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Volumn 39, Issue 7, 2008, Pages 832-842

Immunological identification of fibrinogen in dual-component protein films by AFM imaging

Author keywords

AFM; Biocompatibility; Biomaterials; Fibrinogen; Gold labeling; Immunochemistry; Polymers; Protein adsorption

Indexed keywords

ATOMIC FORCE MICROSCOPY; BIOLOGICAL MATERIALS; BLOOD; FLOW INTERACTIONS; GOLD; MICA; MICROSCOPIC EXAMINATION; SCANNING PROBE MICROSCOPY; SILICATE MINERALS; THEOREM PROVING;

EID: 48749103309     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2007.12.013     Document Type: Article
Times cited : (21)

References (50)
  • 1
    • 33746098208 scopus 로고    scopus 로고
    • Atomic force microscopy visualization of poly(urethane urea) microphase rearrangements under aqueous environment
    • Agnihotri A., Garrett J., Runt J., and Siedlecki C. Atomic force microscopy visualization of poly(urethane urea) microphase rearrangements under aqueous environment. J. Biomater. Sci. Polym. Ed. 17 (2006) 227-238
    • (2006) J. Biomater. Sci. Polym. Ed. , vol.17 , pp. 227-238
    • Agnihotri, A.1    Garrett, J.2    Runt, J.3    Siedlecki, C.4
  • 2
    • 5444270593 scopus 로고    scopus 로고
    • Time-dependent conformational changes in fibrinogen measured by atomic force microscopy
    • Agnihotri A., and Siedlecki C. Time-dependent conformational changes in fibrinogen measured by atomic force microscopy. Langmuir 20 (2004) 8846-8852
    • (2004) Langmuir , vol.20 , pp. 8846-8852
    • Agnihotri, A.1    Siedlecki, C.2
  • 3
    • 13444262175 scopus 로고    scopus 로고
    • Adhesion mode atomic force microscopy study of dual component protein films
    • Agnihotri A., and Siedlecki C. Adhesion mode atomic force microscopy study of dual component protein films. Ultramicroscopy 102 (2005) 257-268
    • (2005) Ultramicroscopy , vol.102 , pp. 257-268
    • Agnihotri, A.1    Siedlecki, C.2
  • 4
    • 0030658844 scopus 로고    scopus 로고
    • Phase imaging of moving DNA molecules and DNA molecules replicated in the atomic force microscope
    • Argaman M., Golan R., Thomson N., and Hansma H. Phase imaging of moving DNA molecules and DNA molecules replicated in the atomic force microscope. Nucl. Acids Res. 25 (1997) 4379-4384
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4379-4384
    • Argaman, M.1    Golan, R.2    Thomson, N.3    Hansma, H.4
  • 6
    • 0031561078 scopus 로고    scopus 로고
    • Factors affecting the height and phase images in tapping mode atomic force microscopy: study of phase-separated polymer blends of poly(ethene-co-styrene) and poly (2,6-dimethyl-1-1,4-phenylene oxide)
    • Bar G., Thomann Y., Brandsch R., and Cantow H. Factors affecting the height and phase images in tapping mode atomic force microscopy: study of phase-separated polymer blends of poly(ethene-co-styrene) and poly (2,6-dimethyl-1-1,4-phenylene oxide). Langmuir 13 (1997) 3807-3812
    • (1997) Langmuir , vol.13 , pp. 3807-3812
    • Bar, G.1    Thomann, Y.2    Brandsch, R.3    Cantow, H.4
  • 8
    • 0028358415 scopus 로고
    • Clues for understanding the structure and function of a prototypic human integrin: the platelet glycoprotein IIb/IIIa complex
    • Calvete J.J. Clues for understanding the structure and function of a prototypic human integrin: the platelet glycoprotein IIb/IIIa complex. Thromb. Haemostasis 72 (1994) 1-15
    • (1994) Thromb. Haemostasis , vol.72 , pp. 1-15
    • Calvete, J.J.1
  • 10
    • 0032029417 scopus 로고    scopus 로고
    • FTIR/ATR for protein adsorption to biomaterial surfaces
    • Chittur K. FTIR/ATR for protein adsorption to biomaterial surfaces. Biomaterials 19 (1998) 357-369
    • (1998) Biomaterials , vol.19 , pp. 357-369
    • Chittur, K.1
  • 11
    • 0028795533 scopus 로고
