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Volumn 7, Issue 1, 1996, Pages 72-77

Protein adsorption on solid surfaces

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0030026989     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(96)80098-X     Document Type: Article
Times cited : (451)

References (67)
  • 1
    • 0003413579 scopus 로고
    • Washington, DC: American Chemical Society
    • Horbett TA, Braah JL (Eds): Proteins at Interfaces II: Fundamentals and Applications. Washington, DC: American Chemical Society; 1995. A collection of papers presented at the American Chemical Society Symposium 'Proteins at Interfaces' held in San Diego, April 1994. The book provides a cross-section of the whole field, including modern experimental methods, competitive adsorption from multiprotein systems, protein conformational changes and surface chemistry effects on protein adsorption.
    • (1995) Proteins at Interfaces II: Fundamentals and Applications
    • Horbett, T.A.1    Braah, J.L.2
  • 2
    • 33746200227 scopus 로고
    • Globular proteins at solid/liquid interfaces
    • Haynes CA, Norde W: Globular proteins at solid/liquid interfaces. Colloids Surfaces [B] 1994, 2:517-566. A comprehensive overview on the driving forces involved in protein adsorption. The basic physical processes determining the conformation of a protein and its interaction with interfaces are evaluated using a thermodynamic approach.
    • (1994) Colloids Surfaces [B] , vol.2 , pp. 517-566
    • Haynes, C.A.1    Norde, W.2
  • 3
    • 0642307922 scopus 로고
    • Puzzles and paradoxes in protein adsorption
    • Ramsden JJ: Puzzles and paradoxes in protein adsorption. Chem Soc Rev 1995, 24:73-78.
    • (1995) Chem Soc Rev , vol.24 , pp. 73-78
    • Ramsden, J.J.1
  • 4
    • 85030195649 scopus 로고
    • Garden City, New York: The Natural History Press
    • Woman L: Blood, Garden City, New York: The Natural History Press; 1968.
    • (1968) Blood
    • Woman, L.1
  • 5
    • 0642354856 scopus 로고
    • London: Current Biology Ltd
    • Hendrickson WA, Wüthrich K (Eds): Macromolecular Structures 1994. London: Current Biology Ltd; 1994. An annually published catalog of solved protein structures. Although somewhat expensive, the series is a valuable resource for any laboratory that is seriously involved in protein work. Other annual catalogs in this series are available from 1991.
    • (1994) Macromolecular Structures 1994
    • Hendrickson, W.A.1    Wüthrich, K.2
  • 6
    • 0028929556 scopus 로고
    • Principles of protein folding - A perspective from simple exact models
    • Dill KA, Bromberg S, Yue K, Fiebig KM, Yee DP, Thomas PD, Chan HS: Principles of protein folding - a perspective from simple exact models. Protein Sci 1995, 4:561-602. Outlines general principles of protein structure, stability and folding kinetics from the perspective of simple exact lattice models. Excellent reading for anyone working with proteins. These simple models represent protein molecules at a very rudimentary level; yet, they permit complete exploration of conformational and sequence space. It is quite possible that the same models can be used to predict interfacial protein stability.
    • (1995) Protein Sci , vol.4 , pp. 561-602
    • Dill, K.A.1    Bromberg, S.2    Yue, K.3    Fiebig, K.M.4    Yee, D.P.5    Thomas, P.D.6    Chan, H.S.7
  • 7
    • 0028364295 scopus 로고
    • Blomolecular Imaging with the atomic force microscope
    • Hansma HG, Hoh JH: Blomolecular Imaging with the atomic force microscope. Annu Rev Biophys Biomol Struct 1994, 23:115-139.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 115-139
    • Hansma, H.G.1    Hoh, J.H.2
  • 8
    • 0029277090 scopus 로고
    • Engineering surfaces
    • Ulman A: Engineering surfaces. Chemtech 1995:22-28.
