메뉴 건너뛰기




Volumn 117, Issue 4, 2013, Pages 1796-1803

Rapid and sensitive polarization measurement for characterizing protein adsorption at the solid-liquid interface

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION OF PROTEINS; BOVINE SERUM ALBUMIN ADSORPTION; ELECTRO-OPTIC MODULATORS; ELLIPSOMETERS; HYDROPHILIC SILICA; PHOTO-ELASTIC MODULATOR; POLARIZATION ANALYSIS; POLARIZATION MEASUREMENTS; PROTEIN ADSORPTION; SALINE SOLUTIONS; SOLID SURFACE; SOLID-LIQUID INTERFACES; STOKES VECTOR; TIME-SCALES;

EID: 84874421995     PISSN: 19327447     EISSN: 19327455     Source Type: Journal    
DOI: 10.1021/jp311573q     Document Type: Article
Times cited : (9)

References (66)
  • 1
    • 34250368096 scopus 로고    scopus 로고
    • Total internal reflection ellipsometry: Ultrahigh sensitivity for protein adsorption on metal surfaces
    • Poksinski, M.; Arwin, H. Total internal reflection ellipsometry: ultrahigh sensitivity for protein adsorption on metal surfaces Opt. Lett. 2007, 32, 1308-1310
    • (2007) Opt. Lett. , vol.32 , pp. 1308-1310
    • Poksinski, M.1    Arwin, H.2
  • 2
    • 0036161285 scopus 로고    scopus 로고
    • A Comparative Study of Protein Adsorption on Titanium Oxide Surfaces Using in situ Ellipsometry, Optical Wavefuide Lightmode Spectroscopy, and Quartz Crystal Microbalance/Dissipation
    • Hook, F.; Voros, J.; Rodahl, M.; Kurrat, R.; Boni, P.; Ramsden, J. J.; Textor, M.; Spencer, N. D.; Tengvall, P.; Gold, J.; Kasemo, B. A Comparative Study of Protein Adsorption on Titanium Oxide Surfaces Using in situ Ellipsometry, Optical Wavefuide Lightmode Spectroscopy, and Quartz Crystal Microbalance/Dissipation Colloid Surf. B 2002, 24, 155-170
    • (2002) Colloid Surf. B , vol.24 , pp. 155-170
    • Hook, F.1    Voros, J.2    Rodahl, M.3    Kurrat, R.4    Boni, P.5    Ramsden, J.J.6    Textor, M.7    Spencer, N.D.8    Tengvall, P.9    Gold, J.10    Kasemo, B.11
  • 3
    • 24644438699 scopus 로고    scopus 로고
    • Protein Adsorption on Solid-Liquid Interfaces Monitored by Laser Ellipsometry
    • Seitz, R.; Brings, R.; Geiger, R. Protein Adsorption on Solid-Liquid Interfaces Monitored by Laser Ellipsometry Appl. Surf. Sci. 2005, 252, 154-157
    • (2005) Appl. Surf. Sci. , vol.252 , pp. 154-157
    • Seitz, R.1    Brings, R.2    Geiger, R.3
  • 4
    • 16244402673 scopus 로고    scopus 로고
    • Reversible Protein Detection Method Based on Self-Assembled Monolayers Using Ellipsometry
    • Gill, K. J. S.; Isaacson, K.; Dew, S.; Kwok, D. Y. Reversible Protein Detection Method Based on Self-Assembled Monolayers Using Ellipsometry Int. Conf. MEMS, NANO, Smart Syst. 2004, 640-643
    • (2004) Int. Conf. MEMS, NANO, Smart Syst. , pp. 640-643
    • Gill, K.J.S.1    Isaacson, K.2    Dew, S.3    Kwok, D.Y.4
  • 5
    • 0032029432 scopus 로고    scopus 로고
    • Protein Absorption and Ellipsometry in Biomaterial Research
    • Elwig, H. Protein Absorption and Ellipsometry in Biomaterial Research Biomaterials 1998, 19, 397-406
    • (1998) Biomaterials , vol.19 , pp. 397-406
    • Elwig, H.1
  • 6
    • 17144451659 scopus 로고    scopus 로고