    • Cell-surface receptors and proteins on platelets imaged by scanning force microscopy using immunogold contrast enhancement
    • Eppell S.J., Simmons S.R., Albrecht R.M., and Marchant R.E. Cell-surface receptors and proteins on platelets imaged by scanning force microscopy using immunogold contrast enhancement. Biophys. J. 68 (1995) 671-680
    • (1995) Biophys. J. , vol.68 , pp. 671-680
    • Eppell, S.J.1    Simmons, S.R.2    Albrecht, R.M.3    Marchant, R.E.4
  • 12
    • 0026476365 scopus 로고
    • Role of fibrinogen alpha and gamma chain sites in platelet aggregation
    • Farrell D., Thiagarajan P., Chung D., and Davie E. Role of fibrinogen alpha and gamma chain sites in platelet aggregation. PNAS 89 (1992) 10729-10732
    • (1992) PNAS , vol.89 , pp. 10729-10732
    • Farrell, D.1    Thiagarajan, P.2    Chung, D.3    Davie, E.4
  • 14
    • 2442501409 scopus 로고    scopus 로고
    • Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes
    • Gorbet M., and Sefton M. Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes. Biomaterials 25 (2004) 5681-5703
    • (2004) Biomaterials , vol.25 , pp. 5681-5703
    • Gorbet, M.1    Sefton, M.2
  • 15
    • 0031106750 scopus 로고    scopus 로고
    • Surface plasmon resonance for real time in situ analysis of protein adsorption to polymer surfaces
    • Green R., Davies J., Davies M., Roberts C., and Tendler S. Surface plasmon resonance for real time in situ analysis of protein adsorption to polymer surfaces. Biomaterials 18 (1997) 405-413
    • (1997) Biomaterials , vol.18 , pp. 405-413
    • Green, R.1    Davies, J.2    Davies, M.3    Roberts, C.4    Tendler, S.5
  • 16
    • 0033080940 scopus 로고    scopus 로고
    • Competitive protein adsorption as observed by surface plasmon resonance
    • Green R., Davies M., Roberts C., and Tendler S. Competitive protein adsorption as observed by surface plasmon resonance. Biomaterials 20 (1999) 385-391
    • (1999) Biomaterials , vol.20 , pp. 385-391
    • Green, R.1    Davies, M.2    Roberts, C.3    Tendler, S.4
  • 17
    • 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., and Tendler S.J.B. Surface plasmon resonance for real time in situ analysis of protein adsorption to polymer surfaces. Biomaterials 18 (1997) 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
  • 18
    • 0008340711 scopus 로고    scopus 로고
    • Nanogold Technology: new frontiers in gold labeling
    • Hainfeld J.F., and Powell R.D. Nanogold Technology: new frontiers in gold labeling. Cell Vision 4 (1997) 408-432
    • (1997) Cell Vision , vol.4 , pp. 408-432
    • Hainfeld, J.F.1    Powell, R.D.2
  • 19
    • 0002218258 scopus 로고    scopus 로고
    • Fibrinogen structure and physiology
    • Colman R.W., Hirsh J., Marder V.J., Clowes A.W., and George J.N. (Eds), Lippincott Williams & Wilkins, Philadelphia
    • Hantgan R., Simpson-Haidaris P., Francis C., and Marder V. Fibrinogen structure and physiology. In: Colman R.W., Hirsh J., Marder V.J., Clowes A.W., and George J.N. (Eds). Hemostasis and Thrombosis (2001), Lippincott Williams & Wilkins, Philadelphia 203-232
    • (2001) Hemostasis and Thrombosis , pp. 203-232
    • Hantgan, R.1    Simpson-Haidaris, P.2    Francis, C.3    Marder, V.4
  • 20
    • 0029883621 scopus 로고    scopus 로고
    • Detection and localization of individual antibody-antigen recognition events by atomic force microscopy
    • Hinterdorfer P., Baumgartner W., Gruber H., Schilcher K., and Schindler H. Detection and localization of individual antibody-antigen recognition events by atomic force microscopy. PNAS 93 (1996) 3477-3481
    • (1996) PNAS , vol.93 , pp. 3477-3481
    • Hinterdorfer, P.1    Baumgartner, W.2    Gruber, H.3    Schilcher, K.4    Schindler, H.5
  • 21
    • 0034609629 scopus 로고    scopus 로고
    • Individual plasma proteins detected on rough biomaterials by phase imaging AFM
