Skip to main content
SpringerLink
Log in

Analysis of Hydroxyapatite Surface Coverage by Amelogenin Nanospheres Following the Langmuir Model for Protein Adsorption

  • Published:
Calcified Tissue International Aims and scope Submit manuscript

Abstract

The assembly of amelogenin protein into nanospheres is postulated to be a key factor in the stability of enamel extracellular matrix framework, which provides the scaffolding for the initial enamel apatite crystals to nucleate and grow. Adsorption isotherms were evaluated in order to investigate the nature of interactions of amelogenin nanospheres with hydroxyapaite crystals in solution, where their assembly status and particle size distribution are defined. We report that the adsorption isotherm of a recombinant mouse amelogenin (rM179) on synthetic hydroxyapatite crystals can be described using a Langmuir model indicating that amelogenin nanospheres adsorb onto the surface of apatite crystals as binding units with defined adsorption sites. The adsorption affinity and the maximum adsorption sites were 19.7 × 105 L/mol and 6.09 × 10−7 mol/m2, respectively, with an r 2 value of 0.99. Knowing the composition and particle size distribution of amelogenin nanospheres under the condition of adsorption experiments, we have calculated the number of nanospheres and the crystal surface area covered by each population of nanospheres at their maximum adsorption. It was found that total maximum binding covers 64% of the area unit. This observation supports the speculation that amelogenin binding onto apatite surface is selective and occurs only at certain sites.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Subscribe and save

Springer+ Basic
$34.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or eBook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. H Lowenstam S Weiner (1989) On Biomineralization. Oxford University Press New York 175

    Google Scholar 

  2. A Fincham J Moradian–Oldak J Simmer (1999) ArticleTitleThe structural biology of the developing dental enamel matrix. J Struct Biol 126 270–299 Occurrence Handle10.1006/jsbi.1999.4130 Occurrence Handle1:CAS:528:DyaK1MXltVagt7Y%3D Occurrence Handle10441532

    Article  CAS  PubMed  Google Scholar 

  3. J Kirkham S Brookes R Shore S Wood D Smith J Zhang H Chen C Robinson (2002) ArticleTitlePhysico-chemical properties of crystal surfaces in matrix–mineral interactions during mammalian biomineralisation. Curr Opin Colloid Interface Sci 7 124–132 Occurrence Handle10.1016/S1359-0294(02)00017-1 Occurrence Handle1:CAS:528:DC%2BD38XjslOnsr8%3D

    Article  CAS  Google Scholar 

  4. ML Paine SN White W Luo H Fong M Sarikaya ML Snead (2001) ArticleTitleRegulated gene expression dictates enamel structure and tooth function. Matrix Biol 20 273–292 Occurrence Handle10.1016/S0945-053X(01)00153-6 Occurrence Handle1:CAS:528:DC%2BD3MXmvVKqsbs%3D Occurrence Handle11566262

    Article  CAS  PubMed  Google Scholar 

  5. A Fincham J Moradian–Oldak J Simmer P Sarte E Lau T Diekwisch H Slavkin (1994) ArticleTitleSelf-assembly of a recombinant amelogenin protein generates supramolecular structures. J Struct Biol 112 103–109 Occurrence Handle10.1006/jsbi.1994.1011 Occurrence Handle1:CAS:528:DyaK2MXktlyquw%3D%3D Occurrence Handle8060728

    Article  CAS  PubMed  Google Scholar 

  6. A Fincham J Moradian–Oldak T Diekwisch D Lyaruu J Wright P Bringas Jr H Slavkin (1995) ArticleTitleEvidence for amelogenin “nanospheres” as functional components of secretory-stage enamel matrix. J Struct Biol 115 50–59 Occurrence Handle10.1006/jsbi.1995.1029 Occurrence Handle1:CAS:528:DyaK2MXpt1ykurc%3D Occurrence Handle7577231

    Article  CAS  PubMed  Google Scholar 

  7. H Wen A Fincham J Moradian–Oldak (2001) ArticleTitleProgressive accretion of amelogenin molecules during nanospheres assembly revealed by atomic force microscopy. Matrix Biol 20 387–395 Occurrence Handle10.1016/S0945-053X(01)00144-5 Occurrence Handle1:CAS:528:DC%2BD3MXmvVKqtrg%3D Occurrence Handle11566273

    Article  CAS  PubMed  Google Scholar 

  8. J Moradian–Oldak N Bouropoulos L Wang N Gharakhanian (2002) ArticleTitleAnalysis of self-assembly and apatite binding properties of amelogenin proteins lacking the hydrophilic C-terminal. Matrix Biol 21 197–205 Occurrence Handle10.1016/S0945-053X(01)00190-1 Occurrence Handle1:CAS:528:DC%2BD38XhtlGntrc%3D Occurrence Handle11852235

    Article  CAS  PubMed  Google Scholar 

  9. M Iijima Y Moriwaki H Wen A Fincham J Moradian–Oldak (2002) ArticleTitleElongated growth of octacalcium phosphate crystals in recombinant amelogenin gels under controlled ionic flow. J Dental Res 81 69–73 Occurrence Handle1:CAS:528:DC%2BD38XnvFemtA%3D%3D

    CAS  Google Scholar 

  10. M Iijima Y Moriwaki T Takagi J Moradian–Oldak (2001) ArticleTitleEffects of bovine amelogenins on the crystal morphology of octacalcium phosphate in a model system of tooth enamel formation. J Cryst Growth 222 615–626 Occurrence Handle10.1016/S0022-0248(00)00984-2 Occurrence Handle1:CAS:528:DC%2BD3MXksFKjuw%3D%3D

