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Volumn 32, Issue 6, 2011, Pages 1646-1656

Protein adsorption and complement activation for di-block copolymer nanoparticles

Author keywords

Adsorption isotherm; BSA; C3; Core diffuse shell nanoparticles; Fibrinogen; Mesh size

Indexed keywords

BSA; C3; FIBRINOGEN; MESH SIZE; SHELL NANOPARTICLES;

EID: 78650283439     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2010.10.026     Document Type: Article
Times cited : (72)

References (48)
  • 1
    • 63949086707 scopus 로고    scopus 로고
    • Methods for the preparation and manufacture of polymeric nanoparticles
    • Vauthier C., Bouchemal K. Methods for the preparation and manufacture of polymeric nanoparticles. Pharm Res 2009, 26:1025-1058.
    • (2009) Pharm Res , vol.26 , pp. 1025-1058
    • Vauthier, C.1    Bouchemal, K.2
  • 2
    • 0029937438 scopus 로고    scopus 로고
    • Stability of orosomucoid-coated polyisobutylcyanoacrylate nanoparticles in the presence of serum
    • Olivier J.C., Vauthier C., Taverna M., Puisieux F., Ferrier D., Couvreur P. Stability of orosomucoid-coated polyisobutylcyanoacrylate nanoparticles in the presence of serum. J Control Release 1996, 40:157-168.
    • (1996) J Control Release , vol.40 , pp. 157-168
    • Olivier, J.C.1    Vauthier, C.2    Taverna, M.3    Puisieux, F.4    Ferrier, D.5    Couvreur, P.6
  • 4
    • 33750190740 scopus 로고    scopus 로고
    • Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect
    • Noh H., Vogler E.A. Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect. Biomaterials 2007, 28:405-422.
    • (2007) Biomaterials , vol.28 , pp. 405-422
    • Noh, H.1    Vogler, E.A.2
  • 5
    • 0035006284 scopus 로고    scopus 로고
    • Structure and biology of complement protein C3, a connecting link between innate and acquired immunity
    • Sahu A., Lambris J.D. Structure and biology of complement protein C3, a connecting link between innate and acquired immunity. Immunol Rev 2001, 180:35-48.
    • (2001) Immunol Rev , vol.180 , pp. 35-48
    • Sahu, A.1    Lambris, J.D.2
  • 6
    • 0031043135 scopus 로고    scopus 로고
    • The internal thioester and the covalent binding properties of the complement proteins C3 and C4
    • Law S.K., Dodds A.W. The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci 1997, 6:263-274.
    • (1997) Protein Sci , vol.6 , pp. 263-274
    • Law, S.K.1    Dodds, A.W.2
  • 7
    • 33646384586 scopus 로고    scopus 로고
    • Parameters influencing the stealthiness of colloidal drug delivery systems
    • Vonarbourg A., Passirani C., Saulnier P., Benoit J.P. Parameters influencing the stealthiness of colloidal drug delivery systems. Biomaterials 2006, 27:4356-4373.
    • (2006) Biomaterials , vol.27 , pp. 4356-4373
    • Vonarbourg, A.1    Passirani, C.2    Saulnier, P.3    Benoit, J.P.4
  • 8
    • 0030209082 scopus 로고    scopus 로고
    • Effect of PEO surface density on long-circulating PLA-PEO nanoparticles which are very low complement activators
    • Vittaz M., Bazile D., Spenlehauer G., Verrecchia T., Veillard M., Puisieux F., et al. Effect of PEO surface density on long-circulating PLA-PEO nanoparticles which are very low complement activators. Biomaterials 1996, 17:1575-1581.
    • (1996) Biomaterials , vol.17 , pp. 1575-1581
    • Vittaz, M.1    Bazile, D.2    Spenlehauer, G.3    Verrecchia, T.4    Veillard, M.5    Puisieux, F.6
  • 9
    • 33745402302 scopus 로고    scopus 로고
    • Complement activation by core-shell poly(isobutylcyanoacrylate)-polysaccharide nanoparticles: influences of surface morphology, length, and type of polysaccharide
    • Bertholon I., Vauthier C., Labarre D. Complement activation by core-shell poly(isobutylcyanoacrylate)-polysaccharide nanoparticles: influences of surface morphology, length, and type of polysaccharide. Pharm Res 2006, 23:1313-1323.