    • Holland N., and Marchant R. Individual plasma proteins detected on rough biomaterials by phase imaging AFM. J. Biomed. Mater. Res. 51 (2000) 307-315
    • (2000) J. Biomed. Mater. Res. , vol.51 , pp. 307-315
    • Holland, N.1    Marchant, R.2
  • 22
    • 43949164704 scopus 로고
    • Principles underlying the role of adsorbed plasma proteins in blood interactions with foreign materials
    • Horbett T.A. Principles underlying the role of adsorbed plasma proteins in blood interactions with foreign materials. Cardiovasc. Pathol. 2 (1993) 137S-148S
    • (1993) Cardiovasc. Pathol. , vol.2
    • Horbett, T.A.1
  • 23
    • 23144456804 scopus 로고    scopus 로고
    • AFM imaging of ligand binding to platelets integrin alpha IIb ß3 receptors reconstituted into planar lipid bilayers
    • Hussain M., Agnihotri A., and Siedlecki C. AFM imaging of ligand binding to platelets integrin alpha IIb ß3 receptors reconstituted into planar lipid bilayers. Langmuir 21 (2005) 6979-6986
    • (2005) Langmuir , vol.21 , pp. 6979-6986
    • Hussain, M.1    Agnihotri, A.2    Siedlecki, C.3
  • 24
    • 33644784853 scopus 로고    scopus 로고
    • Interfacial energetics of blood plasma and serum adsorption to a hydrophobic self-assembled monolayer surface
    • Krishnan A., Cha P., Liu Y.-H., Allara D., and Vogler E.A. Interfacial energetics of blood plasma and serum adsorption to a hydrophobic self-assembled monolayer surface. Biomaterials 27 (2006) 3187-3194
    • (2006) Biomaterials , vol.27 , pp. 3187-3194
    • Krishnan, A.1    Cha, P.2    Liu, Y.-H.3    Allara, D.4    Vogler, E.A.5
  • 25
    • 0029938646 scopus 로고    scopus 로고
    • Competitive protein adsorption studied with TIRF and Ellipsometry
    • Lassen B., and Malmsten M. Competitive protein adsorption studied with TIRF and Ellipsometry. J. Colloid Interface Sci. 179 (1996) 470-477
    • (1996) J. Colloid Interface Sci. , vol.179 , pp. 470-477
    • Lassen, B.1    Malmsten, M.2
  • 26
    • 0034724152 scopus 로고    scopus 로고
    • Imaging and mapping heparin-binding sites on single fibronectin molecules with atomic force microscopy
    • Lin H., Lal R., and Clegg D. Imaging and mapping heparin-binding sites on single fibronectin molecules with atomic force microscopy. Biochemistry 39 (2000) 3192-3196
    • (2000) Biochemistry , vol.39 , pp. 3192-3196
    • Lin, H.1    Lal, R.2    Clegg, D.3
  • 27
  • 28
    • 33645301592 scopus 로고    scopus 로고
    • Sub-micron texturing for reducing platelet adhesion to polyurethane biomaterials
    • Milner K., Snyder A., and Siedlecki C. Sub-micron texturing for reducing platelet adhesion to polyurethane biomaterials. J. Biomed. Mater. Res. A 76A (2006) 561-570
    • (2006) J. Biomed. Mater. Res. A , vol.76 A , pp. 561-570
    • Milner, K.1    Snyder, A.2    Siedlecki, C.3
  • 29
    • 0035958049 scopus 로고    scopus 로고
    • Cryo-electron microscopic localization of protein L7/L12 within the Escherichia coli 70 S ribosome by difference mapping and Nanogold labeling
    • Montesano-Roditis L., Glitz D.G., Traut R.R., and Stewart P.L. Cryo-electron microscopic localization of protein L7/L12 within the Escherichia coli 70 S ribosome by difference mapping and Nanogold labeling. J. Biol. Chem. 276 (2001) 14117-14123
    • (2001) J. Biol. Chem. , vol.276 , pp. 14117-14123
    • Montesano-Roditis, L.1    Glitz, D.G.2    Traut, R.R.3    Stewart, P.L.4
  • 30
    • 33747870203 scopus 로고    scopus 로고
    • Volumetric interpretation of protein adsorption: mass and energy balance for albumin adsorption to particulate adsorbents with incrementally increasing hydrophilicity
    • Noh H., and Vogler E.A. Volumetric interpretation of protein adsorption: mass and energy balance for albumin adsorption to particulate adsorbents with incrementally increasing hydrophilicity. Biomaterials 27 (2006) 5801-5812