    • Protein Absorption and Ellipsometry in Biomaterial Research
    • Pokinski, M.; Arwin, H. Protein Absorption and Ellipsometry in Biomaterial Research Thin Solid Films 2004, 455-456, 716-721
    • (2004) Thin Solid Films , vol.455-456 , pp. 716-721
    • Pokinski, M.1    Arwin, H.2
  • 7
    • 1342332827 scopus 로고    scopus 로고
    • Biofouling and Antifouling
    • Fusetani, N. Biofouling and Antifouling Nat. Prod. Rep. 2004, 21, 94-104
    • (2004) Nat. Prod. Rep. , vol.21 , pp. 94-104
    • Fusetani, N.1
  • 9
    • 52649177044 scopus 로고    scopus 로고
    • Biofilm Formation, Bacterial Adhesion and Host Response on Polymeric Implants - Issues and Prevention
    • Pavritha, D.; Doble, M. Biofilm Formation, Bacterial Adhesion and Host Response on Polymeric Implants-Issues and Prevention Biomed. Mater. 2008, 3, 034003-034003 + 13
    • (2008) Biomed. Mater. , vol.3 , pp. 034003-03400313
    • Pavritha, D.1    Doble, M.2
  • 10
    • 35148893133 scopus 로고    scopus 로고
    • Haemocompatibility of Carbon-based Thin Films
    • Logothetidis, S. Haemocompatibility of Carbon-based Thin Films Diam. Relat. Mater. 2007, 16, 1847-1857
    • (2007) Diam. Relat. Mater. , vol.16 , pp. 1847-1857
    • Logothetidis, S.1
  • 11
    • 50649096995 scopus 로고    scopus 로고
    • In-situ and Real-time Protein Adsorption Study by Spectroscopic Ellipsometry
    • Lousinian, S.; Logothetidis, S. In-situ and Real-time Protein Adsorption Study by Spectroscopic Ellipsometry Thin Solid Films 2008, 516, 8002-8008
    • (2008) Thin Solid Films , vol.516 , pp. 8002-8008
    • Lousinian, S.1    Logothetidis, S.2
  • 12
    • 35549006803 scopus 로고    scopus 로고
    • The Haemocompatibility of Polyurethanehyaluronic Acid Copolymers
    • Xu, F.; Nacker, J. C.; Crone, W. C.; Masters, K. S. The Haemocompatibility of Polyurethanehyaluronic Acid Copolymers Biomaterials 2008, 29, 150-160
    • (2008) Biomaterials , vol.29 , pp. 150-160
    • Xu, F.1    Nacker, J.C.2    Crone, W.C.3    Masters, K.S.4
  • 14
    • 2942574395 scopus 로고    scopus 로고
    • Polymers in Sensor Applications
    • Adhikari, B.; Majumdar, S. Polymers in Sensor Applications Prog. Polym. Sci. 2004, 29, 699-766
    • (2004) Prog. Polym. Sci. , vol.29 , pp. 699-766
    • Adhikari, B.1    Majumdar, S.2
  • 15
    • 0037067114 scopus 로고    scopus 로고
    • Properties and Applications of Proteins Encapsulated Within Sol-gel Derived Materials
    • Jin, W.; Brennan, J. Properties and Applications of Proteins Encapsulated Within Sol-gel Derived Materials Anal. Chim. Acta 2002, 461, 1-36
    • (2002) Anal. Chim. Acta , vol.461 , pp. 1-36
    • Jin, W.1    Brennan, J.2
  • 17
    • 55549085564 scopus 로고    scopus 로고
    • Biocompatible Polymer Materials: Role of Protein-surface Interactions
    • Chena, H.; Yuana, L.; Song, W.; Wub, Z.; Lia, D. Biocompatible Polymer Materials: Role of Protein-surface Interactions Prog. Polym. Sci. 2008, 33, 1059-1087
    • (2008) Prog. Polym. Sci. , vol.33 , pp. 1059-1087
    • Chena, H.1    Yuana, L.2    Song, W.3    Wub, Z.4    Lia, D.5
  • 18
