Next Article in Journal
Characterization of Mechanical and Bactericidal Properties of Cement Mortars Containing Waste Glass Aggregate and Nanomaterials
Next Article in Special Issue
Fabrication and Physical Evaluation of Gelatin-Coated Carbonate Apatite Foam
Previous Article in Journal
Transverse Crack Detection in 3D Angle Interlock Glass Fibre Composites Using Acoustic Emission
Open AccessArticle

Identification of Specific Hydroxyapatite {001} Binding Heptapeptide by Phage Display and Its Nucleation Effect

Department of Stomatology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China
Author to whom correspondence should be addressed.
These authors contributed equally to the work.
Academic Editor: Patrice Laquerriere
Materials 2016, 9(8), 700;
Received: 4 August 2016 / Revised: 12 August 2016 / Accepted: 15 August 2016 / Published: 17 August 2016
(This article belongs to the Special Issue Calcium Phosphate in Biomedical Applications)
With recent developments of molecular biomimetics that combine genetic engineering and nanotechnology, peptides can be genetically engineered to bind specifically to inorganic components and execute the task of collagen matrix proteins. In this study, using biogenous tooth enamel as binding substrate, we identified a new heptapeptide (enamel high-affinity binding peptide, EHBP) from linear 7-mer peptide phage display library. Through the output/input affinity test, it was found that EHBP has the highest affinity to enamel with an output/input ratio of 14.814 × 10−7, while a random peptide (RP) displayed much lower output/input ratio of 0.00035 × 10−7. This binding affinity was also verified by confocal laser scanning microscopy (CLSM) analysis. It was found that EHBP absorbing onto the enamel surface exhibits highest normalized fluorescence intensity (5.6 ± 1.2), comparing to the intensity of EHBP to enamel longitudinal section (1.5 ± 0.9) (p < 0.05) as well as to the intensity of a low-affinity binding peptide (ELBP) to enamel (1.5 ± 0.5) (p < 0.05). Transmission electron microscopy (TEM), Attenuated total Reflection-Fourier transform infrared spectroscopy (ATR-FTIR), and X-ray Diffraction (XRD) studies further confirmed that crystallized hydroxyapatite were precipitated in the mineralization solution containing EHBP. To better understand the nucleation effect of EHBP, EHBP was further investigated on its interaction with calcium phosphate clusters through in vitro mineralization model. The calcium and phosphate ion consumption as well as zeta potential survey revealed that EHBP might previously adsorb to phosphate (PO43−) groups and then initiate the precipitation of calcium and phosphate groups. This study not only proved the electrostatic interaction of phosphate group and the genetically engineering solid-binding peptide, but also provided a novel nucleation motif for potential applications in guided hard tissue biomineralization and regeneration. View Full-Text
Keywords: biomimetic; biomineralization; hydrxyapatite; solid-binding peptide biomimetic; biomineralization; hydrxyapatite; solid-binding peptide
Show Figures

Graphical abstract

MDPI and ACS Style

Mao, J.; Shi, X.; Wu, Y.-B.; Gong, S.-Q. Identification of Specific Hydroxyapatite {001} Binding Heptapeptide by Phage Display and Its Nucleation Effect. Materials 2016, 9, 700.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop