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Updated: Jul 8, 2026

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
Published on: April 11, 2020
The structure, dynamics, and energetics of protein adsorption-lessons learned from adsorption of statherin to
Gil Goobes1, Rivka Goobes, Wendy J Shaw
1Department of Chemistry, University of Washington, Seattle, WA 98195, USA. Gil.Goobes@mail.biu.ac.il
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.
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