    • 75349094390 scopus 로고    scopus 로고
    • Molecular Simulation of Adsorption and Its Implications to Protein Chromatography: A Review
    • Zhang, L.; Sun, Y. Molecular Simulation of Adsorption and Its Implications to Protein Chromatography: A Review Biochem. Eng. J. 2010, 48, 408-415
    • (2010) Biochem. Eng. J. , vol.48 , pp. 408-415
    • Zhang, L.1    Sun, Y.2
  • 19
    • 48249085431 scopus 로고    scopus 로고
    • Advances in Polymers for Anti-biofouling Surfaces
    • Krishnan, S.; Weinman, C. J.; Ober, C. K. Advances in Polymers for Anti-biofouling Surfaces J. Mater. Chem. 2008, 18, 3405-3413
    • (2008) J. Mater. Chem. , vol.18 , pp. 3405-3413
    • Krishnan, S.1    Weinman, C.J.2    Ober, C.K.3
  • 20
    • 0029724374 scopus 로고    scopus 로고
    • Surface Treatments of Polymers for Biocompatibility
    • Elbert, D. L.; Hubbell, J. A. Surface Treatments of Polymers for Biocompatibility Annu. Rev. Mater. Sci. 1996, 26, 365-394
    • (1996) Annu. Rev. Mater. Sci. , vol.26 , pp. 365-394
    • Elbert, D.L.1    Hubbell, J.A.2
  • 23
    • 3943096547 scopus 로고    scopus 로고
    • Correlation of pH-dependent Surface Interaction Forces to Amino Acid Adsoprtion: Implications for the Origin of Life
    • Churchill, H.; Teng, H.; Hazen, R. M. Correlation of pH-dependent Surface Interaction Forces to Amino Acid Adsoprtion: Implications for the Origin of Life Am. Mineral. 2004, 89, 1048-1055
    • (2004) Am. Mineral. , vol.89 , pp. 1048-1055
    • Churchill, H.1    Teng, H.2    Hazen, R.M.3
  • 24
    • 4444220254 scopus 로고    scopus 로고
    • Effects of Temperate and pH on the Helicity of a Peptide Adsorbed to Colloidal Silica
    • Read, M. J.; Mayes, A. M.; Burkett, S. L. Effects of Temperate and pH on the Helicity of a Peptide Adsorbed to Colloidal Silica Colloid Surf. B: Biointerfaces 2004, 37, 113-127
    • (2004) Colloid Surf. B: Biointerfaces , vol.37 , pp. 113-127
    • Read, M.J.1    Mayes, A.M.2    Burkett, S.L.3
  • 25
    • 0001107373 scopus 로고
    • Structural Changes in Proteins Adsorbed on Polymer Surfaces
    • Soderquist, M. E.; Walton, A. G. Structural Changes in Proteins Adsorbed on Polymer Surfaces J. Colloid Interface Sci. 1980, 75, 386-396
    • (1980) J. Colloid Interface Sci. , vol.75 , pp. 386-396
    • Soderquist, M.E.1    Walton, A.G.2
  • 26
    • 54249148490 scopus 로고    scopus 로고
    • Rapid Impedance Scanning QCM for Electrochemical Applications Based on Miniaturized Hardware and Highperformance Curve Fitting
    • Wudy, F.; Multerer, M.; Stock, C.; Schmeer, G.; Gores, H. J. Rapid Impedance Scanning QCM for Electrochemical Applications Based on Miniaturized Hardware and Highperformance Curve Fitting Electrochim. Acta 2008, 53, 6568-6574
    • (2008) Electrochim. Acta , vol.53 , pp. 6568-6574
    • Wudy, F.1    Multerer, M.2    Stock, C.3    Schmeer, G.4    Gores, H.J.5
  • 27
    • 67649884483 scopus 로고    scopus 로고
    • Application of Kevin-Voigt Model in Quantifying Whey Protein Adsorption on Polyethersulfone Using QCM-D
    • Liu, S.; Kim, J. Application of Kevin-Voigt Model in Quantifying Whey Protein Adsorption on Polyethersulfone Using QCM-D J. Lab. Auto. 2009, Aug, 213