    Article  CAS  Google Scholar 

  11. T Aoba M Fukae T Tanabe M Shimizu E Moreno (1987) ArticleTitleSelective adsorption of porcine-amelogenins onto hydroxyapatite and their inhibitory activity on hydroxyapatite growth in supersaturated solutions. Calcif Tissue Int 41 281–289 Occurrence Handle1:CAS:528:DyaL1cXhsVOqt7w%3D Occurrence Handle2825935

    CAS  PubMed  Google Scholar 

  12. J Simmer E Lau et al. (1994) ArticleTitleIsolation and characterization of a mouse amelogenin expressed in Escherichia coli. Calcif Tissue Int 54 312–319

    Google Scholar 

  13. O Ryu C Hu J Simmer (1998) ArticleTitleBiochemical characterization of recombinant mouse amelogenins: protein quantitation, proton absorption, and relative affinity for enamel crystals. Connect Tissue Res 39 207–214 Occurrence Handle11063001

    PubMed  Google Scholar 

  14. H Nagadome H Margolis (2002) ArticleTitleAdsorption of recombinant amelogenins onto hydroxyapatite. J Dent Res 81 (special issue) abstract 2501

    Google Scholar 

  15. M Wallwork J Kirkham J Zhang S Brookes R Shore S Wood O Ryu C Robinson DA Smith (2001) ArticleTitleBinding of matrix proteins to developing enamel crystals: An Atomic Force Microscopy study. Langmuir 17 2508–2513 Occurrence Handle10.1021/la001281r Occurrence Handle1:CAS:528:DC%2BD3MXhslSrtbo%3D

    Article  CAS  Google Scholar 

  16. J Moradian–Oldak J Tan AG Fincham (1998) ArticleTitleInteraction of amelogenin with hydroxyapatite crystals: an adherence effect through amelogenin self-association. Biopolymers 46 225–238 Occurrence Handle10.1002/(SICI)1097-0282(19981005)46:4<225::AID-BIP4>3.0.CO;2-R Occurrence Handle1:CAS:528:DyaK1cXlsVSktr0%3D Occurrence Handle9715666

    Article  CAS  PubMed  Google Scholar 

  17. Y Doi ED Eanes H Shimokawa JD Termine (1984) ArticleTitleInhibition of seeded growth of enamel apatite crystals by amelogenin and enamelin proteins in vitro. J Dent Res 63 98–105 Occurrence Handle1:CAS:528:DyaL2cXhtlKmu7s%3D Occurrence Handle6582100

    CAS  PubMed  Google Scholar 

  18. GK Hunter HA Curtis MD Grynpas JP Simmer AG Fincham (1998) ArticleTitleEffects of recombinant amelogenin on hydroxyapatite formation in vitro. Calcif Tissue Int 65 226–231 Occurrence Handle10.1007/s002239900688

    Article  Google Scholar 

  19. J Moradian–Oldak JP Simmer EC Lau PE Sarte HC Slavkin AG Fincham (1994) ArticleTitleDetection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering. Biopolymers 34 1339–1347 Occurrence Handle1:CAS:528:DyaK2cXmsFShs7g%3D Occurrence Handle7948720

    CAS  PubMed  Google Scholar 

  20. A Fincham J Moradian–Oldak (1993) ArticleTitleAmelogenin post-translational modifications: carboxy-terminal processing and the phosphorylation of bovine and porcine “TRAP” and “LRAP” amelogenins. Biochem Biophys Res Commun 197 248–255 Occurrence Handle10.1006/bbrc.1993.2468 Occurrence Handle1:CAS:528:DyaK2cXhvVGmtLw%3D Occurrence Handle8250931

    Article  CAS  PubMed  Google Scholar 

  21. M Kresak E Moreno R Zahradnik D Hay (1977) ArticleTitleAdsorption of aminoacids onto hydroxyapatite. J Colloid Interface Sci 59 283–292 Occurrence Handle1:CAS:528:DyaE2sXhvVCks7s%3D

    CAS  Google Scholar 

  22. C Richardson M Johnsson P Raj M Levine G Nancollas (1993) ArticleTitleThe influence of histatin-5 fragments on the mineralization of hydroxyapatite. Arch Oral Biol 38 997–1002 Occurrence Handle10.1016/0003-9969(93)90113-Z Occurrence Handle1:CAS:528:DyaK2cXivFGhs78%3D Occurrence Handle8297263

    Article  CAS  PubMed  Google Scholar 

  23. V Hlady H Fueredi–Milhofer (1979) ArticleTitleAdsorption of human serum albumin on precipitated hydroxyapatite. J Colloid Interface Sci 69 460–468 Occurrence Handle1:CAS:528:DyaE1MXksFWgtb0%3D

    CAS  Google Scholar 

  24. M Johnsson M Levine G Nancollas (1993) ArticleTitleHydroxyapatite binding domains in salivary proteins. Crit Rev Oral Biol Med 4 371–378 Occurrence Handle1:STN:280:ByyA1crjvFA%3D Occurrence Handle8396998

    CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, 2250 Alcazar St. CSA, Los Angeles, CA 90033, USA

    N. Bouropoulos & J. Moradian–Oldak

Authors
  1. N. Bouropoulos
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. J. Moradian–Oldak
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to J. Moradian–Oldak.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Bouropoulos, N., Moradian–Oldak, J. Analysis of Hydroxyapatite Surface Coverage by Amelogenin Nanospheres Following the Langmuir Model for Protein Adsorption . Calcif Tissue Int 72, 599–603 (2003). https://doi.org/10.1007/s00223-002-1099-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00223-002-1099-1

Keywords

Search

Navigation