    • (1995) Chemtech , pp. 22-28
    • Ulman, A.1
  • 9
    • 0028933179 scopus 로고
    • Neutron reflection study of bovine β-casein adsorbed on OTS self-assembled monolayers
    • Fragneto G, Thomas RK, Rennie AR, Penfold J: Neutron reflection study of bovine β-casein adsorbed on OTS self-assembled monolayers. Science 1995, 267:657-660. Neutron reflectivity enables the study of the thickness and chemical composition of the interface layers formed by the adsorption of β-casein on OTS self-assembled monolayers. Both the self-assembled monolayer and the adsorbed protein layer were divided into two layers of unequal densities as a result of adsorption.
    • (1995) Science , vol.267 , pp. 657-660
    • Fragneto, G.1    Thomas, R.K.2    Rennie, A.R.3    Penfold, J.4
  • 10
    • 0000311426 scopus 로고
    • Wetting and protein adsorption of self-assembled monolayers of alkanetholates supported on transparent films of gold
    • DiMilla PA, Folkers JP, Biebuyck HA, Härter R, Lopez GP, Whitesides GM: Wetting and protein adsorption of self-assembled monolayers of alkanetholates supported on transparent films of gold. J Am Chem Soc 1994, 116:2225-2226.
    • (1994) J am Chem Soc , vol.116 , pp. 2225-2226
    • Dimilla, P.A.1    Folkers, J.P.2    Biebuyck, H.A.3    Härter, R.4    Lopez, G.P.5    Whitesides, G.M.6
  • 12
    • 0028448697 scopus 로고
    • Human serum albumin adsorption onto octadeyidimethylsilyl-silica gradient surface
    • Lin Y-S, Hlady V: Human serum albumin adsorption onto octadeyidimethylsilyl-silica gradient surface. Colloids Surfaces [B] 1994, 2:481-491.
    • (1994) Colloids Surfaces [B] , vol.2 , pp. 481-491
    • Lin, Y.-S.1    Hlady, V.2
  • 13
    • 0003081479 scopus 로고
    • Adsorption of human low density lipoprotein onto a silica-octadecvWImethylsllyl (C18) gradient surface
    • Edited by Horbett TA, Brash JL. Washington, DC: American Chemical Society
    • Ho C-H, Hlady V: Adsorption of human low density lipoprotein onto a silica-octadecvWImethylsllyl (C18) gradient surface. In Proteins at Interfaces II; Fundamentals and Applications. Edited by Horbett TA, Brash JL. Washington, DC: American Chemical Society; 1995:371-384. The kinetics of the binding of human low-density lipoprotein to a partially covered C18-silica surface are simply predicted by the sum of two adsorption kinetics, one occurring on silica sites and the other on C18 sites. The two contributions have to be weighted according to the average fractional surface density of the two sites.
    • (1995) Proteins at Interfaces II; Fundamentals and Applications , pp. 371-384
    • Ho, C.-H.1    Hlady, V.2
  • 14
    • 0029639161 scopus 로고
    • The desorption of ribonuclease a from charge density gradient surfaces studied by spatially-resolved total Internal reflection fluorescence
    • Lin Y-S, Hlady V: The desorption of ribonuclease A from charge density gradient surfaces studied by spatially-resolved total Internal reflection fluorescence. Colloids Surfaces [B] 1995, 4:65-75.
    • (1995) Colloids Surfaces [B] , vol.4 , pp. 65-75
    • Lin, Y.-S.1    Hlady, V.2
  • 15
    • 0028508051 scopus 로고
    • The surface density of poly(ethyleneoxide): Preparation, characterization and protein adsorption
    • Lin YS, Hlady V, Gölander C-G: The surface density of poly(ethyleneoxide): preparation, characterization and protein adsorption. Colloids Surfaces [B] 1994, 3:49-62.