    • (2009) J. Lab. Auto. , pp. 213
    • Liu, S.1    Kim, J.2
  • 28
    • 66249100899 scopus 로고    scopus 로고
    • Fibrinogen Adsorption and Conformational Change on Model Polymers: Novel Aspects of Mutual Molecular Rearrangement
    • Berglin, M.; Pinori, E.; Sellborn, A.; Andersson, M.; Hulander, M.; Elwing, H. Fibrinogen Adsorption and Conformational Change on Model Polymers: Novel Aspects of Mutual Molecular Rearrangement Langmuir 2009, 25, 5602
    • (2009) Langmuir , vol.25 , pp. 5602
    • Berglin, M.1    Pinori, E.2    Sellborn, A.3    Andersson, M.4    Hulander, M.5    Elwing, H.6
  • 29
    • 69949129406 scopus 로고    scopus 로고
    • Controlling Tyrosinase Activity on Charged Polyelectrolyte Surfaces: A QCM-D Analysis
    • Gormally, M.; McKibben, R.; Johal, M.; Selassie, C. Controlling Tyrosinase Activity on Charged Polyelectrolyte Surfaces: A QCM-D Analysis Langmuir 2009, 25, 10014
    • (2009) Langmuir , vol.25 , pp. 10014
    • Gormally, M.1    McKibben, R.2    Johal, M.3    Selassie, C.4
  • 30
    • 0031106750 scopus 로고    scopus 로고
    • Surface Plasmon Resonance for Real Time in situ Analysis of Protein Adsorption to Polymer Surfaces
    • Green, R. J.; Davies, J.; Davies, M. C.; Roberts, C. J.; Tendler, S. J. B. Surface Plasmon Resonance for Real Time in situ Analysis of Protein Adsorption to Polymer Surfaces Biomaterials 1997, 18, 405-413
    • (1997) Biomaterials , vol.18 , pp. 405-413
    • Green, R.J.1    Davies, J.2    Davies, M.C.3    Roberts, C.J.4    Tendler, S.J.B.5
  • 31
    • 10344222181 scopus 로고    scopus 로고
    • Nanosensors Based on Responsive Polymer Brushes and Gold Nanoparticle Enhanced Transmission Surface Plasmon Resonance Spectroscopy
    • Tokareva, I.; Minko, S.; Fendler, J. H.; Hutter, E. Nanosensors Based on Responsive Polymer Brushes and Gold Nanoparticle Enhanced Transmission Surface Plasmon Resonance Spectroscopy J. Am. Chem. Soc. 2004, 126, 15950-15951
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15950-15951
    • Tokareva, I.1    Minko, S.2    Fendler, J.H.3    Hutter, E.4
  • 32
    • 84865682919 scopus 로고    scopus 로고
    • A Novel Polymerization of Ultrathin Sensitive Imprinted Film on Surface Plasmon Resonance Sensor
    • Dong, J.; Peng, Y.; Gao, N.; Bai, J.; Ning, B.; Liu, M.; Gao, Z. A Novel Polymerization of Ultrathin Sensitive Imprinted Film on Surface Plasmon Resonance Sensor Analyst 2012, 137, 4571-4576
    • (2012) Analyst , vol.137 , pp. 4571-4576
    • Dong, J.1    Peng, Y.2    Gao, N.3    Bai, J.4    Ning, B.5    Liu, M.6    Gao, Z.7
  • 35
    • 33749619528 scopus 로고    scopus 로고
    • Another Century of Ellipsometry
    • Schubert, M. Another Century of Ellipsometry Ann. Phys 2006, 15, 480-497
    • (2006) Ann. Phys , vol.15 , pp. 480-497
    • Schubert, M.1
  • 36
    • 40149084492 scopus 로고    scopus 로고
    • The measurement of the Stokes parameters: A Generalized Methodology Using a Dual PhotoelasticModulator System