    • (2006) Biomaterials , vol.27 , pp. 5801-5812
    • Noh, H.1    Vogler, E.A.2
  • 31
    • 33750190740 scopus 로고    scopus 로고
    • Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect
    • Noh H., and Vogler E.A. Volumetric interpretation of protein adsorption: competition from mixtures and the Vroman effect. Biomaterials 28 (2007) 405-422
    • (2007) Biomaterials , vol.28 , pp. 405-422
    • Noh, H.1    Vogler, E.A.2
  • 32
    • 0038203392 scopus 로고    scopus 로고
    • Mapping of the receptor-associated protein (RAP) binding proteins on living fibroblast cells using an atomic force microscope
    • Osada T., Itoh A., and Ikai A. Mapping of the receptor-associated protein (RAP) binding proteins on living fibroblast cells using an atomic force microscope. Ultramicroscopy 97 (2003) 353-357
    • (2003) Ultramicroscopy , vol.97 , pp. 353-357
    • Osada, T.1    Itoh, A.2    Ikai, A.3
  • 33
    • 0000398836 scopus 로고    scopus 로고
    • Apparent contrast reversal in tapping mode atomic force microscope images on films of polystyrene-b-polyisoprene-b-polystyrene
    • Pickering J., and Vancso G. Apparent contrast reversal in tapping mode atomic force microscope images on films of polystyrene-b-polyisoprene-b-polystyrene. Polym. Bull. 40 (1998) 549-554
    • (1998) Polym. Bull. , vol.40 , pp. 549-554
    • Pickering, J.1    Vancso, G.2
  • 34
    • 0002111559 scopus 로고    scopus 로고
    • Integrin alpha IIb ß3 and platelet aggregation
    • Colman R.W., Hirsh J., Marder V.J., Clowes A.W., and George J.N. (Eds), Lippincott Williams & Wilkins, Philadelphia
    • Plow E., and Shattil S. Integrin alpha IIb ß3 and platelet aggregation. In: Colman R.W., Hirsh J., Marder V.J., Clowes A.W., and George J.N. (Eds). Hemostasis and Thrombosis (2001), Lippincott Williams & Wilkins, Philadelphia 479-492
    • (2001) Hemostasis and Thrombosis , pp. 479-492
    • Plow, E.1    Shattil, S.2
  • 36
    • 0031106327 scopus 로고    scopus 로고
    • Measuring the elastic properties of biological samples with the AFM
    • Radmacher M. Measuring the elastic properties of biological samples with the AFM. Eng. Med. Biol. Mag., IEEE 16 (1997) 47-57
    • (1997) Eng. Med. Biol. Mag., IEEE , vol.16 , pp. 47-57
    • Radmacher, M.1
  • 37
    • 0034657607 scopus 로고    scopus 로고
    • Determining intramolecular binding sites on surface-bound von Willebrand Factor under aqueous conditions
    • Raghavachari M., Kottke-Marchant K., and Marchant R. Determining intramolecular binding sites on surface-bound von Willebrand Factor under aqueous conditions. Thromb. Res. 98 (2000) 351-358
    • (2000) Thromb. Res. , vol.98 , pp. 351-358
    • Raghavachari, M.1    Kottke-Marchant, K.2    Marchant, R.3
  • 38
    • 0033894687 scopus 로고    scopus 로고
    • Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy
    • Reviakine I., and Brisson A. Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy. Langmuir 16 (2000) 1806-1815
    • (2000) Langmuir , vol.16 , pp. 1806-1815
    • Reviakine, I.1    Brisson, A.2
  • 39
    • 0033880358 scopus 로고    scopus 로고
    • 2+ on the morphology of mixed DPPC-DOPS supported phospholipid bilayers
    • 2+ on the morphology of mixed DPPC-DOPS supported phospholipid bilayers. Langmuir 16 (2000) 1473-1477
    • (2000) Langmuir , vol.16 , pp. 1473-1477
    • Reviakine, I.1    Simon, A.2    Brisson, A.3
  • 41
    • 33645515274 scopus 로고    scopus 로고
    • Fibrinogen adsorption on three silica-based surfaces: conformation and kinetics
    • Toscano A., and Santore M. Fibrinogen adsorption on three silica-based surfaces: conformation and kinetics. Langmuir 22 (2006) 2588-2597
    • (2006) Langmuir , vol.22 , pp. 2588-2597
    • Toscano, A.1    Santore, M.2
  • 42
    • 0037783430 scopus 로고    scopus 로고
    • Nanoscale mapping of the elasticity of microbial cells by atomic force microscopy
