Effect of Ca2+ Ions on the Adhesion and Mechanical Properties of Adsorbed Layers of Human Osteopontin

Using an atomic force microscope and a surface force apparatus, we measured the surface coverage, adhesion, and mechanical properties of layers of osteopontin (OPN), a phosphoprotein of the human bones, adsorbed on mica. OPN is believed to connect mineralized collagen fibrils of the bone in a matrix...

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Published inBiophysical journal Vol. 95; no. 6; pp. 2939 - 2950
Main Authors Zappone, Bruno, Thurner, Philipp J., Adams, Jonathan, Fantner, Georg E., Hansma, Paul K.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.09.2008
The Biophysical Society
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Abstract Using an atomic force microscope and a surface force apparatus, we measured the surface coverage, adhesion, and mechanical properties of layers of osteopontin (OPN), a phosphoprotein of the human bones, adsorbed on mica. OPN is believed to connect mineralized collagen fibrils of the bone in a matrix that dissipates energy, reducing the risk of fractures. Atomic force microscopy normal force measurements showed large adhesion and energy dissipation upon retraction of the tip, which were due to the breaking of the many OPN-OPN and OPN-mica bonds formed during tip-sample contact. The dissipated energy increased in the presence of Ca2+ ions due to the formation of additional OPN-OPN and OPN-mica salt bridges between negative charges. The forces measured by surface force apparatus between two macroscopic mica surfaces were mainly repulsive and became hysteretic only in the presence of Ca2+: adsorbed layers underwent an irreversible compaction during compression due to the formation of long-lived calcium salt bridges. This provides an energy storage mechanism, which is complementary to energy dissipation and may be equally relevant to bone recovery after yield. The prevalence of one mechanism or the other appears to depend on the confinement geometry, adsorption protocol, and loading-unloading rates.
AbstractList Using an atomic force microscope and a surface force apparatus, we measured the surface coverage, adhesion, and mechanical properties of layers of osteopontin (OPN), a phosphoprotein of the human bones, adsorbed on mica. OPN is believed to connect mineralized collagen fibrils of the bone in a matrix that dissipates energy, reducing the risk of fractures. Atomic force microscopy normal force measurements showed large adhesion and energy dissipation upon retraction of the tip, which were due to the breaking of the many OPN-OPN and OPN-mica bonds formed during tip-sample contact. The dissipated energy increased in the presence of Ca(2+) ions due to the formation of additional OPN-OPN and OPN-mica salt bridges between negative charges. The forces measured by surface force apparatus between two macroscopic mica surfaces were mainly repulsive and became hysteretic only in the presence of Ca(2+): adsorbed layers underwent an irreversible compaction during compression due to the formation of long-lived calcium salt bridges. This provides an energy storage mechanism, which is complementary to energy dissipation and may be equally relevant to bone recovery after yield. The prevalence of one mechanism or the other appears to depend on the confinement geometry, adsorption protocol, and loading-unloading rates.
Using an atomic force microscope and a surface force apparatus, we measured the surface coverage, adhesion, and mechanical properties of layers of osteopontin (OPN), a phosphoprotein of the human bones, adsorbed on mica. OPN is believed to connect mineralized collagen fibrils of the bone in a matrix that dissipates energy, reducing the risk of fractures. Atomic force microscopy normal force measurements showed large adhesion and energy dissipation upon retraction of the tip, which were due to the breaking of the many OPN-OPN and OPN-mica bonds formed during tip-sample contact. The dissipated energy increased in the presence of Ca2+ ions due to the formation of additional OPN-OPN and OPN-mica salt bridges between negative charges. The forces measured by surface force apparatus between two macroscopic mica surfaces were mainly repulsive and became hysteretic only in the presence of Ca2+: adsorbed layers underwent an irreversible compaction during compression due to the formation of long-lived calcium salt bridges. This provides an energy storage mechanism, which is complementary to energy dissipation and may be equally relevant to bone recovery after yield. The prevalence of one mechanism or the other appears to depend on the confinement geometry, adsorption protocol, and loading-unloading rates.
