Public Lecture by Paul Anderson, Queen Mary University of London, UK

Bio-sketch of  Paul Anderson

Paul Anderson  BSc (Biophysics, Leeds)  PhD (Biophysics, London)
Email : p.anderson@qmul.ac.uk
Reader in Biophysics in relation to Dentistry
Institute of Dentistry
Queen Mary University of London, UK

The Role of Salivary Proteins particularly Statherin in Enamel Homeostasis – Molecular Dentistry

Saliva contains over one thousand proteins. Some of these including cystatin, the histatins, and proline-rich proteins (PRPs) are involved in prevention of mineral precipitation within the supersaturated environment of the oral cavity. Another salivary protein statherin may also be involved in reducing enamel dissolution, by interfering directly with the dissolution processes on hydroxyapatite surfaces. At the molecular level, statherin inhibits the kinetics of hydroxyapatite and enamel dissolution by binding to its surface, acquiring structure, and then preventing the congregation and enlargement of dissolution sites on the hydroxyapatite surfaces.  At the whole tooth level, statherin significantly reduces the progress of enamel dissolution, and therefore the development of dental caries within the oral environment. In vitro X-ray absorption studies were used to show that statherin, when applied to enamel and hydroxyapatite surfaces at concentrations similar to those found in saliva, reduced the rate of demineralisation by up to 45%. The molecular architecture of statherin is imposed by a particular crystal face of a hydroxyapatite surface, conferring structure to the protein resulting in its cariostatic function. It is likely that further “molecular dentistry” using drug design techniques will be required to engineer similar peptides which will have superior cariostatic function, and therefore better clinical outcomes for patients.