    • (1994) Colloids Surfaces [B] , vol.3 , pp. 49-62
    • Lin, Y.S.1    Hlady, V.2    Gölander, C.-G.3
  • 16
    • 0027933482 scopus 로고
    • Influence of surface and protein modification on immunoglobulin G adsorption observed by scanning force microscopy
    • Droz E, Taborelli M, Descouts P, Wells TNC: Influence of surface and protein modification on immunoglobulin G adsorption observed by scanning force microscopy. Biophys J 1994, 67:1316-1323.
    • (1994) Biophys J , vol.67 , pp. 1316-1323
    • Droz, E.1    Taborelli, M.2    Descouts, P.3    Wells, T.N.C.4
  • 17
    • 0030224813 scopus 로고    scopus 로고
    • Human low density lipoprotein and human serum albumin adsorption onto model surfaces studied by total internal reflection fluorescence and scanning force microscopy
    • in press
    • Ho C-H, Britt DW, Hlady V: Human low density lipoprotein and human serum albumin adsorption onto model surfaces studied by total internal reflection fluorescence and scanning force microscopy. J Mol Recognit 1996, in press.
    • (1996) J Mol Recognit
    • Ho, C.-H.1    Britt, D.W.2    Hlady, V.3
  • 18
    • 0029249344 scopus 로고
    • A scanning force microscopy study of human serum albumin and porcine pancreas trypsln adsorption on mica surfaces
    • Quist AP, Bjorck LP, Reimann CT, Oscarsson SO, Sundqvist BUR: A scanning force microscopy study of human serum albumin and porcine pancreas trypsln adsorption on mica surfaces. Surface Sci 1995, 325:L406-L412.
    • (1995) Surface Sci , vol.325
    • Quist, A.P.1    Bjorck, L.P.2    Reimann, C.T.3    Oscarsson, S.O.4    Sundqvist, B.U.R.5
  • 19
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic force microscope
    • Radmacher M, Fritz M, Hanema HG, Hansma PK: Direct observation of enzyme activity with the atomic force microscope. Science 1994, 265:1577-1579. These authors use the tapping' mode of AFM to monitor a fluctuation in the thickness of adsorbed lysozyme. Short (50 ms) fluctuations, with an apparent 1 nm change in the dimensions of lysozyme, are related to enzymatic activity.
    • (1994) Science , vol.265 , pp. 1577-1579
    • Radmacher, M.1    Fritz, M.2    Hanema, H.G.3    Hansma, P.K.4
  • 20
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin E-L, Moy VT, Gaub HE: Adhesion forces between individual ligand-receptor pairs. Science 1994, 264:415-417. This represents a significant advance in the measurement of weak specific receptor-ligand (un)binding forces, opening the possibility of using AFM as a proximity sensor. The immobilization of biotin ligands by non-specific physical adsorption of biotinylated albumin will have to be improved for any future use of the technique.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 21
    • 0001493611 scopus 로고
    • Effects of discrete protein surface interactions in scanning force microscopy adhesion force measurements
    • Stuart JK, Hlady V: Effects of discrete protein surface interactions in scanning force microscopy adhesion force measurements. Langmuir 1995, 11:1368-1374.
    • (1995) Langmuir , vol.11 , pp. 1368-1374
    • Stuart, J.K.1    Hlady, V.2
  • 23
    • 0029647053 scopus 로고
    • The surface force apparatus - A tool for probing molecular protein Interactions
    • Leckband D: The surface force apparatus - a tool for probing molecular protein Interactions. Nature 1995, 376:617-618. The surface force apparatus offers the possibility of directly monitoring intermolecular forces. This system is applied to monitor the receptor-ligand forces in the biotin-streptavidin interaction. Forces with a resolution of 10 nN can be measured as function of distance with a resolution of 0.1 nm.
    • (1995) Nature , vol.376 , pp. 617-618
    • Leckband, D.1
  • 24
    • 0342979915 scopus 로고
    • Neutron reflectivity of adsorbed β-casein and β-lactoglobulin at the air/water Interface
    • Atkinson PJ, Dickinson E, Home DS, Richardson RM: Neutron reflectivity of adsorbed β-casein and β-lactoglobulin at the air/water Interface. J Chem SQC Faraday Trans 1995, 91:2847-2854.