    • Guan, W.; Jones, G. A.; Liu, Y. W.; Shen, T. H. The measurement of the Stokes parameters: A Generalized Methodology Using a Dual PhotoelasticModulator System J. Appl. Phys. 2008, 103, 043104
    • (2008) J. Appl. Phys. , vol.103 , pp. 043104
    • Guan, W.1    Jones, G.A.2    Liu, Y.W.3    Shen, T.H.4
  • 37
    • 0038380662 scopus 로고    scopus 로고
    • Modulation, Alignment, and Calibration Methods for Phasemodulated Optical Polarimeters
    • Mackey, J. R.; Salari, E.; Tin, P. Modulation, Alignment, and Calibration Methods for Phasemodulated Optical Polarimeters Opt. Eng. 2003, 42, 1460-1466
    • (2003) Opt. Eng. , vol.42 , pp. 1460-1466
    • MacKey, J.R.1    Salari, E.2    Tin, P.3
  • 38
    • 33749316435 scopus 로고    scopus 로고
    • Generalized Theory and Application of Stokes Parameter Measurements Made with a Single Photoelastic Modulator
    • Liu, Y. W.; Jones, G. A.; Peng, Y.; Shen, T. H. Generalized Theory and Application of Stokes Parameter Measurements Made with a Single Photoelastic Modulator J. Appl. Phys. 2006, 100, 063537
    • (2006) J. Appl. Phys. , vol.100 , pp. 063537
    • Liu, Y.W.1    Jones, G.A.2    Peng, Y.3    Shen, T.H.4
  • 39
    • 28044470968 scopus 로고    scopus 로고
    • Accurate Polarization Measurements with a Dual Photoelastic Modulator
    • Kuldkepp, M.; Hawkes, N. C.; Rachlew, E.; Schunke, B. Accurate Polarization Measurements with a Dual Photoelastic Modulator Appl. Opt. 2005, 44, 5899-5904
    • (2005) Appl. Opt. , vol.44 , pp. 5899-5904
    • Kuldkepp, M.1    Hawkes, N.C.2    Rachlew, E.3    Schunke, B.4
  • 40
    • 84864193797 scopus 로고    scopus 로고
    • Dual-modulator Broadband Infrared Mueller Matrix Ellipsometry
    • Cross, L. J. K.; Hore, D. K. Dual-modulator Broadband Infrared Mueller Matrix Ellipsometry Appl. Opt. 2012, 51, 5100-5110
    • (2012) Appl. Opt. , vol.51 , pp. 5100-5110
    • Cross, L.J.K.1    Hore, D.K.2
  • 41
    • 0030026989 scopus 로고    scopus 로고
    • Protein Adsorption on Solid Surfaces
    • Hlady, V.; Buijs, J. Protein Adsorption on Solid Surfaces Curr. Opin. Biotechnol. 1996, 7, 72-77
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 72-77
    • Hlady, V.1    Buijs, J.2
  • 42
    • 79955883878 scopus 로고    scopus 로고
    • The Effect of Salt on the Water Structure at a Charged Solid Surface: Differentiating Second- and Third-order Nonlinear Contributions
    • Jena, K. C.; Covert, P. A.; Hore, D. K. The Effect of Salt on the Water Structure at a Charged Solid Surface: Differentiating Second- and Third-order Nonlinear Contributions J. Phys. Chem. Lett. 2011, 2, 1056-1061
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 1056-1061
    • Jena, K.C.1    Covert, P.A.2    Hore, D.K.3
  • 44
    • 0031345518 scopus 로고    scopus 로고
    • L-BFGS-B: Algorithm 778: L-BFGS-B, FORTRAN Routines for Large Scale Bound Constrained Optimization
    • Zhu, C.; Byrd, R.; Nocedal, J. L-BFGS-B: Algorithm 778: L-BFGS-B, FORTRAN Routines for Large Scale Bound Constrained Optimization ACM Trans. Math. Software 1997, 23, 550-560
    • (1997) ACM Trans. Math. Software , vol.23 , pp. 550-560
    • Zhu, C.1    Byrd, R.2    Nocedal, J.3
