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Rapid Mix Preparation of Bioinspired Nanoscale Hydroxyapatite for Biomedical Applications
Published on: February 23, 2017
Histatin 1 resists proteolytic degradation when adsorbed to hydroxyapatite
E E McDonald1, H A Goldberg, N Tabbara
1School of Dentistry, Dental Sciences Building-DSB0071, Schulich School of Medicine & Dentistry, The University of Western Ontario, London N6A 5C1, ON, Canada.
Journal of Dental Research
|November 16, 2010
Summary
Histatins, salivary proteins, resist breakdown by saliva enzymes when bound to hydroxyapatite. This binding protects intact histatin molecules within the acquired enamel pellicle.
Area of Science:
- Oral biology
- Biochemistry
- Proteomics
Background:
- Histatins are salivary proteins crucial for the acquired enamel pellicle.
- Saliva contains high proteolytic activity, yet intact histatins are found in the pellicle.
- This suggests a protective mechanism for histatins in the oral environment.
Purpose of the Study:
- To investigate the hypothesis that hydroxyapatite binding protects histatins from salivary proteolysis.
- To elucidate the stability of histatin 1 when adsorbed onto hydroxyapatite in the presence of saliva.
Main Methods:
- Incubation of histatin 1 with hydroxyapatite and human whole saliva.
- Characterization of proteolytic degradation products using PAGE, HPLC, and mass spectrometry.
Main Results:
- Histatin 1 bound to hydroxyapatite demonstrated significant resistance to proteolytic degradation by saliva.
- This is the first study to demonstrate hydroxyapatite-mediated protection of histatin 1 against salivary proteinases.
Conclusions:
- Hydroxyapatite binding confers resistance to proteolytic degradation on histatin 1.
- This mechanism contributes to the stability and function of histatins in the acquired enamel pellicle.
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