메뉴 건너뛰기




Volumn 29, Issue 27, 2013, Pages 8554-8560

Surface-dependent mechanical stability of adsorbed human plasma fibronectin on Ti6Al4V: Domain unfolding and stepwise unraveling of single compact molecules

Author keywords

[No Author keywords available]

Indexed keywords

FLEXIBLE CONFORMATION; FORCE DISPLACEMENT; INDIVIDUAL PROTEINS; IRRADIATION PROCESS; MATERIAL SURFACE; MECHANICAL DENATURATIONS; MOLECULAR LEVELS; PROTEIN COMPONENTS;

EID: 84880144940     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la401776e     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 34547422260 scopus 로고    scopus 로고
    • Engineered Microcapsules Fabricated from Reconstituted Spider Silk
    • Hermanson, K. D.; Huemmerich, D.; Scheibel, T.; Bausch, A. R. Engineered Microcapsules Fabricated from Reconstituted Spider Silk Adv. Mater. 2007, 19, 1810-1815
    • (2007) Adv. Mater. , vol.19 , pp. 1810-1815
    • Hermanson, K.D.1    Huemmerich, D.2    Scheibel, T.3    Bausch, A.R.4
  • 2
    • 42149100435 scopus 로고    scopus 로고
    • Microscopy, Microstructure and Displacement of Proteins from Interfaces: Implications for Food Quality and Digestion
    • Morris, V. J.; Gunning, A. P. Microscopy, Microstructure and Displacement of Proteins from Interfaces: Implications for Food Quality and Digestion Soft Matter. 2008, 4, 943-951
    • (2008) Soft Matter. , vol.4 , pp. 943-951
    • Morris, V.J.1    Gunning, A.P.2
  • 3
    • 70549095846 scopus 로고    scopus 로고
    • Novel Surface Coatings Modulating Eukaryotic Cell Adhesion and Preventing Implant Infection
    • Groll, J.; Fiedler, J.; Bruellhoff, K.; Moeller, M.; Brenner, R. E. Novel Surface Coatings Modulating Eukaryotic Cell Adhesion and Preventing Implant Infection Int. J. Artif. Organs 2009, 32, 655-662
    • (2009) Int. J. Artif. Organs , vol.32 , pp. 655-662
    • Groll, J.1    Fiedler, J.2    Bruellhoff, K.3    Moeller, M.4    Brenner, R.E.5
  • 4
    • 30644471966 scopus 로고    scopus 로고
    • Biofilm in Implant Infections: Its Production and Regulation
    • Costerton, J. W.; Montanaro, L.; Arciola, C. R. Biofilm in Implant Infections: Its Production and Regulation Int. J. Artif. Organs 2005, 28, 1062-1068
    • (2005) Int. J. Artif. Organs , vol.28 , pp. 1062-1068
    • Costerton, J.W.1    Montanaro, L.2    Arciola, C.R.3
  • 8
    • 78650028835 scopus 로고    scopus 로고
    • Fibronectin: A Multidomain Host Adhesin Targeted by Bacterial Fibronectin-Binding Proteins
    • Henderson, B.; Nair, S.; Pallas, J.; Williams, M. A. Fibronectin: a Multidomain Host Adhesin Targeted by Bacterial Fibronectin-Binding Proteins FEMS Microbiol. Rev. 2011, 35, 147-200
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 147-200
    • Henderson, B.1    Nair, S.2    Pallas, J.3    Williams, M.A.4
  • 10
    • 0042008055 scopus 로고    scopus 로고
    • Surface-Dependent Conformations of Human Plasma Fibronectin Adsorbed to Silica, Mica, and Hydrophobic Surfaces, Studied with Use of Atomic Force Microscopy
    • Bergkvist, M.; Carlsson, J.; Oscarsson, S. Surface-Dependent Conformations of Human Plasma Fibronectin Adsorbed to Silica, Mica, and Hydrophobic Surfaces, Studied with Use of Atomic Force Microscopy J. Biomed. Mater. Res., Part A 2003, 64, 349-356
    • (2003) J. Biomed. Mater. Res., Part A , vol.64 , pp. 349-356
    • Bergkvist, M.1    Carlsson, J.2    Oscarsson, S.3
  • 12
    • 0028213715 scopus 로고
    • Solution Structure of a Pair of Fibronectin Type 1 Modules with Fibrin Binding Activity