    • (1995) J Chem SQC Faraday Trans , vol.91 , pp. 2847-2854
    • Atkinson, P.J.1    Dickinson, E.2    Home, D.S.3    Richardson, R.M.4
  • 25
    • 0000731735 scopus 로고
    • Temperature dependence of activity and conformational changes in a-amylases with different thermostability upon adsorption on ultrafine silica particles
    • Kondo A, Urabe T: Temperature dependence of activity and conformational changes in a-amylases with different thermostability upon adsorption on ultrafine silica particles. J Colloid Interface Sci 1995, 174:191-198. The mechanism of thermal deactivation of α-amylases is quantitatively studied by monitoring the enzymatic activity and the amount of α-helix using CD. The α-amylases are studied in solution and adsorbed onto two kinds of silica particles that differ in surface hydrophobicity. It is clearly shown that α-amylase shows a decreased activity with increasing temperature, increasing surface hydrophobicity, decreasing surface coverage, and decreasing thermal stability. It should be noted that, in some cases, a reduction in enzymatic activity is found when the α-helix content seems unaltered.
    • (1995) J Colloid Interface Sci , vol.174 , pp. 191-198
    • Kondo, A.1    Urabe, T.2
  • 26
    • 0002091980 scopus 로고
    • Structural changes of T4 lysozyme upon adsorption to silica nanoparticles measured by circular dlchroism
    • Billsten P, Wahlgren M, Arnebrant T, McGuire J, Elwing H: Structural changes of T4 lysozyme upon adsorption to silica nanoparticles measured by circular dlchroism. J Colloid Interface Sci 1995, 175:77-82.
    • (1995) J Colloid Interface Sci , vol.175 , pp. 77-82
    • Billsten, P.1    Wahlgren, M.2    Arnebrant, T.3    McGuire, J.4    Elwing, H.5
  • 27
    • 0028449450 scopus 로고
    • A fluorescence technique for Investigating protein adsorption phenomena at a colloidal silica surface
    • Clark SR, Billsten P, Elwing H: A fluorescence technique for Investigating protein adsorption phenomena at a colloidal silica surface. Colloids Surfaces [B] 1994, 2:457-461.
    • (1994) Colloids Surfaces [B] , vol.2 , pp. 457-461
    • Clark, S.R.1    Billsten, P.2    Elwing, H.3
  • 28
    • 0000250129 scopus 로고
    • Electrostatic and van der Waals contributions to protein adsorption: Comparison of theory and experiment
    • Roth CM, Lenhoff AM: Electrostatic and van der Waals contributions to protein adsorption: comparison of theory and experiment. Langmuir 1995, 11:3500-3509.
    • (1995) Langmuir , vol.11 , pp. 3500-3509
    • Roth, C.M.1    Lenhoff, A.M.2
  • 29
    • 0028347589 scopus 로고
    • 5 and a simulated anion-exchange adsorbent surface
    • 5 and a simulated anion-exchange adsorbent surface. Biophys J 1994, 66:1290-1300.
    • (1994) Biophys J , vol.66 , pp. 1290-1300
    • Roush, D.J.1    Gill, D.S.2    Willson, R.C.3
  • 30
    • 0028894113 scopus 로고
    • Protein adsorption kinetics drastically altered by repositioning a single charge
    • Ramsden JJ, Roush DJ, Gill DS, Kurrat R,1 Willson RC: Protein adsorption kinetics drastically altered by repositioning a single charge. J Am Chem Soc 1995, 117:8511-8516.