Using an atomic force microscope and a surface force apparatus, we measured the surface coverage, adhesion, and mechanical properties of layers of osteopontin (OPN), a phosphoprotein of the human bones, adsorbed on mica. OPN is believed to connect mineralized collagen fibrils of the bone in a matrix that dissipates energy, reducing the risk of fractures. Atomic force microscopy normal force measurements showed large adhesion and energy dissipation upon retraction of the tip, which were due to the breaking of the many OPN-OPN and OPN-mica bonds formed during tip-sample contact. The dissipated energy increased in the presence of Ca 2+ ions due to the formation of additional OPN-OPN and OPN-mica salt bridges between negative charges. The forces measured by surface force apparatus between two macroscopic mica surfaces were mainly repulsive and became hysteretic only in the presence of Ca 2+ : adsorbed layers underwent an irreversible compaction during compression due to the formation of long-lived calcium salt bridges. This provides an energy storage mechanism, which is complementary to energy dissipation and may be equally relevant to bone recovery after yield. The prevalence of one mechanism or the other appears to depend on the confinement geometry, adsorption protocol, and loading-unloading rates.
Author Adams, Jonathan
Zappone, Bruno
Hansma, Paul K.
Thurner, Philipp J.
Fantner, Georg E.
AuthorAffiliation Liquid Crystal Laboratory, Regional Laboratory and Center of Excellence for Functional Nanostructured Materials, Centro Nazionale delle Ricerche and Istituto Nazionale per la Fisica della Materia, Arcavacata di Rende (CS) 87036, Italy; † Bioengineering Science Research Group, University of Southampton, Southampton, United Kingdom; ‡ Department of Physics, University of California, Santa Barbara, California; and § Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts
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Cites_doi 10.1038/nmat1428
10.1016/0021-9797(87)90447-4
10.1093/glycob/cwh151
10.1093/bioinformatics/18.5.769
10.1093/glycob/cwl009
10.1016/0021-9797(73)90218-X
10.1038/1781304b0
10.1557/JMR.1990.2223
10.1529/biophysj.106.088799
10.1017/S0033583501003687
10.1146/annurev.matsci.28.1.271
10.1002/(SICI)1097-0282(199812)46:7<489::AID-BIP6>3.0.CO;2-E
10.1016/0021-9797(81)90348-9
10.1074/jbc.273.45.29935
10.1021/la020002s
10.1021/ma00045a039
10.1038/370634a0
10.1529/biophysj.103.030072
10.1016/0021-9797(92)90506-H
10.1074/jbc.M001123200
10.1016/j.cis.2004.09.008
10.1098/rsif.2006.0172
10.1039/f19848000865
10.1038/414773a
10.1016/S0021-9258(18)35844-7
10.1093/glycob/cwm050
10.1073/pnas.0607852104
10.1529/biophysj.105.069344
10.1006/bbrc.2000.4146
10.1073/pnas.0307900100
10.1016/0021-9797(86)90278-X
10.1073/pnas.0604237103
10.1006/jmbi.1999.3310
10.1002/jbm.10215
10.1021/nl0712769
10.1126/science.248.4954.454
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Notes Address reprint requests to Bruno Zappone, E-mail: zappone@fis.unical.it.
Editor: Jane Clarke.
Bruno Zappone and Philipp J. Thurner contributed equally to this work.
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References Gupta, Seto, Wagermaier, Zaslansky, Boesecke, Fratzl (bib3) 2006; 103
Fisher, Torchia, Fohr, Young, Fedarko (bib7) 2001; 280
Weiner, Wagner (bib1) 1998; 28
Voros (bib18) 2004; 87
Claesson, Poptoshev, Blomberg, Dedinaite (bib27) 2005; 114
Pashley (bib29) 1981; 83
Lin, Gourdon, Sun, Holten-Andersen, Anderson, Waite, Israelachvili (bib12) 2007; 104
Israelachvili (bib16) 1991
Kamiyama, Israelachvili (bib24) 1992; 25
Raviv, Frey, Sak, Laurat, Tadmor, Klein (bib20) 2002; 18
Chen, Bal, Gorski (bib10) 1992; 267
Landman, Luedtke, Burnham, Colton (bib36) 1990; 248
Gupta, Fratzl, Kerschnitzki, Benecke, Wagermaier, Kirchner (bib6) 2007; 4
Israelachvili (bib15) 1973; 44
Perez, Proust (bib23) 1987; 118
Ball, Ramsden (bib17) 1998; 46
Flory (bib28) 1969
Fantner, Oroudjev, Schitter, Golde, Thurner, Finch, Turner, Gutsmann, Morse, Hansma, Hansma (bib11) 2006; 90
Johansen, Kiemer, Brunak (bib35) 2006; 16
Blom, Gammeltoft, Brunak (bib8) 1999; 294
Reference deleted in proof.