  • 45
    • 0000732463 scopus 로고
    • A Limited Memory Algorithm for Bound Constrained Optimization
    • Byrd, R.; Lu, P.; Nocedal, J. A Limited Memory Algorithm for Bound Constrained Optimization SIAM J. Sci. Stat. Comp. 1995, 16, 1190-1208
    • (1995) SIAM J. Sci. Stat. Comp. , vol.16 , pp. 1190-1208
    • Byrd, R.1    Lu, P.2    Nocedal, J.3
  • 46
    • 79960380131 scopus 로고    scopus 로고
    • The Refractive Index of Human Hemoglobin in the Visible Range
    • Zhernovaya, O.; Sydoruk, O.; Tuchin, V.; Douplik, A. The Refractive Index of Human Hemoglobin in the Visible Range Phys. Med. Biol. 2011, 56, 4013-4021
    • (2011) Phys. Med. Biol. , vol.56 , pp. 4013-4021
    • Zhernovaya, O.1    Sydoruk, O.2    Tuchin, V.3    Douplik, A.4
  • 47
    • 0000416414 scopus 로고
    • Interspecimen Comparison of the Refractive Index of Fused Silica
    • Malitson, I. H. Interspecimen Comparison of the Refractive Index of Fused Silica J. Opt. Soc. Am. 1965, 55, 1205-1209
    • (1965) J. Opt. Soc. Am. , vol.55 , pp. 1205-1209
    • Malitson, I.H.1
  • 48
    • 0001123248 scopus 로고    scopus 로고
    • Refractive Index and Thickness Sensitivity in Surface Plasmon Resonance Spectroscopy
    • Akimoto, T.; Sasaki, S.; Ikebukuro, K.; Karube, I. Refractive Index and Thickness Sensitivity in Surface Plasmon Resonance Spectroscopy Appl. Opt. 1999, 38, 4058-4064
    • (1999) Appl. Opt. , vol.38 , pp. 4058-4064
    • Akimoto, T.1    Sasaki, S.2    Ikebukuro, K.3    Karube, I.4
  • 49
    • 33749587631 scopus 로고    scopus 로고
    • Refractive Index Measurement for Biomaterial Samples by Total Internal Reflection
    • Jin, Y. L.; Chen, J. Y.; Xu, L.; Wang, P. N. Refractive Index Measurement for Biomaterial Samples by Total Internal Reflection Phys. Med. Biol. 2006, 51, N371-N379
    • (2006) Phys. Med. Biol. , vol.51
    • Jin, Y.L.1    Chen, J.Y.2    Xu, L.3    Wang, P.N.4
  • 50
    • 48349102155 scopus 로고    scopus 로고
    • An Enhanced Optical Multimode Fiber Sensor Based on Surface Plasmon ResonanceWith Cascaded Structure
    • Lin, Y.-C.; Tsai, W.-H.; Tsao, Y.-C.; Tai, J.-K. An Enhanced Optical Multimode Fiber Sensor Based on Surface Plasmon ResonanceWith Cascaded Structure IEEE Photonics Techol. Lett 2008, 20, 1287-1289
    • (2008) IEEE Photonics Techol. Lett , vol.20 , pp. 1287-1289
    • Lin, Y.-C.1    Tsai, W.-H.2    Tsao, Y.-C.3    Tai, J.-K.4
  • 51
    • 4644274073 scopus 로고    scopus 로고
    • Determination of the Refractive Index Increment (dn/dc) of Molecule and Macromolecule Solutions by Surface Plasmon Resonance
    • Tumolo, T.; Angnes, L.; Baptista, M. S. Determination of the Refractive Index Increment (dn/dc) of Molecule and Macromolecule Solutions by Surface Plasmon Resonance Anal. Biochem. 2004, 333, 273-279
    • (2004) Anal. Biochem. , vol.333 , pp. 273-279
    • Tumolo, T.1    Angnes, L.2    Baptista, M.S.3
  • 52
    • 67649958586 scopus 로고    scopus 로고
    • Nonlinear Optical Stokes Ellipsometry. 1. Theoretical Framework
    • Begue, N. J.; Moad, A. J.; Simpson, G. J. Nonlinear Optical Stokes Ellipsometry. 1. Theoretical Framework J. Phys. Chem. C 2009, 113, 10158-10165