    • Williams, M. J.; Phan, I.; Harvey, T. S.; Rostagno, A.; Gold, L. I.; Campbell, I. D. Solution Structure of a Pair of Fibronectin Type 1 Modules with Fibrin Binding Activity J. Mol. Biol. 1994, 235, 1302-1311
    • (1994) J. Mol. Biol. , vol.235 , pp. 1302-1311
    • Williams, M.J.1    Phan, I.2    Harvey, T.S.3    Rostagno, A.4    Gold, L.I.5    Campbell, I.D.6
  • 13
    • 0032512876 scopus 로고    scopus 로고
    • Solution Structure of the Glycosylated Second Type 2 Module of Fibronectin
    • Sticht, H.; Pickford, A. F.; Potts, J. R.; Campbell, I. D. Solution Structure of the Glycosylated Second Type 2 Module of Fibronectin J. Mol. Biol. 1998, 276, 177-187
    • (1998) J. Mol. Biol. , vol.276 , pp. 177-187
    • Sticht, H.1    Pickford, A.F.2    Potts, J.R.3    Campbell, I.D.4
  • 15
    • 0033016468 scopus 로고    scopus 로고
    • The Compact Conformation of Fibronectin is Determined by Intramolecular Ionic Interactions
    • Johnson, K. J.; Sage, H.; Briscoe, G.; Erickson, H. P. The Compact Conformation of Fibronectin is Determined by Intramolecular Ionic Interactions J. Biol. Chem. 1999, 274, 15473-15479
    • (1999) J. Biol. Chem. , vol.274 , pp. 15473-15479
    • Johnson, K.J.1    Sage, H.2    Briscoe, G.3    Erickson, H.P.4
  • 16
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction Involving Multimodular Proteins: Converting Force into Biochemical Signals
    • Vogel, V. Mechanotransduction Involving Multimodular Proteins: Converting Force into Biochemical Signals Annu. Rev. Biophys. Biomol. Struct. 2006, 35, 459-488
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 459-488
    • Vogel, V.1
  • 17
    • 0035826819 scopus 로고    scopus 로고
    • Comparison of the Early Stages of Forced Unfolding for Fibronectin Type III Modules
    • Craig, D.; Krammer, A.; Schulten, K.; Vogel, V. Comparison of the Early Stages of Forced Unfolding for Fibronectin Type III Modules Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 5590-5595
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5590-5595
    • Craig, D.1    Krammer, A.2    Schulten, K.3    Vogel, V.4
  • 18
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and Unfolding of Single Molecules of the Giant Muscle Protein Titin
    • Tskhovrebova, L.; Trinick, J.; Sleep, J. A.; Simmons, R. M. Elasticity and Unfolding of Single Molecules of the Giant Muscle Protein Titin Nature 1997, 387, 308-312
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 19
    • 0031011695 scopus 로고    scopus 로고
    • Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM
    • Rief, M.; Gautel, M.; Oesterhelt, F.; Fernandez, J. M.; Gaub, H. E. Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM Science 1997, 276, 1109-1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 20
    • 0032516205 scopus 로고    scopus 로고
    • The Molecular Elasticity of the Extracellular Matrix Protein Tenascin
    • Oberhauser, A. F.; Marszalek, P. E.; Erickson, H. P.; Ferndandez, J. M. The Molecular Elasticity of the Extracellular Matrix Protein Tenascin Nature 1998, 393, 181185
    • (1998) Nature , vol.393 , pp. 181185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Ferndandez, J.M.4
  • 21
    • 0033582763 scopus 로고    scopus 로고
    • Single Molecule Force Spectroscopy of Spectrin Repeats: Low Unfolding Forces in Helix Bundles
    • Rief, M.; Pascual, J.; Saraste, M.; Gaub, H. E. Single Molecule Force Spectroscopy of Spectrin Repeats: Low Unfolding Forces in Helix Bundles J. Mol. Biol. 1998, 286, 553-561
    • (1998) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 23
    • 2442448427 scopus 로고    scopus 로고
    • The Unfolding Kinetics of Ubiquitin Captured with Single-Molecule Force-Clamp Techniques