Monigatti, Gasteiger, Bairoch, Jung (bib39) 2002; 18
Gaines (bib22) 1956; 178
Luckham, Klein (bib19) 1984; 80
Fedarko, Fohr, Robey, Young, Fisher (bib13) 2000; 275
Israelachvili, McGuiggan (bib14) 1990; 5
Julenius, Molgaard, Gupta, Brunak (bib33) 2005; 15
Zappone, Ruths, Greene, Jay, Israelachvili (bib26) 2007; 92
Klein, Kumacheva, Mahalu, Perahia, Fetters (bib37) 1994; 370
Thompson, Kindt, Drake, Hansma, Morse, Hansma (bib4) 2001; 414
Fantner, Adams, Turner, Thurner, Fisher, Hansma (bib5) 2007; 7
Julenius (bib32) 2007; 17
Claesson, Herder, Stenius, Eriksson, Pashley (bib31) 1986; 109
Safran, Butler, Farach-Carson (bib9) 1998; 273
Leckband, Israelachvili (bib30) 2001; 34
Malmsten, Blomberg, Claesson, Carlstedt, Ljusegren (bib25) 1992; 151
Fantner, Hassenkam, Kindt, Weaver, Birkedal, Pechenik, Cutroni, Cidade, Stucky, Morse, Hansma (bib2) 2005; 4
Qiu, Wierzbicki, Orme, Cody, Hoyer, Nancollas, Zepeda, De Yoreo (bib38) 2004; 101
Tadmor, Chen, Israelachvili (bib21) 2002; 61
17645366 - Nano Lett. 2007 Aug;7(8):2491-8
17251154 - J R Soc Interface. 2007 Apr 22;4(13):277-82
1447223 - J Biol Chem. 1992 Dec 5;267(34):24871-8
15385431 - Glycobiology. 2005 Feb;15(2):153-64
14766970 - Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1811-5
15936291 - Adv Colloid Interface Sci. 2005 Jun 30;114-115:173-87
15240488 - Biophys J. 2004 Jul;87(1):553-61
12115441 - J Biomed Mater Res. 2002 Sep 15;61(4):514-23
11162539 - Biochem Biophys Res Commun. 2001 Jan 19;280(2):460-5
16762979 - Glycobiology. 2006 Sep;16(9):844-53
11742405 - Nature. 2001 Dec 13;414(6865):773-6
17494086 - Glycobiology. 2007 Aug;17(8):868-76
10600390 - J Mol Biol. 1999 Dec 17;294(5):1351-62
17360430 - Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3782-6
17095608 - Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17741-6
16025123 - Nat Mater. 2005 Aug;4(8):612-6
9792712 - J Biol Chem. 1998 Nov 6;273(45):29935-41
12050077 - Bioinformatics. 2002 May;18(5):769-70
17142292 - Biophys J. 2007 Mar 1;92(5):1693-708
17815594 - Science. 1990 Apr 27;248(4954):454-61
11771120 - Q Rev Biophys. 2001 May;34(2):105-267
10747989 - J Biol Chem. 2000 Jun 2;275(22):16666-72
16326907 - Biophys J. 2006 Feb 15;90(4):1411-8
Israelachvili (10.1529/biophysj.108.135889_bib16) 1991
Monigatti (10.1529/biophysj.108.135889_bib39) 2002; 18
Luckham (10.1529/biophysj.108.135889_bib19) 1984; 80
Leckband (10.1529/biophysj.108.135889_bib30) 2001; 34
Lin (10.1529/biophysj.108.135889_bib12) 2007; 104
Fisher (10.1529/biophysj.108.135889_bib7) 2001; 280
Raviv (10.1529/biophysj.108.135889_bib20) 2002; 18
Thompson (10.1529/biophysj.108.135889_bib4) 2001; 414
Klein (10.1529/biophysj.108.135889_bib37) 1994; 370
Fantner (10.1529/biophysj.108.135889_bib2) 2005; 4
Gaines (10.1529/biophysj.108.135889_bib22) 1956; 178
Fedarko (10.1529/biophysj.108.135889_bib13) 2000; 275
Johansen (10.1529/biophysj.108.135889_bib35) 2006; 16
Julenius (10.1529/biophysj.108.135889_bib32) 2007; 17
Perez (10.1529/biophysj.108.135889_bib23) 1987; 118
Israelachvili (10.1529/biophysj.108.135889_bib15) 1973; 44
Flory (10.1529/biophysj.108.135889_bib28) 1969
Landman (10.1529/biophysj.108.135889_bib36) 1990; 248
Gupta (10.1529/biophysj.108.135889_bib3) 2006; 103
Gupta (10.1529/biophysj.108.135889_bib6) 2007; 4
Julenius (10.1529/biophysj.108.135889_bib33) 2005; 15
Blom (10.1529/biophysj.108.135889_bib8) 1999; 294
Safran (10.1529/biophysj.108.135889_bib9) 1998; 273
Voros (10.1529/biophysj.108.135889_bib18) 2004; 87
Israelachvili (10.1529/biophysj.108.135889_bib14) 1990; 5
Ball (10.1529/biophysj.108.135889_bib17) 1998; 46
Malmsten (10.1529/biophysj.108.135889_bib25) 1992; 151
Claesson (10.1529/biophysj.108.135889_bib27) 2005; 114