    • (1995) J am Chem Soc , vol.117 , pp. 8511-8516
    • Ramsden, J.J.1    Roush, D.J.2    Gill, D.S.3    Kurrat, R.4    Willson, R.C.5
  • 31
    • 0000964469 scopus 로고
    • Modeling of protein adsorption on polymer surfaces. Computation of adsorption potential
    • Noinville V, Vidalmadjar C, Sebille B: Modeling of protein adsorption on polymer surfaces. Computation of adsorption potential. J Phys Chem 1995, 99:1616-1522. The adsorption of a-lactalbumin and lysozyme on a polymer surface is studied by calculating the interaction between the model structures of these proteins, obtained from the protein data bank, and a model of a poly(vinylimidazole) surface. The interactions are evaluated for 2592 different protein/surface configurations.
    • (1995) J Phys Chem , vol.99 , pp. 1616-11522
    • Noinville, V.1    Vidalmadjar, C.2    Sebille, B.3
  • 32
    • 0000011627 scopus 로고
    • Protein adsorption at the Agl-water Interface
    • Galisleo F, Norde W: Protein adsorption at the Agl-water Interface. J Colloid Interface Sci 1995, 172:502-509.
    • (1995) J Colloid Interface Sci , vol.172 , pp. 502-509
    • Galisleo, F.1    Norde, W.2
  • 33
    • 0028917483 scopus 로고
    • The Temkln isotherm describes heterogeneous protein adsorption
    • Johnson RD, Arnold FH: The Temkln isotherm describes heterogeneous protein adsorption. Biochim Biophys Acta 1995, 1247:293-297.
    • (1995) Biochim Biophys Acta , vol.1247 , pp. 293-297
    • Johnson, R.D.1    Arnold, F.H.2
  • 34
    • 0026064798 scopus 로고
    • The heterogeneity of protein/surface Interactions and structural alterations of adsorbed albumin and Immunoglobulin G
    • Kulik EA, Kalinin ID, Sevastianov VI: The heterogeneity of protein/surface Interactions and structural alterations of adsorbed albumin and Immunoglobulin G. Artif Organs 1991, 15:386-391.
    • (1991) Artif Organs , vol.15 , pp. 386-391
    • Kulik, E.A.1    Kalinin, I.D.2    Sevastianov, V.I.3
  • 35
    • 0000146709 scopus 로고
    • Kinetic evidence for protein clustering at a surface
    • Ramsden JJ, Bachmanova GI, Archakov AI: Kinetic evidence for protein clustering at a surface. Phys Rev E 1994, 50:5072-5076.
    • (1994) Phys Rev E , vol.50 , pp. 5072-5076
    • Ramsden, J.J.1    Bachmanova, G.I.2    Archakov, A.I.3
  • 36
    • 0029252068 scopus 로고
    • Antibody binding to antigen-coated substrates studied with surface plasmon oscillations
    • Rahn JR, Hallock RB: Antibody binding to antigen-coated substrates studied with surface plasmon oscillations. Langmuir 1995, 11:650-654.
    • (1995) Langmuir , vol.11 , pp. 650-654
    • Rahn, J.R.1    Hallock, R.B.2
  • 37
    • 0002264389 scopus 로고
    • Kinetic-diffusive-convective adsorption in TIRF flow cells
    • Filippov LK: Kinetic-diffusive-convective adsorption in TIRF flow cells. J Colloid Interface Sci 1995, 174:32-39.
    • (1995) J Colloid Interface Sci , vol.174 , pp. 32-39
    • Filippov, L.K.1
  • 38
    • 0011116357 scopus 로고
    • Determination of the orientation distribution of adsorbed fluorophores using TIRF. 2. Measurements on porphyrin and cytochrome c
    • Bos MA, Klein JM: Determination of the orientation distribution of adsorbed fluorophores using TIRF. 2. Measurements on porphyrin and cytochrome c. Biophys J 1995, 68:955-962. Using polarized total internal reflection fluorescence, these authors obtain information on the orientation of adsorbed cytochrome c and porphyrins. The maximum entropy method is used to extract maximum information on the orientation distribution. The orientation was, however, hardly affected either by the potential of the sorbent surface or by the surface coverage.