    • Schlierf, M.; Li, H.; Fernandez, J. M. The Unfolding Kinetics of Ubiquitin Captured with Single-Molecule Force-Clamp Techniques Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 7299-7304
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.2    Fernandez, J.M.3
  • 24
    • 33847774117 scopus 로고    scopus 로고
    • Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM
    • Brown, A. E.; Litvinov, R. I.; Discher, D. E.; Weisel, J. W. Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM Biophys. J. 2007, 92, L39-L41
    • (2007) Biophys. J. , vol.92
    • Brown, A.E.1    Litvinov, R.I.2    Discher, D.E.3    Weisel, J.W.4
  • 26
    • 0034804341 scopus 로고    scopus 로고
    • Can Non-Mechanical Proteins Withstand Force? Stretching Barnase by Atomic Force Microscopy and Molecular Dynamics Simulation
    • Best, R. B.; Li, B.; Steward, A.; Daggett, V.; Clarke, J. Can Non-Mechanical Proteins Withstand Force? Stretching Barnase by Atomic Force Microscopy and Molecular Dynamics Simulation Biophys. J. 2001, 81, 2344-2356
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 30
    • 0343777458 scopus 로고    scopus 로고
    • Observing Single Biomolecules at Work with the Atomic Force Microscope
    • Engel, A.; Muller, D. J. Observing Single Biomolecules at Work With the Atomic Force Microscope Nat. Struct. Biol. 2000, 7, 715-718
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 31
    • 33645515274 scopus 로고    scopus 로고
    • Fibrinogen Adsorption on Three Silica-Based Surfaces: Conformation and Kinetics
    • Toscano, A.; Santore, M. M. Fibrinogen Adsorption on Three Silica-Based Surfaces: Conformation and Kinetics Langmuir 2006, 14, 2588-2597
    • (2006) Langmuir , vol.14 , pp. 2588-2597
    • Toscano, A.1    Santore, M.M.2
  • 32
    • 0021058825 scopus 로고
    • Fibronectin in Extended and Compact Conformations. Electron Microscopy and Sedimentation Analysis
    • Erickson, H. P.; Carrell, N. A. Fibronectin in Extended and Compact Conformations. Electron Microscopy and Sedimentation Analysis J. Biol. Chem. 1983, 258, 14539-14544
    • (1983) J. Biol. Chem. , vol.258 , pp. 14539-14544
    • Erickson, H.P.1    Carrell, N.A.2
  • 34
    • 0032126449 scopus 로고    scopus 로고
    • Surface Analysis of Human Plasma Fibronectin Adsorbed to Commercially Pure Titanium Materials
    • MacDonald, D. E.; Markovic, B.; Allen, M.; Somasundaran, P.; Boskey, A. L. Surface Analysis of Human Plasma Fibronectin Adsorbed to Commercially Pure Titanium Materials J. Biomed. Mater. Res. 1998, 41, 120-130
    • (1998) J. Biomed. Mater. Res. , vol.41 , pp. 120-130
    • Macdonald, D.E.1    Markovic, B.2    Allen, M.3    Somasundaran, P.4    Boskey, A.L.5
  • 36
    • 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
  • 37
    • 58149374589 scopus 로고    scopus 로고
    • UV-C Irradiation Disrupts Platelet Surface Disulfide Bonds and Activates the Platelet Integrin αiIbβ3
    • Verhaar, R.; Dekkers, D. W. C.; De Cuyper, I. M.; Ginsberg, M. H.; De Korte, D.; Verhoeven, A. J. UV-C Irradiation Disrupts Platelet Surface Disulfide Bonds and Activates the Platelet Integrin αIIbβ3 Blood 2008, 112, 49-35-4939
    • (2008) Blood , vol.112 , pp. 4935-4939
    • Verhaar, R.1    Dekkers, D.W.C.2    De Cuyper, I.M.3    Ginsberg, M.H.4    De Korte, D.5    Verhoeven, A.J.6
  • 38
    • 33746084916 scopus 로고    scopus 로고
    • Proteomic Analysis of UVC Irradiation-Induced Damage of Plasma Proteins: Serum Amyloid P Component as a Major Target of Photolysis