Qiu (10.1529/biophysj.108.135889_bib38) 2004; 101
Chen (10.1529/biophysj.108.135889_bib10) 1992; 267
Fantner (10.1529/biophysj.108.135889_bib11) 2006; 90
Fantner (10.1529/biophysj.108.135889_bib5) 2007; 7
Kamiyama (10.1529/biophysj.108.135889_bib24) 1992; 25
Pashley (10.1529/biophysj.108.135889_bib29) 1981; 83
10.1529/biophysj.108.135889_bib34
Zappone (10.1529/biophysj.108.135889_bib26) 2007; 92
Claesson (10.1529/biophysj.108.135889_bib31) 1986; 109
Weiner (10.1529/biophysj.108.135889_bib1) 1998; 28
Tadmor (10.1529/biophysj.108.135889_bib21) 2002; 61
References_xml – year: 1991
  ident: bib16
  article-title: Intermolecular and Surface Forces
  contributor:
    fullname: Israelachvili
– volume: 92
  start-page: 1693
  year: 2007
  end-page: 1708
  ident: bib26
  article-title: Adsorption, lubrication, and wear of lubricin on model surfaces: polymer brush-like behavior of a glycoprotein
  publication-title: Biophys. J.
  contributor:
    fullname: Israelachvili
– volume: 83
  start-page: 531
  year: 1981
  end-page: 546
  ident: bib29
  article-title: DLVO and hydration forces between mica surfaces in Li
  publication-title: J. Colloid Interface Sci.
  contributor:
    fullname: Pashley
– volume: 118
  start-page: 182
  year: 1987
  end-page: 191
  ident: bib23
  article-title: Forces between mica surfaces covered with adsorbed mucin across aqueous solution
  publication-title: J. Colloid Interface Sci.
  contributor:
    fullname: Proust
– volume: 4
  start-page: 277
  year: 2007
  end-page: 282
  ident: bib6
  article-title: Evidence for an elementary process in bone plasticity with an activation enthalpy of 1
  publication-title: J. R. Soc. Interface
  contributor:
    fullname: Kirchner
– volume: 7
  start-page: 2491
  year: 2007
  end-page: 2498
  ident: bib5
  article-title: Nanoscale ion mediated networks in bone: osteopontin can repeatedly dissipate large amounts of energy
  publication-title: Nano Lett.
  contributor:
    fullname: Hansma
– volume: 414
  start-page: 773
  year: 2001
  end-page: 775
  ident: bib4
  article-title: Bone indentation recovery time correlates with bond reforming time
  publication-title: Nature
  contributor:
    fullname: Hansma
– volume: 25
  start-page: 5081
  year: 1992
  end-page: 5088
  ident: bib24
  article-title: Effect of pH and salt on the adsorption and interactions of an amphoteric polyelectrolyte
  publication-title: Macromolecules
  contributor:
    fullname: Israelachvili
– volume: 267
  start-page: 24871
  year: 1992
  end-page: 24878
  ident: bib10
  article-title: Calcium and collagen binding properties of osteopontin, bone sialoprotein, and bone acidic glycoprotein-75 from bone
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Gorski
– volume: 87
  start-page: 553
  year: 2004
  end-page: 561
  ident: bib18
  article-title: The density and refractive index of adsorbing protein layers
  publication-title: Biophys. J.
  contributor:
    fullname: Voros
– volume: 4
  start-page: 612
  year: 2005
  end-page: 616
  ident: bib2
  article-title: Sacrificial bonds and hidden length dissipate energy as mineralized fibrils separate during bone fracture
  publication-title: Nat. Mater.
  contributor:
    fullname: Hansma
– volume: 101
  start-page: 1811
  year: 2004
  end-page: 1815
  ident: bib38
  article-title: Molecular modulation of calcium oxalate crystallization by osteopontin and citrate
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: De Yoreo
– volume: 61
  start-page: 514
  year: 2002
  end-page: 523
  ident: bib21
  article-title: Thin film rheology and lubricity of hyaluronic acid solutions at a normal physiological concentration
  publication-title: J. Biomed. Mater. Res.
