Mineralization of calcium phosphate controlled by biomimetic self-assembled peptide monolayers via surface electrostatic potentials.
basic_science · Level V
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- Record sourced from PubMed, PMID 32258828.
- Also identified by DOI 10.1016/j.bioactmat.2020.03.003 and PMC identifier 7113442.
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Abstract
The functions of acidic-rich domains in non-collagenous protein during biomineralization are thought to induce nucleation and control the growth of hydroxyapatite. The tripeptide Asp-Ser-Ser (DSS) repeats are the most common acidic-rich repeated unit in non-collagenous protein of dentin phosphoprotein, the functions of which have aroused extensive interests. In this study, biomimetic peptides (DSS)<sub>n</sub> (n = 2 or 3) were designed and fabricated into self-assembled monolayers (SAMs) on Au (111) surface as biomimetic organic templates to regulate hydroxyapatite (HAp) mineralization in 1.5 simulated body fluid (1.5 SBF) at 37 °C. The early mineralization processes and minerals deposited on the SAMs were characterized by X-ray diffraction, scanning electron microscope, and Fourier transform infrared spectroscopy analyses. The SAM-DSS9/DSS9G showed the highest capacity to induce HAp nucleation and growth, followed by SAM-DSS6/DSS6G, SAM-COOH, and SAM-OH. The SAM-(DSS)<sub>n</sub> had more negative zeta potentials than SAM-COOH surface, indicating that DSS repeats contributed to the biomineralization, which not only provided strong affinity with Ca<sup>2+</sup> ions through direct electrostatic bonds, but more importantly influence surface electrostatic potentials of the assembled organic template for nucleation.