    • Chan, H. L.; Gaffney, P. R.; Waterfield, M. D.; Anderle, H.; Matthiessen, P. H.; Schwarz, H. P.; Turecek, P. L.; Timms, J. F. Proteomic Analysis of UVC Irradiation-Induced Damage of Plasma Proteins: Serum Amyloid P Component as a Major Target of Photolysis FEBS Lett. 2006, 580, 3229-3236
    • (2006) FEBS Lett. , vol.580 , pp. 3229-3236
    • Chan, H.L.1    Gaffney, P.R.2    Waterfield, M.D.3    Anderle, H.4    Matthiessen, P.H.5    Schwarz, H.P.6    Turecek, P.L.7    Timms, J.F.8
  • 40
    • 33645417227 scopus 로고    scopus 로고
    • Understanding the Elasticity of Fibronectin Fibrils: Unfolding Strengths of FN-III and GFP Domains Measured by Single Molecule Force Spectroscopy
    • Abu-Lail, N. I.; Ohashi, T.; Clark, R. L.; Erickson, H. P.; Zauscher, S. Understanding the Elasticity of Fibronectin Fibrils: Unfolding Strengths of FN-III and GFP Domains Measured by Single Molecule Force Spectroscopy Matrix Biol. 2006, 25, 175-184
    • (2006) Matrix Biol. , vol.25 , pp. 175-184
    • Abu-Lail, N.I.1    Ohashi, T.2    Clark, R.L.3    Erickson, H.P.4    Zauscher, S.5
  • 41
    • 0344062772 scopus 로고    scopus 로고
    • Single-Molecule Force Spectroscopy of Isolated and Aggregated Fibronectin Proteins on Negatively Charged Surfaces in Aqueous Liquids
    • Meadows, P. Y.; Bemis, J. E.; Walker, G. C. Single-Molecule Force Spectroscopy of Isolated and Aggregated Fibronectin Proteins on Negatively Charged Surfaces in Aqueous Liquids Langmuir 2003, 19, 9566-9572
    • (2003) Langmuir , vol.19 , pp. 9566-9572
    • Meadows, P.Y.1    Bemis, J.E.2    Walker, G.C.3
  • 42
    • 0038368702 scopus 로고    scopus 로고
    • Conformational Analysis of Native Fibronectin by Means of Force Spectroscopy
    • Oberdorfer, Y.; Fuchs, H.; Janshoff, A. Conformational Analysis of Native Fibronectin by Means of Force Spectroscopy Langmuir 2000, 16, 9955-9958
    • (2000) Langmuir , vol.16 , pp. 9955-9958
    • Oberdorfer, Y.1    Fuchs, H.2    Janshoff, A.3
  • 43
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical Unfolding Intermediates Observed by Single-Molecule Force Spectroscopy in a Fibronectin Type III Module
    • Li, L.; Huang, H. H.-L.; Badilla, C. L.; Fernandez, J. M. Mechanical Unfolding Intermediates Observed by Single-Molecule Force Spectroscopy in a Fibronectin Type III Module J. Mol. Biol. 2005, 345, 817-826
    • (2005) J. Mol. Biol. , vol.345 , pp. 817-826
    • Li, L.1    Huang, H.H.-L.2    Badilla, C.L.3    Fernandez, J.M.4
  • 44
    • 0033531973 scopus 로고    scopus 로고
    • Forced Unfolding of Fibronectin Type 3 Modules: An Analysis by Biased Molecular Dynamics Simulations
    • Paci, E.; Karplus, M. Forced Unfolding of Fibronectin Type 3 Modules: an Analysis by Biased Molecular Dynamics Simulations J. Mol. Biol. 1999, 288, 441-459
    • (1999) J. Mol. Biol. , vol.288 , pp. 441-459
    • Paci, E.1    Karplus, M.2
  • 45
    • 0035852740 scopus 로고    scopus 로고
    • Forced Unfolding Modulated by Disulfide Bonds in the Ig Domains of a Cell Adhesion Molecule
    • Carl, P.; Kwok, C. H.; Manderson, G.; Speicher, D. W.; Discher, D. E. Forced Unfolding Modulated by Disulfide Bonds in the Ig Domains of a Cell Adhesion Molecule Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 1565-1570
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1565-1570
    • Carl, P.1    Kwok, C.H.2    Manderson, G.3    Speicher, D.W.4    Discher, D.E.5
  • 46
    • 8544278061 scopus 로고    scopus 로고
    • Chemistry on a Single Protein, Vascular Cell Adhesion Molecule-1, during Forced Unfolding
