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The structure, dynamics, and energetics of protein adsorption—lessons learned from adsorption of statherin to hydroxyapatite

  1. Gil Goobes1,†,*,
  2. Rivka Goobes2,
  3. Wendy J. Shaw1,‡,
  4. James M. Gibson2,§,
  5. Joanna R. Long2,¶,
  6. Vinodhkumar Raghunathan1,
  7. Ora Schueler-Furman3,‖,
  8. Jennifer M. Popham1,
  9. David Baker3,
  10. Charles T. Campbell1,
  11. Patrick S. Stayton2,
  12. Gary P. Drobny1,*

Article first published online: 3 JAN 2008

DOI: 10.1002/mrc.2123

Issue

Magnetic Resonance in Chemistry

Magnetic Resonance in Chemistry

Special Issue: New techniques in solid-state NMR

Volume 45, Issue S1, pages S32–S47, December 2007

Additional Information

How to Cite

Goobes, G., Goobes, R., Shaw, W. J., Gibson, J. M., Long, J. R., Raghunathan, V., Schueler-Furman, O., Popham, J. M., Baker, D., Campbell, C. T., Stayton, P. S. and Drobny, G. P. (2007), The structure, dynamics, and energetics of protein adsorption—lessons learned from adsorption of statherin to hydroxyapatite. Magn. Reson. Chem., 45: S32–S47. doi: 10.1002/mrc.2123

Author Information

  1. 1

    Department of Chemistry, University of Washington, Seattle WA 98195, USA

  2. 2

    Department of Bioengineering, University of Washington, Seattle WA 98195, USA

  3. 3

    Department of Biochemistry, University of Washington, Seattle WA 98195, USA

  1. †

    Department of Chemistry, BarIlan University, Ramat Gan 52900, Israel.

  2. ‡

    Pacific Northwest National Laboratory, Richland, WA 99352, USA

  3. §

    Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, USA

  4. Department of Biochemistry and Molecular Biology, McKnight Brain Institute, University of Florida, Gainesville, FA 32610, USA

  5. ‖

    Department of Molecular Genetics and Biotechnology, Hebrew University, Hadassah Medical School, Jerusalem 91120, Israel

*Department of Chemistry, University of Washington, Box 351700, Seattle WA 98195, USA.

Publication History

  1. Issue published online: 3 JAN 2008
  2. Article first published online: 3 JAN 2008
  3. Manuscript Accepted: 1 OCT 2007
  4. Manuscript Revised: 27 SEP 2007
  5. Manuscript Received: 23 JUL 2007

Funded by

  • NSF. Grant Numbers: EEC 9529161, DMR 0110505
  • NIH
  • National Dental Institute. Grant Number: RO1 DE-12554
  • Institute of General Medicine. Grant Number: RO1 GM074511

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Keywords:

  • solid-state NMR;
  • protein;
  • structure;
  • adsorption;
  • recoupling;
  • magic angle spinning;
  • calorimetry

Abstract

Proteins are found to be involved in interaction with solid surfaces in numerous natural events. Acidic proteins that adsorb to crystal faces of a biomineral to control the growth and morphology of hard tissue are only one example. Deducing the mechanisms of surface recognition exercised by proteins has implications to osteogenesis, pathological calcification and other proteins functions at their adsorbed state. Statherin is an enamel pellicle protein that inhibits hydroxyapatite nucleation and growth, lubricates the enamel surface, and is recognized by oral bacteria in periodontal diseases. Here, we highlight some of the insights we obtained recently using both thermodynamic and solid state NMR measurements to the adsorption process of statherin to hydroxyapatite. We combine macroscopic energy characterization with microscopic structural findings to present our views of protein adsorption mechanisms and the structural changes accompanying it and discuss the implications of these studies to understanding the functions of the protein adsorbed to the enamel surfaces. Copyright © 2007 John Wiley & Sons, Ltd.

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