    • (2006) Pharm Res , vol.23 , pp. 1313-1323
    • Bertholon, I.1    Vauthier, C.2    Labarre, D.3
  • 10
    • 7444238105 scopus 로고    scopus 로고
    • Binding of C3 fragments on top of adsorbed plasma proteins during complement activation on a model biomaterial surface
    • Andersson J., Nilsson Ekdahla K., Lambris J.D., Nilsson B. Binding of C3 fragments on top of adsorbed plasma proteins during complement activation on a model biomaterial surface. Biomaterials 2005, 26:1477-1485.
    • (2005) Biomaterials , vol.26 , pp. 1477-1485
    • Andersson, J.1    Nilsson Ekdahla, K.2    Lambris, J.D.3    Nilsson, B.4
  • 11
    • 36749067955 scopus 로고    scopus 로고
    • Design aspects of poly(alkylcyanoacrylate) nanoparticles for drug delivery
    • Vauthier C., Ponchel G., Labarre D. Design aspects of poly(alkylcyanoacrylate) nanoparticles for drug delivery. J Drug Target 2007, 15:641-663.
    • (2007) J Drug Target , vol.15 , pp. 641-663
    • Vauthier, C.1    Ponchel, G.2    Labarre, D.3
  • 13
    • 0029311133 scopus 로고
    • Protein-rejecting ability of surface-bound dextran in end-on and side-on configurations: comparison to PEG
    • Osterberg E., Bergström K., Holmberg K., Schuman T.P., Riggs J.A., Burns N.L., et al. Protein-rejecting ability of surface-bound dextran in end-on and side-on configurations: comparison to PEG. J Biomed Mater Res 1995, 29:741-747.
    • (1995) J Biomed Mater Res , vol.29 , pp. 741-747
    • Osterberg, E.1    Bergström, K.2    Holmberg, K.3    Schuman, T.P.4    Riggs, J.A.5    Burns, N.L.6
  • 14
    • 33947388411 scopus 로고    scopus 로고
    • Development of dextran-derivative arrays to identify physicochemical properties involved in biofouling from serum
    • Monchaux E., Vermette P. Development of dextran-derivative arrays to identify physicochemical properties involved in biofouling from serum. Langmuir 2007, 23:3290-3297.
    • (2007) Langmuir , vol.23 , pp. 3290-3297
    • Monchaux, E.1    Vermette, P.2
  • 15
    • 50849106680 scopus 로고    scopus 로고
    • A biomimetic alternative to poly(ethylene glycol) as an antifouling coating: resistance to nonspecific protein adsorption of poly(l-lysine)-graft-dextran
    • Perrino C., Lee S., Choi S.W., Maruyama A., Spencer N.D. A biomimetic alternative to poly(ethylene glycol) as an antifouling coating: resistance to nonspecific protein adsorption of poly(l-lysine)-graft-dextran. Langmuir 2008, 24:8850-8856.
    • (2008) Langmuir , vol.24 , pp. 8850-8856
    • Perrino, C.1    Lee, S.2    Choi, S.W.3    Maruyama, A.4    Spencer, N.D.5
  • 16
    • 33744490152 scopus 로고    scopus 로고
    • Characterization of dextran-poly(isobutylcyanoacrylate) copolymers obtained by redox radical and anionic emulsion polymerization
    • Bertholon I., Lesieur S., Labarre D., Besnard M., Vauthier C. Characterization of dextran-poly(isobutylcyanoacrylate) copolymers obtained by redox radical and anionic emulsion polymerization. Macromolecules 2006, 39:3559-3567.
    • (2006) Macromolecules , vol.39 , pp. 3559-3567
    • Bertholon, I.1    Lesieur, S.2    Labarre, D.3    Besnard, M.4    Vauthier, C.5
  • 17
    • 0013895324 scopus 로고
    • Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies
    • Laurell C.B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 1966, 15:45-52.
    • (1966) Anal Biochem , vol.15 , pp. 45-52
    • Laurell, C.B.1
  • 18
    • 0013797229 scopus 로고
    • Immunochemical quantitation of antigens by single radial immunodiffusion
    • Mancini G., Carbonara A.O., Heremans J.F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 1965, 2:235-254.
    • (1965) Immunochemistry , vol.2 , pp. 235-254
    • Mancini, G.1    Carbonara, A.O.2    Heremans, J.F.3
  • 19
    • 0021064269 scopus 로고
    • Potentiation of factor H by heparin: a rate-limiting mechanism for inhibition of the alternative complement pathway
    • Boackle R.J., Caughman G.B., Vesely J., Medgyesi G., Fudenberg H.H. Potentiation of factor H by heparin: a rate-limiting mechanism for inhibition of the alternative complement pathway. Mol Immunol 1983, 20:1157-1164.