  contributor:
    fullname: Israelachvili
– year: 1969
  ident: bib28
  article-title: Statistical Mechanics of Chain Molecules
  contributor:
    fullname: Flory
– volume: 16
  start-page: 844
  year: 2006
  end-page: 853
  ident: bib35
  article-title: Analysis and prediction of mammalian protein glycation
  publication-title: Glycobiology
  contributor:
    fullname: Brunak
– volume: 80
  start-page: 865
  year: 1984
  end-page: 878
  ident: bib19
  article-title: Forces between mica surfaces bearing adsorbed polyelectrolyte, poly-L-lysine, in aqueous media
  publication-title: J. Chem. Soc., Faraday Trans. 1
  contributor:
    fullname: Klein
– volume: 370
  start-page: 634
  year: 1994
  end-page: 636
  ident: bib37
  article-title: Reduction of frictional forces between solid surfaces bearing polymer brushes
  publication-title: Nature
  contributor:
    fullname: Fetters
– volume: 44
  start-page: 259
  year: 1973
  end-page: 272
  ident: bib15
  article-title: Thin film studies using multiple-beam interferometry
  publication-title: J. Colloid Interface Sci.
  contributor:
    fullname: Israelachvili
– volume: 114
  start-page: 173
  year: 2005
  end-page: 187
  ident: bib27
  article-title: Polyelectrolyte-mediated surface interactions
  publication-title: Adv. Colloid Interface Sci.
  contributor:
    fullname: Dedinaite
– volume: 248
  start-page: 454
  year: 1990
  end-page: 461
  ident: bib36
  article-title: Atomistic mechanisms and dynamics of adhesion, nanoindentation, and fracture
  publication-title: Science
  contributor:
    fullname: Colton
– volume: 109
  start-page: 31
  year: 1986
  end-page: 39
  ident: bib31
  article-title: An ESCA and AES study of ion-exchange on the basal plane of mica
  publication-title: J. Colloid Interface Sci.
  contributor:
    fullname: Pashley
– volume: 178
  start-page: 1304
  year: 1956
  end-page: 1305
  ident: bib22
  article-title: Surface adhesion and elastic properties of mica
  publication-title: Nature
  contributor:
    fullname: Gaines
– volume: 294
  start-page: 1351
  year: 1999
  end-page: 1362
  ident: bib8
  article-title: Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Brunak
– volume: 5
  start-page: 2223
  year: 1990
  end-page: 2231
  ident: bib14
  article-title: Adhesion and short-range forces between surfaces. Part I: New apparatus for surface force measurements
  publication-title: J. Mater. Res.
  contributor:
    fullname: McGuiggan
– volume: 46
  start-page: 489
  year: 1998
  end-page: 492
  ident: bib17
  article-title: Buffer dependence of refractive index increments of protein solutions
  publication-title: Biopolymers
  contributor:
    fullname: Ramsden
– volume: 34
  start-page: 105
  year: 2001
  end-page: 267
  ident: bib30
  article-title: Intermolecular forces in biology
  publication-title: Q. Rev. Biophys.
  contributor:
    fullname: Israelachvili
– volume: 17
  start-page: 868
  year: 2007
  end-page: 876
  ident: bib32
  article-title: NetCGlyc 1.0: prediction of mammalian C-mannosylation sites
  publication-title: Glycobiology
  contributor:
    fullname: Julenius
– volume: 18
  start-page: 769
  year: 2002
  end-page: 770
  ident: bib39
  article-title: The sulfinator: predicting tyrosine sulfation sites in protein sequences
  publication-title: Bioinformatics
  contributor:
    fullname: Jung
– volume: 28
  start-page: 271
  year: 1998
  end-page: 298
  ident: bib1
  article-title: The material bone: structure mechanical function relations
  publication-title: Annu. Rev. Mater. Sci.
  contributor:
    fullname: Wagner
– volume: 273
  start-page: 29935
  year: 1998
  end-page: 29941
  ident: bib9
  article-title: Modulation of osteopontin post-translational state by 1, 25-(OH)2-vitamin D3. Dependence on Ca
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Farach-Carson
– volume: 104
  start-page: 3782
  year: 2007
  end-page: 3786
  ident: bib12
  article-title: Adhesion mechanism of the mussel foot proteins mfp-1 and mfp-3
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Israelachvili
– volume: 151
  start-page: 579
  year: 1992
  end-page: 590
  ident: bib25
  article-title: Mucin layers on hydrophobic surfaces studied with ellipsometry and surface force measurements
  publication-title: J. Colloid Interface Sci.