    • (2009) J. Phys. Chem. C , vol.113 , pp. 10158-10165
    • Begue, N.J.1    Moad, A.J.2    Simpson, G.J.3
  • 53
    • 67649989722 scopus 로고    scopus 로고
    • Nonlinear Optical Stokes Ellipsometry. 2. Experimental Demonstration
    • Begue, N. J.; Everly, R. M.; Hall, V. J.; Haupert, L.; Simpson, G. J. Nonlinear Optical Stokes Ellipsometry. 2. Experimental Demonstration J. Phys. Chem. C 2009, 113, 10166-10175
    • (2009) J. Phys. Chem. C , vol.113 , pp. 10166-10175
    • Begue, N.J.1    Everly, R.M.2    Hall, V.J.3    Haupert, L.4    Simpson, G.J.5
  • 54
    • 1842841004 scopus 로고    scopus 로고
    • Ellipsometric Approach for the Real-time Detection of Label-free Protein Adsorption by Second Harmonic Generation
    • Polizzi, M. A.; Plocinik, R. M.; Simpson, G. J. Ellipsometric Approach for the Real-time Detection of Label-free Protein Adsorption by Second Harmonic Generation J. Am. Chem. Soc. 2004, 126, 5001-5007
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5001-5007
    • Polizzi, M.A.1    Plocinik, R.M.2    Simpson, G.J.3
  • 55
    • 0035862293 scopus 로고    scopus 로고
    • The Adsorption-Desorption Cycle. Reversibility of the BSA- Silica System
    • Giacomelli, C. E.; Norde, W. The Adsorption-Desorption Cycle. Reversibility of the BSA- Silica System J. Colloid Interface Sci. 2001, 233, 234-240
    • (2001) J. Colloid Interface Sci. , vol.233 , pp. 234-240
    • Giacomelli, C.E.1    Norde, W.2
  • 56
    • 3342905386 scopus 로고    scopus 로고
    • Time-resolved EvanescentWave-induced Fluorescence Anisotropy for the Determination of Molecular Conformational Changes of Proteins at an Interface
    • Gee, M. L.; Lensun, L.; Smith, T. A.; Scholes, C. A. Time-resolved EvanescentWave-induced Fluorescence Anisotropy for the Determination of Molecular Conformational Changes of Proteins at an Interface Eur. Biophys. J. 2004, 33, 130-139
    • (2004) Eur. Biophys. J. , vol.33 , pp. 130-139
    • Gee, M.L.1    Lensun, L.2    Smith, T.A.3    Scholes, C.A.4
  • 57
    • 13444251301 scopus 로고    scopus 로고
    • Lysozyme and Bovine Serum Albumin Adsorption on Uncoated Silica and AlOOH-coated Silica Particles: The Influence of Positively and Negatively Charged Oxide Surface Coatings
    • Rezwan, K.; Meier, L. P.; Gauckler, L. J. Lysozyme and Bovine Serum Albumin Adsorption on Uncoated Silica and AlOOH-coated Silica Particles: the Influence of Positively and Negatively Charged Oxide Surface Coatings Biomaterals 2005, 26, 4351-4357
    • (2005) Biomaterals , vol.26 , pp. 4351-4357
    • Rezwan, K.1    Meier, L.P.2    Gauckler, L.J.3
  • 58
    • 0025597864 scopus 로고
    • Amount and Surface Structure of Albumin Adsorbed to Solid Substrata with Different Wettabilities in a Parallel Plate Flow Cell
    • Uyen, H. M. W.; Schakenraad, J. M.; Sjollema, J.; Noordmans, J.; Jongebloed, W. L.; Stokroos, I.; Busscher, H. J. Amount and Surface Structure of Albumin Adsorbed to Solid Substrata with Different Wettabilities in a Parallel Plate Flow Cell J. Biomed. Res. 1990, 24, 1599-1614