    • (1983) Mol Immunol , vol.20 , pp. 1157-1164
    • Boackle, R.J.1    Caughman, G.B.2    Vesely, J.3    Medgyesi, G.4    Fudenberg, H.H.5
  • 20
    • 60449112775 scopus 로고    scopus 로고
    • Configuration of bovine serum albumin adsorbed on polymer particles with grafted dextran corona
    • Vauthier C., Lindner P., Cabane B. Configuration of bovine serum albumin adsorbed on polymer particles with grafted dextran corona. Colloids Surf B Biointerfaces 2009, 69:207-215.
    • (2009) Colloids Surf B Biointerfaces , vol.69 , pp. 207-215
    • Vauthier, C.1    Lindner, P.2    Cabane, B.3
  • 21
    • 0029937893 scopus 로고    scopus 로고
    • Characterization of polybutyleyanoacrylate nanoparticles. part II: determination of polymer content by NMR-analysis
    • Pirker S., Kruse J., Noe C., Langer K., Zimmer A., Kreuter J. Characterization of polybutyleyanoacrylate nanoparticles. part II: determination of polymer content by NMR-analysis. Int J Pharm 1996, 128:189-195.
    • (1996) Int J Pharm , vol.128 , pp. 189-195
    • Pirker, S.1    Kruse, J.2    Noe, C.3    Langer, K.4    Zimmer, A.5    Kreuter, J.6
  • 23
    • 0034228594 scopus 로고    scopus 로고
    • Structure properties of dextran. 2. dilute solution
    • Ioan C.E., Aberle T., Burchard W. Structure properties of dextran. 2. dilute solution. Macromolecules 2000, 33:5730-5739.
    • (2000) Macromolecules , vol.33 , pp. 5730-5739
    • Ioan, C.E.1    Aberle, T.2    Burchard, W.3
  • 24
    • 0000635229 scopus 로고
    • A comparison of the adsorbed layer thickness obtained by several techniques of various molecular weight fractions of poly(vinyl alcohol) on aqueous polystyrene latex particles
    • Garvey M.J., Tadros T.F., Vincent B. A comparison of the adsorbed layer thickness obtained by several techniques of various molecular weight fractions of poly(vinyl alcohol) on aqueous polystyrene latex particles. J Colloid Interface Sci 1976, 55:440-453.
    • (1976) J Colloid Interface Sci , vol.55 , pp. 440-453
    • Garvey, M.J.1    Tadros, T.F.2    Vincent, B.3
  • 25
    • 0002600914 scopus 로고
    • Bridging of colloidal particles through adsorbed polymers
    • Lafuma F., Wong K., Cabane B. Bridging of colloidal particles through adsorbed polymers. J Colloid Interface Sci 1991, 143:9-21.
    • (1991) J Colloid Interface Sci , vol.143 , pp. 9-21
    • Lafuma, F.1    Wong, K.2    Cabane, B.3
  • 27
    • 0007377156 scopus 로고
    • Molecular and crystal structure of dextrans: a combined electron and X-ray diffraction study. 1. the anhydrous high-temperature polymorph
    • Guizard C., Chanzy H., Sarko A. Molecular and crystal structure of dextrans: a combined electron and X-ray diffraction study. 1. the anhydrous high-temperature polymorph. Macromolecules 1984, 17:100-107.
    • (1984) Macromolecules , vol.17 , pp. 100-107
    • Guizard, C.1    Chanzy, H.2    Sarko, A.3
  • 28
    • 0029344512 scopus 로고
    • Preparation and characterization of biodegradable poly(isobutylcyanoacrylate) nanoparticles with the surface modified by the adsorption of proteins
    • Olivier J.C., Vauthier C., Taverna M., Ferrier D., Couvreur P. Preparation and characterization of biodegradable poly(isobutylcyanoacrylate) nanoparticles with the surface modified by the adsorption of proteins. Colloids Surf B Biointerfaces 1995, 4:349-356.