  contributor:
    fullname: Ljusegren
– volume: 90
  start-page: 1411
  year: 2006
  end-page: 1418
  ident: bib11
  article-title: Sacrificial bonds and hidden length: unraveling molecular mesostructures in tough materials
  publication-title: Biophys. J.
  contributor:
    fullname: Hansma
– volume: 18
  start-page: 7482
  year: 2002
  end-page: 7495
  ident: bib20
  article-title: Properties and interactions of physigrafted end-functionalized poly(ethylene glycol) layers
  publication-title: Langmuir
  contributor:
    fullname: Klein
– volume: 275
  start-page: 16666
  year: 2000
  end-page: 16672
  ident: bib13
  article-title: Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Fisher
– volume: 15
  start-page: 153
  year: 2005
  end-page: 164
  ident: bib33
  article-title: Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
  publication-title: Glycobiology
  contributor:
    fullname: Brunak
– volume: 103
  start-page: 17741
  year: 2006
  end-page: 17746
  ident: bib3
  article-title: Cooperative deformation of mineral and collagen in bone at the nanoscale
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Fratzl
– volume: 280
  start-page: 460
  year: 2001
  end-page: 465
  ident: bib7
  article-title: Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin
  publication-title: Biochem. Biophys. Res. Commun.
  contributor:
    fullname: Fedarko
– volume: 4
  start-page: 612
  year: 2005
  ident: 10.1529/biophysj.108.135889_bib2
  article-title: Sacrificial bonds and hidden length dissipate energy as mineralized fibrils separate during bone fracture
  publication-title: Nat. Mater.
  doi: 10.1038/nmat1428
  contributor:
    fullname: Fantner
– volume: 118
  start-page: 182
  year: 1987
  ident: 10.1529/biophysj.108.135889_bib23
  article-title: Forces between mica surfaces covered with adsorbed mucin across aqueous solution
  publication-title: J. Colloid Interface Sci.
  doi: 10.1016/0021-9797(87)90447-4
  contributor:
    fullname: Perez
– volume: 15
  start-page: 153
  year: 2005
  ident: 10.1529/biophysj.108.135889_bib33
  article-title: Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwh151
  contributor:
    fullname: Julenius
– volume: 18
  start-page: 769
  year: 2002
  ident: 10.1529/biophysj.108.135889_bib39
  article-title: The sulfinator: predicting tyrosine sulfation sites in protein sequences
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/18.5.769
  contributor:
    fullname: Monigatti
– volume: 16
  start-page: 844
  year: 2006
  ident: 10.1529/biophysj.108.135889_bib35
  article-title: Analysis and prediction of mammalian protein glycation
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwl009
  contributor:
    fullname: Johansen
– volume: 44
  start-page: 259
  year: 1973
  ident: 10.1529/biophysj.108.135889_bib15
  article-title: Thin film studies using multiple-beam interferometry
  publication-title: J. Colloid Interface Sci.
  doi: 10.1016/0021-9797(73)90218-X
  contributor:
    fullname: Israelachvili
– ident: 10.1529/biophysj.108.135889_bib34
– volume: 178
  start-page: 1304
  year: 1956
  ident: 10.1529/biophysj.108.135889_bib22
  article-title: Surface adhesion and elastic properties of mica
  publication-title: Nature
  doi: 10.1038/1781304b0
  contributor:
    fullname: Gaines
– volume: 5
  start-page: 2223
  year: 1990
  ident: 10.1529/biophysj.108.135889_bib14
  article-title: Adhesion and short-range forces between surfaces. Part I: New apparatus for surface force measurements
  publication-title: J. Mater. Res.
  doi: 10.1557/JMR.1990.2223
  contributor:
    fullname: Israelachvili
– volume: 92
  start-page: 1693
  year: 2007
  ident: 10.1529/biophysj.108.135889_bib26
  article-title: Adsorption, lubrication, and wear of lubricin on model surfaces: polymer brush-like behavior of a glycoprotein
  publication-title: Biophys. J.
  doi: 10.1529/biophysj.106.088799
  contributor:
    fullname: Zappone
– volume: 34
  start-page: 105
  year: 2001
  ident: 10.1529/biophysj.108.135889_bib30
  article-title: Intermolecular forces in biology
  publication-title: Q. Rev. Biophys.
  doi: 10.1017/S0033583501003687
  contributor:
    fullname: Leckband
– volume: 28
  start-page: 271
  year: 1998
  ident: 10.1529/biophysj.108.135889_bib1
  article-title: The material bone: structure mechanical function relations
  publication-title: Annu. Rev. Mater. Sci.