    • (1990) J. Biomed. Res. , vol.24 , pp. 1599-1614
    • Uyen, H.M.W.1    Schakenraad, J.M.2    Sjollema, J.3    Noordmans, J.4    Jongebloed, W.L.5    Stokroos, I.6    Busscher, H.J.7
  • 59
    • 84947146127 scopus 로고
    • Analogies in the Two-dimensional Spatial Arrangement of Adsorbed Proteins and Adhering Bacteria: Bovine Serum Albumin and Streptococcus Sanguis 12
    • Busscher, H. J.; van der Mei, H. C.; Schakenraad, J. M. Analogies in the Two-dimensional Spatial Arrangement of Adsorbed Proteins and Adhering Bacteria: Bovine Serum Albumin and Streptococcus Sanguis 12 J. Biomater. Sci., Polym. Ed. 1991, 3, 85-94
    • (1991) J. Biomater. Sci., Polym. Ed. , vol.3 , pp. 85-94
    • Busscher, H.J.1    Van Der Mei, H.C.2    Schakenraad, J.M.3
  • 61
    • 1542349573 scopus 로고
    • Addision-Wesley: Reading, MA
    • Hecht, E.; Zajac, A. Optics; Addision-Wesley: Reading, MA, 1979.
    • (1979) Optics
    • Hecht, E.1    Zajac, A.2
  • 63
    • 0000025283 scopus 로고
    • Preparation and Properties of Serum and Plasma Proteins. XII. The Refractive Properties of the Proteins of Human Plasma and Certain Purified Fractions
    • Armstrong, S. H.; Budka, M. J. E.; Morrison, K. C.; Hasson, M. Preparation and Properties of Serum and Plasma Proteins. XII. The Refractive Properties of the Proteins of Human Plasma and Certain Purified Fractions J. Am. Chem. Soc. 1947, 69, 1747-1753
    • (1947) J. Am. Chem. Soc. , vol.69 , pp. 1747-1753
    • Armstrong, S.H.1    Budka, M.J.E.2    Morrison, K.C.3    Hasson, M.4
  • 64
    • 0343201955 scopus 로고
    • The Thickness of Hemoglobin and Bovine Serum Albumin Molecules as Unimolecular Layers Adsorbed onto Films of Barium Stearate
    • Fisk, A. A. The Thickness of Hemoglobin and Bovine Serum Albumin Molecules as Unimolecular Layers Adsorbed onto Films of Barium Stearate Proc. Natl. Acad. Sci. U.S.A. 1950, 36, 518-523
    • (1950) Proc. Natl. Acad. Sci. U.S.A. , vol.36 , pp. 518-523
    • Fisk, A.A.1
  • 65
    • 79961162004 scopus 로고    scopus 로고
    • Measurement of the Thickness of Ultra-thin Adsorbed Globular Protein Layers with Dual-polarisation Interferometry: A Comparison with Neutron Reflectivity
    • Cowsill, B. J.; Coffey, P. D.; Yaseen, M.; Waigh, T. A.; Freeman, N. J.; Lu, J. R. Measurement of the Thickness of Ultra-thin Adsorbed Globular Protein Layers with Dual-polarisation Interferometry: A Comparison with Neutron Reflectivity Soft Matter 2011, 7, 7223-7230
    • (2011) Soft Matter , vol.7 , pp. 7223-7230
    • Cowsill, B.J.1    Coffey, P.D.2    Yaseen, M.3    Waigh, T.A.4    Freeman, N.J.5    Lu, J.R.6
  • 66
    • 0032122890 scopus 로고    scopus 로고
    • Molecular Packing of HSA, IgG, and Fibrinogen Adsorbed on Silicon by AFM Imaging
    • Ortega-Vinuesa, J. L.; Tengvall, P.; Lundström, I. Molecular Packing of HSA, IgG, and Fibrinogen Adsorbed on Silicon by AFM Imaging Thin Solid Films 1998, 324, 257-273
    • (1998) Thin Solid Films , vol.324 , pp. 257-273
    • Ortega-Vinuesa, J.L.1    Tengvall, P.2    Lundström, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.