The structure, dynamics, and energetics of protein adsorption - Lessons learned from adsorption of statherin to hydroxyapatite

Gil Goobes*, Rivka Goobes, Wendy J. Shaw, James M. Gibson, Joanna R. Long, Vinodhkumar Raghunathan, Ora Schueler-Furman, Jennifer M. Popham, David Baker, Charles T. Campbell, Patrick S. Stayton, Gary P. Drobny

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

45 Scopus citations

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.

Original languageAmerican English
Pages (from-to)S32-S47
JournalMagnetic Resonance in Chemistry
Volume45
Issue numberSUPPL.
DOIs
StatePublished - Dec 2007

Keywords

  • Adsorption
  • Calorimetry
  • Magic angle spinning
  • Protein
  • Recoupling
  • Solid-state NMR
  • Structure

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