  doi: 10.1146/annurev.matsci.28.1.271
  contributor:
    fullname: Weiner
– volume: 46
  start-page: 489
  year: 1998
  ident: 10.1529/biophysj.108.135889_bib17
  article-title: Buffer dependence of refractive index increments of protein solutions
  publication-title: Biopolymers
  doi: 10.1002/(SICI)1097-0282(199812)46:7<489::AID-BIP6>3.0.CO;2-E
  contributor:
    fullname: Ball
– volume: 83
  start-page: 531
  year: 1981
  ident: 10.1529/biophysj.108.135889_bib29
  article-title: DLVO and hydration forces between mica surfaces in Li+, Na+, K+, and Cs+ electrolyte solutions: a correlation of double-layer and hydration forces with surface cation exchange properties
  publication-title: J. Colloid Interface Sci.
  doi: 10.1016/0021-9797(81)90348-9
  contributor:
    fullname: Pashley
– volume: 273
  start-page: 29935
  year: 1998
  ident: 10.1529/biophysj.108.135889_bib9
  article-title: Modulation of osteopontin post-translational state by 1, 25-(OH)2-vitamin D3. Dependence on Ca2+ influx
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.45.29935
  contributor:
    fullname: Safran
– volume: 18
  start-page: 7482
  year: 2002
  ident: 10.1529/biophysj.108.135889_bib20
  article-title: Properties and interactions of physigrafted end-functionalized poly(ethylene glycol) layers
  publication-title: Langmuir
  doi: 10.1021/la020002s
  contributor:
    fullname: Raviv
– volume: 25
  start-page: 5081
  year: 1992
  ident: 10.1529/biophysj.108.135889_bib24
  article-title: Effect of pH and salt on the adsorption and interactions of an amphoteric polyelectrolyte
  publication-title: Macromolecules
  doi: 10.1021/ma00045a039
  contributor:
    fullname: Kamiyama
– volume: 370
  start-page: 634
  year: 1994
  ident: 10.1529/biophysj.108.135889_bib37
  article-title: Reduction of frictional forces between solid surfaces bearing polymer brushes
  publication-title: Nature
  doi: 10.1038/370634a0
  contributor:
    fullname: Klein
– volume: 87
  start-page: 553
  year: 2004
  ident: 10.1529/biophysj.108.135889_bib18
  article-title: The density and refractive index of adsorbing protein layers
  publication-title: Biophys. J.
  doi: 10.1529/biophysj.103.030072
  contributor:
    fullname: Voros
– volume: 151
  start-page: 579
  year: 1992
  ident: 10.1529/biophysj.108.135889_bib25
  article-title: Mucin layers on hydrophobic surfaces studied with ellipsometry and surface force measurements
  publication-title: J. Colloid Interface Sci.
  doi: 10.1016/0021-9797(92)90506-H
  contributor:
    fullname: Malmsten
– volume: 275
  start-page: 16666
  year: 2000
  ident: 10.1529/biophysj.108.135889_bib13
  article-title: Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M001123200
  contributor:
    fullname: Fedarko
– volume: 114
  start-page: 173
  year: 2005
  ident: 10.1529/biophysj.108.135889_bib27
  article-title: Polyelectrolyte-mediated surface interactions
  publication-title: Adv. Colloid Interface Sci.
  doi: 10.1016/j.cis.2004.09.008
  contributor:
    fullname: Claesson
– volume: 4
  start-page: 277
  year: 2007
  ident: 10.1529/biophysj.108.135889_bib6
  article-title: Evidence for an elementary process in bone plasticity with an activation enthalpy of 1eV
  publication-title: J. R. Soc. Interface
  doi: 10.1098/rsif.2006.0172
  contributor:
    fullname: Gupta
– volume: 80
  start-page: 865
  year: 1984
  ident: 10.1529/biophysj.108.135889_bib19
  article-title: Forces between mica surfaces bearing adsorbed polyelectrolyte, poly-L-lysine, in aqueous media
  publication-title: J. Chem. Soc., Faraday Trans. 1
  doi: 10.1039/f19848000865
  contributor:
    fullname: Luckham
– volume: 414
  start-page: 773
  year: 2001
  ident: 10.1529/biophysj.108.135889_bib4
  article-title: Bone indentation recovery time correlates with bond reforming time
  publication-title: Nature
  doi: 10.1038/414773a
  contributor:
    fullname: Thompson
– volume: 267
  start-page: 24871
  year: 1992
  ident: 10.1529/biophysj.108.135889_bib10
  article-title: Calcium and collagen binding properties of osteopontin, bone sialoprotein, and bone acidic glycoprotein-75 from bone
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)35844-7
  contributor:
    fullname: Chen
– volume: 17
  start-page: 868
  year: 2007
  ident: 10.1529/biophysj.108.135889_bib32
  article-title: NetCGlyc 1.0: prediction of mammalian C-mannosylation sites
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwm050
  contributor:
    fullname: Julenius
– volume: 104
  start-page: 3782
  year: 2007
  ident: 10.1529/biophysj.108.135889_bib12
  article-title: Adhesion mechanism of the mussel foot proteins mfp-1 and mfp-3
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0607852104
  contributor:
    fullname: Lin
– volume: 90
  start-page: 1411
  year: 2006
  ident: 10.1529/biophysj.108.135889_bib11
  article-title: Sacrificial bonds and hidden length: unraveling molecular mesostructures in tough materials
  publication-title: Biophys. J.