    • (1995) Colloids Surf B Biointerfaces , vol.4 , pp. 349-356
    • Olivier, J.C.1    Vauthier, C.2    Taverna, M.3    Ferrier, D.4    Couvreur, P.5
  • 29
    • 64149086416 scopus 로고    scopus 로고
    • Effect of poly(N-vinyl-pyrrolidone)-block-poly(D, L-lactide) as coating agent on the opsonization, phagocytosis, and pharmacokinetics of biodegradable nanoparticles
    • Gaucher G., Asahina K., Wang J., Leroux J.C. Effect of poly(N-vinyl-pyrrolidone)-block-poly(D, L-lactide) as coating agent on the opsonization, phagocytosis, and pharmacokinetics of biodegradable nanoparticles. Biomacromolecules 2009, 10:408-416.
    • (2009) Biomacromolecules , vol.10 , pp. 408-416
    • Gaucher, G.1    Asahina, K.2    Wang, J.3    Leroux, J.C.4
  • 31
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry
    • Roach P., Farrar D., Perry C.C. Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J Am Chem Soc 2006, 128:3939-3945.
    • (2006) J Am Chem Soc , vol.128 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 32
    • 0034717340 scopus 로고    scopus 로고
    • BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states
    • Norde W., Giacomelli C.E. BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states. J Biotechnol 2000, 79:259-268.
    • (2000) J Biotechnol , vol.79 , pp. 259-268
    • Norde, W.1    Giacomelli, C.E.2
  • 33
    • 33846803773 scopus 로고    scopus 로고
    • Proteins at fluid interfaces: adsorption layers and thin liquid films
    • Yampolskaya G., Platikanov D. Proteins at fluid interfaces: adsorption layers and thin liquid films. Adv Colloid Interface Sci 2006, 128-130:159-183.
    • (2006) Adv Colloid Interface Sci , vol.128-130 , pp. 159-183
    • Yampolskaya, G.1    Platikanov, D.2
  • 34
    • 65249097917 scopus 로고    scopus 로고
    • Structure of fibrinogen in electrolyte solutions derived from dynamic light scattering (DLS) and viscosity measurements
    • Wasilewska M., Adamczyk Z., Jachimska B. Structure of fibrinogen in electrolyte solutions derived from dynamic light scattering (DLS) and viscosity measurements. Langmuir 2009, 25:3698-3704.
    • (2009) Langmuir , vol.25 , pp. 3698-3704
    • Wasilewska, M.1    Adamczyk, Z.2    Jachimska, B.3
  • 37
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin high resolution crystal structures. the protein data bank
    • Pbd Id 1E78
    • Bhattacharya A.A., Curry S., Franks N.P. Binding of the general anesthetics propofol and halothane to human serum albumin high resolution crystal structures. the protein data bank. J Biol Chem 2000, 275:38731-38738. Pbd Id 1E78.
    • (2000) J Biol Chem , vol.275 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 38
    • 66149138396 scopus 로고    scopus 로고
    • Crystal structure of human fibrinogen. the protein data bank
    • Pbd Id 3GHG
    • Kollman J.M., Pandi L., Sawaya M.R., Riley M., Doolittle R.F. Crystal structure of human fibrinogen. the protein data bank. Biochemistry 2009, 48:3877-3886. Pbd Id 3GHG.
    • (2009) Biochemistry , vol.48 , pp. 3877-3886
    • Kollman, J.M.1    Pandi, L.2    Sawaya, M.R.3    Riley, M.4    Doolittle, R.F.5
  • 39
    • 25644452794 scopus 로고    scopus 로고
    • Structures of complement component C3 provide insights into the function and evolution of immunity. the protein data bank
    • Pbd Id 2A73
    • Janssen B.J., Huizinga E.G., Raaijmakers H.C., Roos A., Daha M.R., Nilsson-Ekdahl K., et al. Structures of complement component C3 provide insights into the function and evolution of immunity. the protein data bank. Nature 2005, 437:505-511. Pbd Id 2A73.
    • (2005) Nature , vol.437 , pp. 505-511
    • Janssen, B.J.1    Huizinga, E.G.2    Raaijmakers, H.C.3    Roos, A.4    Daha, M.R.5    Nilsson-Ekdahl, K.6
  • 40
    • 49349124955 scopus 로고
    • The adsorption of human plasma albumin and bovine pancreas ribonuclease at negatively charged polystyrene surfaces: 1 adsorption isotherms: effects of charge, ionic strength, and temperature
    • Norde W., Lyklema J. The adsorption of human plasma albumin and bovine pancreas ribonuclease at negatively charged polystyrene surfaces: 1 adsorption isotherms: effects of charge, ionic strength, and temperature. J Colloid Interface Sci 1978, 66:257-265.