    • (1995) Biophys J , vol.68 , pp. 955-962
    • Ma, B.1    Klein, J.M.2
  • 39
    • 0028519261 scopus 로고
    • Conformation of human plasma proteins at polymer surfaces: The effectiveness of surface heparinization
    • Barbucci R, Magnani A: Conformation of human plasma proteins at polymer surfaces: the effectiveness of surface heparinization. Biomaterials 1994, 15:955-962.
    • (1994) Biomaterials , vol.15 , pp. 955-962
    • Barbucci, R.1    Magnani, A.2
  • 40
    • 0028464408 scopus 로고
    • Changes in conformation of human serum albumin (HSA) and gamma globulins (γ-G) upon adsorption to polystyrene and poly(styrene/acrolein) latexes: Studies by fluorescence spectroscopy
    • Kowalczyk D, Slomkowski S, Wang FW: Changes In conformation of human serum albumin (HSA) and gamma globulins (γ-G) upon adsorption to polystyrene and poly(styrene/acrolein) latexes: studies by fluorescence spectroscopy. J Bioact Compat Polymers 1994, 9:282-309.
    • (1994) J Bioact Compat Polymers , vol.9 , pp. 282-309
    • Kowalczyk, D.1    Slomkowski, S.2    Wang, F.W.3
  • 42
    • 0028336837 scopus 로고
    • Conformational changes of proteins at an Interface Induced by a supported planar phosphatidic acid monolayer
    • Sui SF, Wu H, Sheng J, Guo Y: Conformational changes of proteins at an Interface Induced by a supported planar phosphatidic acid monolayer. J Biochem 1994, 115:1053-1057.
    • (1994) J Biochem , vol.115 , pp. 1053-1057
    • Sui, S.F.1    Wu, H.2    Sheng, J.3    Guo, Y.4
  • 43
    • 0029059110 scopus 로고
    • Dynamics surrounding Cys-34 in native, chemically denatured, and silica-adsorbed bovine serum albumin
    • Wang R, Sun S, Bekos EJ, Bright FV: Dynamics surrounding Cys-34 in native, chemically denatured, and silica-adsorbed bovine serum albumin. Anal Chem 1995, 67:149-159.
    • (1995) Anal Chem , vol.67 , pp. 149-159
    • Wang, R.1    Sun, S.2    Bekos, E.J.3    Bright, F.V.4
  • 44
    • 0001102616 scopus 로고
    • Ellipsometry studies of the effect of surface hydrophobicity on protein adsorption
    • Malmsten M: Ellipsometry studies of the effect of surface hydrophobicity on protein adsorption. Colloids Surfaces [B]. 1995, 3:297-308.
    • (1995) Colloids Surfaces [B] , vol.3 , pp. 297-308
    • Malmsten, M.1
  • 45
    • 4243766747 scopus 로고    scopus 로고
    • Changes in the secondary structure of adsorbed IgG and F(ab′)a studied by FTIR spectroscopy
    • in press
    • 2 part of an IgG molecule is structurally more stable than the whole IgG molecule, with respect to adsorption. The reduction in the amount of β-sheet structure in the whole IgG is relatively large when the net charge on the protein rises and when the sorbent surface is more hydrophobic.
    • (1996) Langmuir
    • Buijs, J.1    Norde, W.2    Lichtenbelt, J.W.T.3
  • 47
    • 0028295673 scopus 로고
    • Covalent immobilization of protein monolayers for biosensor applications
    • Williams RA, Blanch HW: Covalent immobilization of protein monolayers for biosensor applications. Biosens Bioelectron 1994, 9:159-167.
    • (1994) Biosens Bioelectron , vol.9 , pp. 159-167
    • Williams, R.A.1    Blanch, H.W.2
  • 48
    • 0028934326 scopus 로고
    • Electrochemical techniques for the modification of microelectrodes
    • Strike DJ, De Rooij NF, Koudelka-Hep M: Electrochemical techniques for the modification of microelectrodes. Biosens Bioelectron 1995, 10:61-66.