  doi: 10.1529/biophysj.105.069344
  contributor:
    fullname: Fantner
– volume: 280
  start-page: 460
  year: 2001
  ident: 10.1529/biophysj.108.135889_bib7
  article-title: Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1006/bbrc.2000.4146
  contributor:
    fullname: Fisher
– year: 1969
  ident: 10.1529/biophysj.108.135889_bib28
  contributor:
    fullname: Flory
– volume: 101
  start-page: 1811
  year: 2004
  ident: 10.1529/biophysj.108.135889_bib38
  article-title: Molecular modulation of calcium oxalate crystallization by osteopontin and citrate
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0307900100
  contributor:
    fullname: Qiu
– volume: 109
  start-page: 31
  year: 1986
  ident: 10.1529/biophysj.108.135889_bib31
  article-title: An ESCA and AES study of ion-exchange on the basal plane of mica
  publication-title: J. Colloid Interface Sci.
  doi: 10.1016/0021-9797(86)90278-X
  contributor:
    fullname: Claesson
– volume: 103
  start-page: 17741
  year: 2006
  ident: 10.1529/biophysj.108.135889_bib3
  article-title: Cooperative deformation of mineral and collagen in bone at the nanoscale
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0604237103
  contributor:
    fullname: Gupta
– year: 1991
  ident: 10.1529/biophysj.108.135889_bib16
  contributor:
    fullname: Israelachvili
– volume: 294
  start-page: 1351
  year: 1999
  ident: 10.1529/biophysj.108.135889_bib8
  article-title: Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1999.3310
  contributor:
    fullname: Blom
– volume: 61
  start-page: 514
  year: 2002
  ident: 10.1529/biophysj.108.135889_bib21
  article-title: Thin film rheology and lubricity of hyaluronic acid solutions at a normal physiological concentration
  publication-title: J. Biomed. Mater. Res.
  doi: 10.1002/jbm.10215
  contributor:
    fullname: Tadmor
– volume: 7
  start-page: 2491
  year: 2007
  ident: 10.1529/biophysj.108.135889_bib5
  article-title: Nanoscale ion mediated networks in bone: osteopontin can repeatedly dissipate large amounts of energy
  publication-title: Nano Lett.
  doi: 10.1021/nl0712769
  contributor:
    fullname: Fantner
– volume: 248
  start-page: 454
  year: 1990
  ident: 10.1529/biophysj.108.135889_bib36
  article-title: Atomistic mechanisms and dynamics of adhesion, nanoindentation, and fracture
  publication-title: Science
  doi: 10.1126/science.248.4954.454
  contributor:
    fullname: Landman
SSID ssj0012501
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Snippet Using an atomic force microscope and a surface force apparatus, we measured the surface coverage, adhesion, and mechanical properties of layers of osteopontin...
SourceID pubmedcentral
crossref
pubmed
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 2939
SubjectTerms Adsorption - drug effects
Aluminum Silicates - metabolism
Biomechanical Phenomena
Buffers
Calcium - pharmacology
Humans
Microscopy, Atomic Force
Osteopontin - chemistry
Osteopontin - metabolism
Proteins
Sodium Hydroxide - chemistry
Surface Properties
Time Factors
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Title Effect of Ca2+ Ions on the Adhesion and Mechanical Properties of Adsorbed Layers of Human Osteopontin
URI https://dx.doi.org/10.1529/biophysj.108.135889
https://www.ncbi.nlm.nih.gov/pubmed/18586839
https://pubmed.ncbi.nlm.nih.gov/PMC2527241
Volume 95
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