    • Bhasin, N.; Carl, P.; Harper, S.; Feng, G.; Lu, H.; Speicher, D. W.; Discher, D. E. Chemistry on a Single Protein, Vascular Cell Adhesion Molecule-1, during Forced Unfolding J. Biol. Chem. 2004, 279, 45865-45874
    • (2004) J. Biol. Chem. , vol.279 , pp. 45865-45874
    • Bhasin, N.1    Carl, P.2    Harper, S.3    Feng, G.4    Lu, H.5    Speicher, D.W.6    Discher, D.E.7
  • 47
    • 0036977558 scopus 로고    scopus 로고
    • The Myosin Coiled-Coil is a Truly Elastic Protein Structure
    • Schwaiger, I.; Sattler, C.; Hostetter, D. R.; Rief, M. The Myosin Coiled-Coil is a Truly Elastic Protein Structure Nat. Mater. 2002, 1, 232-235
    • (2002) Nat. Mater. , vol.1 , pp. 232-235
    • Schwaiger, I.1    Sattler, C.2    Hostetter, D.R.3    Rief, M.4
  • 48
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The Elastic Response of Individual Double-Stranded and Single-Stranded DNA Molecules
    • Smith, S. B.; Cui, Y.; Bustamante, C. Overstretching B-DNA: the Elastic Response of Individual Double-Stranded and Single-Stranded DNA Molecules Science 1996, 271, 795-799
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 49
    • 0033064934 scopus 로고    scopus 로고
    • Unraveling Proteins: A Molecular Mechanics Study
    • Rohs, R.; Etchebest, C.; Lavery, R. Unraveling Proteins: a Molecular Mechanics Study Biophys. J. 1999, 76, 2760-2768
    • (1999) Biophys. J. , vol.76 , pp. 2760-2768
    • Rohs, R.1    Etchebest, C.2    Lavery, R.3
  • 50
    • 0033151955 scopus 로고    scopus 로고
    • Steered Molecular Dynamics Simulations of Force-Induced Protein Domain Unfolding
    • Lu, H.; Schulten, K. Steered Molecular Dynamics Simulations of Force-Induced Protein Domain Unfolding Proteins 1999, 35, 453-463
    • (1999) Proteins , vol.35 , pp. 453-463
    • Lu, H.1    Schulten, K.2
  • 51
    • 0031767965 scopus 로고    scopus 로고
    • The Mechanical Stability of Immunoglobulin and Fibronectin III Domains in the Muscle Protein Titin Measured by Atomic Force Microscopy
    • Rief, M.; Gautel, M.; Schemmel, A.; Gaub, H. E. The Mechanical Stability of Immunoglobulin and Fibronectin III Domains in the Muscle Protein Titin Measured by Atomic Force Microscopy Biophys. J. 1998, 75, 3008-3014
    • (1998) Biophys. J. , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 53
    • 0028213715 scopus 로고
    • Solution structure of a Pair of Fibronectin Type 1 Modules with Fibrin Binding Activity
    • Williams, M. J.; Phan, I.; Harvey, T. S.; Rostagno, A.; Gold, L. I. Solution structure of a Pair of Fibronectin Type 1 Modules with Fibrin Binding Activity J. Mol. Biol. 1994, 235, 1302-1311
    • (1994) J. Mol. Biol. , vol.235 , pp. 1302-1311
    • Williams, M.J.1    Phan, I.2    Harvey, T.S.3    Rostagno, A.4    Gold, L.I.5
  • 54
    • 0031569351 scopus 로고    scopus 로고
    • Solution Structure of a Type 2 Module from Fibronectin: Implications for the Structure and Function of the Gelatin-Binding Domain
    • Pickford, A. R.; Potts, J. R.; Bright, J. R.; Phan, I.; Campbell, I. D. Solution Structure of a Type 2 Module from Fibronectin: Implications for the Structure and Function of the Gelatin-Binding Domain Structure 1997, 5, 359-370
    • (1997) Structure , vol.5 , pp. 359-370
    • Pickford, A.R.1    Potts, J.R.2    Bright, J.R.3    Phan, I.4    Campbell, I.D.5
  • 55
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A Crystal Structure of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop and Synergy Region
    • Leahy, D. J.; Aukhil, I.; Erickson, H. P. 2.0 A Crystal Structure of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop and Synergy Region Cell 1996, 84, 155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.