    • (1995) Biosens Bioelectron , vol.10 , pp. 61-66
    • Strike, D.J.1    De Rooij, N.F.2    Koudelka-Hep, M.3
  • 50
    • 84988057779 scopus 로고
    • Protein adsorption at glassy carbon electrodes: The effect of covalently bound surface groups
    • Downard AJ, Roddick AD: Protein adsorption at glassy carbon electrodes: the effect of covalently bound surface groups. Electroanalysis 1995, 7:376-378.
    • (1995) Electroanalysis , vol.7 , pp. 376-378
    • Downard, A.J.1    Roddick, A.D.2
  • 51
    • 0028929261 scopus 로고
    • Direct electron transfer bioelectronic interfaces: Application to clinical analysis
    • McNeil CJ, Athey D, Ho WO: Direct electron transfer bioelectronic interfaces: application to clinical analysis. Biosens Bioelectron 1995, 10:75-83.
    • (1995) Biosens Bioelectron , vol.10 , pp. 75-83
    • McNeil, C.J.1    Athey, D.2    Ho, W.O.3
  • 52
    • 0000710998 scopus 로고
    • Layer-by-layer assembly of alternate protein polylon utrathin films
    • Lvov Y, Ariga K,1 Kunitake T: Layer-by-layer assembly of alternate protein polylon utrathin films. Chem Lett 1994:2323-2326. Presents a novel method for the construction of thin multilayared protein films by sequential co-adsorption of charged polyetectrolytes and proteins. The charged protein layers form multilayers, with linear polymers acting as 'glue' or 'filler'. These layered structures open a way to construct artificial protein systems that can carry out complex coupled enzymatic reactions.
    • (1994) Chem Lett , pp. 2323-2326
    • Lvov, Y.1    Ariga, K.2    Kunitake, T.3
  • 53
    • 0028609085 scopus 로고
    • New nanocomposite films for biosensors: Layer-by-layer adsorbed films of polyelectrolytes, proteins or DNA
    • Decher G, Lehr B, Lowack K, Lvov Y, Schmitt J: New nanocomposite films for biosensors: layer-by-layer adsorbed films of polyelectrolytes, proteins or DNA. Biosens Bioelectron 1904, 9:677-664. Describes the construction of ultrathin multicomponent films at the nanometer scale. The films provide a well defined substrate-independent interface for the immobilization of biological macromolecules.
    • (1904) Biosens Bioelectron , vol.9 , pp. 677-1664
    • Decher, G.1    Lehr, B.2    Lowack, K.3    Lvov, Y.4    Schmitt, J.5
  • 55
    • 0001604912 scopus 로고
    • Exchange kinetics for a heterogeneous protein system on a solid surface
    • Huetz P, Ball V, Voegel JC, Schaaf P: Exchange kinetics for a heterogeneous protein system on a solid surface. Langmuir 1995, 11:3145-3152.
    • (1995) Langmuir , vol.11 , pp. 3145-3152
    • Huetz, P.1    Ball, V.2    Voegel, J.C.3    Schaaf, P.4
  • 56
    • 0001440148 scopus 로고
    • Protein adsorption at phosphollpid surfaces
    • Malmsten M: Protein adsorption at phosphollpid surfaces. J Colloid Interface Sci 1995, 172:106-115.
    • (1995) J Colloid Interface Sci , vol.172 , pp. 106-115
    • Malmsten, M.1
  • 57
    • 0028141554 scopus 로고
    • Differential surface binding of albumin, immunoglobulin G and fibrinogen
    • Warkentin P, Walivaara B, Lundstrom I, Tengvall P: Differential surface binding of albumin, immunoglobulin G and fibrinogen. Biomaterials 1994, 15:786-795.
    • (1994) Biomaterials , vol.15 , pp. 786-795
    • Warkentin, P.1    Walivaara, B.2    Lundstrom, I.3    Tengvall, P.4
  • 59
    • 84947356772 scopus 로고
    • Interactions of plasma proteins with a novel polysaccharide surfactant physisorbed to polyethylene
    • Marchant RE, Yuan S, Szakalas-Gratzl G: Interactions of plasma proteins with a novel polysaccharide surfactant physisorbed to polyethylene. J Biomater Sci Polymer Edn 1994, 6:549-564.
