Dentistry Publications
Title
Histatin 1 Resists Proteolytic Degradation When Adsorbed to Hydroxyapatite
Document Type
Article
Publication Date
2-2011
Journal
Journal of Dental Research
Volume
90
Issue
2
First Page
268
Last Page
272
URL with Digital Object Identifier
http://dx.doi.org/10.1177/0022034510388653
Abstract
Histatins are salivary proteins that exhibit a high affinity for hydroxyapatite and contribute to the acquired enamel pellicle. Previous studies have observed that, despite the high proteolytic activity in saliva, significant numbers of histatin molecules in acquired enamel pellicle are intact. Our working hypothesis was that histatins are less susceptible to proteinases present in saliva when adsorbed on the hydroxyapatite. To test this premise, we incubated histatin 1 with hydroxyapatite and human whole saliva. Proteolytic products of this incubation were then characterized by PAGE, HPLC, and mass spectrometry. This study shows for the first time that binding to hydroxyapatite confers intact histatin 1 with resistance to proteolytic degradation.