    • (1978) J Colloid Interface Sci , vol.66 , pp. 257-265
    • Norde, W.1    Lyklema, J.2
  • 41
    • 17444427145 scopus 로고    scopus 로고
    • Surface enrichment of proteins at quartz/water interfaces: a neutron reflectivity study
    • Forcini D., Hamilton W.A. Surface enrichment of proteins at quartz/water interfaces: a neutron reflectivity study. J Colloid Interface Sci 2005, 285:458-468.
    • (2005) J Colloid Interface Sci , vol.285 , pp. 458-468
    • Forcini, D.1    Hamilton, W.A.2
  • 42
    • 0345551888 scopus 로고    scopus 로고
    • Bovine serum albumin adsorption on titania surfaces and its relation to wettability aspects
    • Amadeu do Serro A.P.V., la Catarino Fernandes A., de Jesus Vieira Saramago B., Norde W. Bovine serum albumin adsorption on titania surfaces and its relation to wettability aspects. J Biomed Mater Res 1999, 46:376-381.
    • (1999) J Biomed Mater Res , vol.46 , pp. 376-381
    • Amadeu do Serro, A.P.V.1    la Catarino, F.A.2    de Jesus Vieira, S.B.3    Norde, W.4
  • 43
    • 0027643021 scopus 로고
    • Adsorption/desorption of human serum albumin at the surface of poly(lactic acid) nanoparticles prepared by a solvent evaporation process
    • Verrecchia T., Huve P., Bazile D., Veillard M., Spenlehauer G., Couvreur P. Adsorption/desorption of human serum albumin at the surface of poly(lactic acid) nanoparticles prepared by a solvent evaporation process. J Biomed Mater Res 1993, 27:1019-1028.
    • (1993) J Biomed Mater Res , vol.27 , pp. 1019-1028
    • Verrecchia, T.1    Huve, P.2    Bazile, D.3    Veillard, M.4    Spenlehauer, G.5    Couvreur, P.6
  • 44
    • 0034158220 scopus 로고    scopus 로고
    • Surface characterization of functionalized polylactide through the coating with heterobifunctional poly(ethylene glycol)/polylactide block copolymers
    • Oksuka H., Nagasaki Y., Kataoka K. Surface characterization of functionalized polylactide through the coating with heterobifunctional poly(ethylene glycol)/polylactide block copolymers. Biomacromolecules 2000, 1:39-48.
    • (2000) Biomacromolecules , vol.1 , pp. 39-48
    • Oksuka, H.1    Nagasaki, Y.2    Kataoka, K.3
  • 45
    • 20444421544 scopus 로고    scopus 로고
    • Interpretation of protein adsorption: surface-induced conformational changes
    • Roach P., Farrar D., Perry C.C. Interpretation of protein adsorption: surface-induced conformational changes. J Am Chem Soc 2005, 127:8168-8173.
    • (2005) J Am Chem Soc , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 46
    • 33847697025 scopus 로고    scopus 로고
    • PH-dependent protein conformational changes in albumin: gold nanoparticle bioconjugates: a spectroscopic study
    • Shang L., Wang Y., Jiang J., Dong S. pH-dependent protein conformational changes in albumin: gold nanoparticle bioconjugates: a spectroscopic study. Langmuir 2007, 23:2714-2721.
    • (2007) Langmuir , vol.23 , pp. 2714-2721
    • Shang, L.1    Wang, Y.2    Jiang, J.3    Dong, S.4
  • 47
    • 41649108815 scopus 로고    scopus 로고
    • Interaction of gold nanoparticles with protein: a spectroscopic study to monitor protein conformational changes
    • 133104-133111-133104-3
    • Wangoo N., Suri R., Shekhawat G. Interaction of gold nanoparticles with protein: a spectroscopic study to monitor protein conformational changes. Appl Phys Lett 2008, 92. 133104-133111-133104-3.
    • (2008) Appl Phys Lett , vol.92
    • Wangoo, N.1    Suri, R.2    Shekhawat, G.3
  • 48
    • 0035501275 scopus 로고    scopus 로고
    • Surface-dependent differences in fibrin assembly visualized by atomic force microscopy
    • Sit P.S., Marchand R.E. Surface-dependent differences in fibrin assembly visualized by atomic force microscopy. Surf Sci 2001, 491:421-432.
    • (2001) Surf Sci , vol.491 , pp. 421-432
    • Sit, P.S.1    Marchand, R.E.2


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