    • (1994) J Biomater Sci Polymer Edn , vol.6 , pp. 549-564
    • Marchant, R.E.1    Yuan, S.2    Szakalas-Gratzl, G.3
  • 62
    • 0028452838 scopus 로고
    • Protein adsorption on low-temperature isotropic carbon: I. Protein conformational change probed by differential scanning calorimetry
    • Feng L, Andrade O: Protein adsorption on low-temperature isotropic carbon: I. Protein conformational change probed by differential scanning calorimetry. J Biomed Mater Res 1994, 28:735-743.
    • (1994) J Biomed Mater Res , vol.28 , pp. 735-743
    • Feng, L.1    Andrade, O.2
  • 63
    • 0028518670 scopus 로고
    • Adherent platelet morphology on adsorbed fibrinogen: Effects of protein incubation time and albumin addition
    • Sheppard JI, McClung WG, Fuerstein IA: Adherent platelet morphology on adsorbed fibrinogen: effects of protein incubation time and albumin addition. J Biomed Mater Res 1994, 28:1175-1186.
    • (1994) J Biomed Mater Res , vol.28 , pp. 1175-1186
    • Sheppard, J.I.1    McClung, W.G.2    Fuerstein, I.A.3
  • 64
    • 84867227916 scopus 로고
    • Protein adsorption, lymphocyte adhesion and platelet adhesion/activation on Polyurethane ureas is related to hard segment content and composition
    • Groth T, Klosz K, Campbell EJ, New RRC, Hall B, Goering H: Protein adsorption, lymphocyte adhesion and platelet adhesion/activation on Polyurethane ureas is related to hard segment content and composition. J Biomater Sci Polymer Edn 1994, 6:497-510.
    • (1994) J Biomater Sci Polymer Edn , vol.6 , pp. 497-510
    • Groth, T.1    Klosz, K.2    Campbell, E.J.3    New, R.R.C.4    Hall, B.5    Goering, H.6
  • 65
    • 0029278145 scopus 로고
    • Bacteria/blood/material Interactions. I. Injected and preseeded slime-forming Staphytococcus epidermidis in flowing blood with biomaterials
    • Brunstedt MR, Sapatnekar S, Rubin KR, Kieswetter KM, Ziats NP, Merritt K, Anderson JM: Bacteria/blood/material Interactions. I. Injected and preseeded slime-forming Staphytococcus epidermidis in flowing blood with biomaterials. J Biomed Mater Res 1995, 29:455-466.
    • (1995) J Biomed Mater Res , vol.29 , pp. 455-466
    • Brunstedt, M.R.1    Sapatnekar, S.2    Rubin, K.R.3    Kieswetter, K.M.4    Ziats, N.P.5    Merritt, K.6    Anderson, J.M.7
  • 66
    • 0028470882 scopus 로고
    • Lans-on-surrace method for investigating adhesion of Stophylococcus aureus to solid surfaces Incubated in blood plasma
    • Elwing H, Aakendal A: Lans-on-surrace method for investigating adhesion of Stophylococcus aureus to solid surfaces Incubated In blood plasma. J Biomed Mater Res 1994, 28:775-782.
    • (1994) J Biomed Mater Res , vol.28 , pp. 775-782
    • Elwing, H.1    Aakendal, A.2
  • 67
    • 0023468837 scopus 로고
    • Protein adsorption and materials biocompatibility: A tutorial review and suggested hypotheses
    • Andrade JD, Hlady V: Protein adsorption and materials biocompatibility: a tutorial review and suggested hypotheses. Adv Polym Sci 1986, 79:1-63.
    • (1986) Adv Polym Sci , vol.79 , pp. 1-63
    • Andrade, J.D.1    Hlady, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.