox-dependent changes in β-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide i infrared spectra
    • A. Dong, P. Huang, and W.S. Caughey Redox-dependent changes in β-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra Biochemistry 31 1992 182 189
    • (1992) Biochemistry , vol.31 , pp. 182-189
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 46
    • 0023656152 scopus 로고
    • Conformational properties of azurin in solution as determined from resolution-enhanced Fourier-transform infrared spectra
    • W.K. Surewicz, A.G. Szabo, and H.H. Mantsch Conformational properties of azurin in solution as determined from resolution-enhanced Fourier-transform infrared spectra European Journal of Biochemistry 167 1987 519 523
    • (1987) European Journal of Biochemistry , vol.167 , pp. 519-523
    • Surewicz, W.K.1    Szabo, A.G.2    Mantsch, H.H.3
  • 49
    • 33747758358 scopus 로고    scopus 로고
    • The secondary structure of pressure- and temperature-induced aggregates of equine serum albumin studied by FT-IR spectroscopy
    • A. Okuno, M. Kato, and Y. Taniguchi The secondary structure of pressure- and temperature-induced aggregates of equine serum albumin studied by FT-IR spectroscopy Biochimica et Biophysica Acta 1764 2006 1407 1412
    • (2006) Biochimica et Biophysica Acta , vol.1764 , pp. 1407-1412
    • Okuno, A.1    Kato, M.2    Taniguchi, Y.3
  • 50
    • 0035861633 scopus 로고    scopus 로고
    • High pressure refolding of recombinant human growth hormone from insoluble aggregates
    • R.J.S. John, J.F. Carpenter, C. Balny, and T.W. Randolph High pressure refolding of recombinant human growth hormone from insoluble aggregates Journal of Biological Chemistry 276 2001 46856 46863
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 46856-46863
    • John, R.J.S.1    Carpenter, J.F.2    Balny, C.3    Randolph, T.W.4


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