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

• Published in: Magnetic resonance in chemistry Vol. 45; no. S1; pp. S32 - S47
• Main Authors: Goobes, Gil, Goobes, Rivka, Shaw, Wendy J., Gibson, James M., Long, Joanna R., Raghunathan, Vinodhkumar, Schueler-Furman, Ora, Popham, Jennifer M., Baker, David, Campbell, Charles T., Stayton, Patrick S., Drobny, Gary P.
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.12.2007
• Subjects: Adsorption; Bacterial Adhesion; Calcification, Physiologic; calorimetry; Crystallization; Dental Pellicle - chemistry; Durapatite - chemistry; Humans; Kinetics; magic angle spinning; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; protein; recoupling; Saliva - chemistry; Salivary Proteins and Peptides - chemistry; solid-state NMR; Staining and Labeling; structure; Surface Properties; Thermodynamics
• ISSN: 0749-1581; 1097-458X
• DOI: 10.1002/mrc.2123

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.