    • Touhami A., Nysten B., and Dufrene Y.F. Nanoscale mapping of the elasticity of microbial cells by atomic force microscopy. Langmuir 19 (2003) 4539-4543
    • (2003) Langmuir , vol.19 , pp. 4539-4543
    • Touhami, A.1    Nysten, B.2    Dufrene, Y.F.3
  • 43
    • 0032046426 scopus 로고    scopus 로고
    • Real-time observation of plasma protein film formation on well-defined surfaces with scanning force microscopy
    • Truong C., Sykes M., and McDermott M. Real-time observation of plasma protein film formation on well-defined surfaces with scanning force microscopy. Langmuir 14 (1998) 2435-2443
    • (1998) Langmuir , vol.14 , pp. 2435-2443
    • Truong, C.1    Sykes, M.2    McDermott, M.3
  • 44
    • 0033080578 scopus 로고    scopus 로고
    • Human plasma fibrinogen adsorption and platelet adhesion to polystyrene
    • Tsai W.B., Grunkemeier J.M., and Horbett T.A. Human plasma fibrinogen adsorption and platelet adhesion to polystyrene. J. Biomed. Mater. Res. 44 (1999) 130-139
    • (1999) J. Biomed. Mater. Res. , vol.44 , pp. 130-139
    • Tsai, W.B.1    Grunkemeier, J.M.2    Horbett, T.A.3
  • 45
    • 0029347525 scopus 로고
    • Contact activation of the plasma coagulation cascade.II. Protein adsorption to procoagulant surfaces
    • Vogler E., Graper J., Sugg H., Lander L., and Brittain W. Contact activation of the plasma coagulation cascade.II. Protein adsorption to procoagulant surfaces. J. Biomed. Mater. Res. 29 (1995) 1017-1028
    • (1995) J. Biomed. Mater. Res. , vol.29 , pp. 1017-1028
    • Vogler, E.1    Graper, J.2    Sugg, H.3    Lander, L.4    Brittain, W.5
  • 46
    • 0037400643 scopus 로고    scopus 로고
    • Characterizing multicomponent adsorbed protein films using electron spectroscopy for chemical analysis, time-of-flight secondary ion mass spectrometry, and radiolabeling: capabilities and limitations
    • Wagner M., Horbett T., and Castner D. Characterizing multicomponent adsorbed protein films using electron spectroscopy for chemical analysis, time-of-flight secondary ion mass spectrometry, and radiolabeling: capabilities and limitations. Biomaterials 24 (2003) 1897-1908
    • (2003) Biomaterials , vol.24 , pp. 1897-1908
    • Wagner, M.1    Horbett, T.2    Castner, D.3
  • 47
    • 0002861111 scopus 로고    scopus 로고
    • Quantitative analysis of binary adsorbed protein films by time of flight secondary ion mass spectrometry
    • Wagner M., Shen M., Horbett T., and Castner D. Quantitative analysis of binary adsorbed protein films by time of flight secondary ion mass spectrometry. J. Biomed. Mater. Res. Part A 64A (2003) 1-11
    • (2003) J. Biomed. Mater. Res. Part A , vol.64 A , pp. 1-11
    • Wagner, M.1    Shen, M.2    Horbett, T.3    Castner, D.4
  • 49
    • 0035874552 scopus 로고    scopus 로고
    • Effect of surface hydrophobicity on adsorption and relaxation kinetics of albumin and fibrinogen: single-species and competitive behavior
    • Wertz C.F., and Santore M.M. Effect of surface hydrophobicity on adsorption and relaxation kinetics of albumin and fibrinogen: single-species and competitive behavior. Langmuir 17 (2001) 3006-3016
    • (2001) Langmuir , vol.17 , pp. 3006-3016
    • Wertz, C.F.1    Santore, M.M.2
  • 50
    • 0034638260 scopus 로고    scopus 로고
    • Ultrastructural localization of gustducin immunoreactivity in microvilli of type II taste cells in the rat
    • Yang R., Tabata S., Crowley H.H., Margolskee R.F., and Kinnamon J.C. Ultrastructural localization of gustducin immunoreactivity in microvilli of type II taste cells in the rat. J. Comp. Neurol. 425 (2000) 139-151
    • (2000) J. Comp. Neurol. , vol.425 , pp. 139-151
    • Yang, R.1    Tabata, S.2    Crowley, H.H.3    Margolskee, R.F.4    Kinnamon, J.C.5


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