Abstract
Dental cementum contains unique molecules that regulate the mineralization process in vitro and in vivo, such as cementum protein 1 (CEMP1). This protein possesses amino acid sequence motifs like the human recombinant CEMP1 with biological activity. This novel cementum protein 1-derived peptide (CEMP1-p3, from the CEMP1’s N-terminal domain: (QPLPKGCAAVKAEVGIPAPH), consists of 20 amino acids. Hydroxyapatite (HA) crystals could be obtained through the combination of the amorphous precursor phase and macromolecules such as proteins and peptides. We used a simple method to synthesize peptide/hydroxyapatite nanocomposites using OCP and CEMP1-p3. The characterization of the crystals through scanning electron microscopy (SEM), powder X-ray diffraction (XRD), high--resolution transmission electron microscopy (HRTEM), and Raman spectroscopy revealed that CEMP1-p3 transformed OCP into hydroxyapatite (HA) under constant ionic strength and in a buffered solution. CEMP1-p3 binds and highly adsorbs to OCP and is a potent growth stimulator of OCP crystals. CEMP1-p3 fosters the transformation of OCP into HA crystals with crystalline planes (300) and (004) that correspond to the cell of hexagonal HA. Octacalcium phosphate crystals treated with CEMP1-p3 grown in simulated physiological buffer acquired hexagonal arrangement corresponding to HA. These findings provide new insights into the potential application of CEMP1-p3 on possible biomimetic approaches to generate materials for the repair and regeneration of mineralized tissues, or restorative materials in the orthopedic field.
Highlights
Cementum is a mineralized tissue that covers the root; it possesses unique molecules that promote cell proliferation and differentiation of periodontal ligament cells [1]. One of these molecules; cementum protein 1 (CEMP1), which is synthesized by cementoblasts, nucleates hydroxyapatite crystals in vitro [2]
Octacalcium phosphate crystalizes in the triclinic system, with P-1Ci 1 group
We observed through the laser confocal microscopy that as the peptide concentration in the solution increases, it binds to the surface of the octacalcium phosphate (OCP) crystal
Summary
Cementum is a mineralized tissue that covers the root; it possesses unique molecules that promote cell proliferation and differentiation of periodontal ligament cells [1] One of these molecules; cementum protein 1 (CEMP1), which is synthesized by cementoblasts, nucleates hydroxyapatite crystals in vitro [2]. Human recombinant CEMP1 plays a role in the development of the periodontium, which surrounds and supports the teeth by promoting the differentiation of multipotent cells from the periodontal ligament into cementoblasts that form cementum [1,5,6]. It binds hydroxyapatite and may promote the biomineralization of cementum [7]. The control of crystal nucleation and growth has Crystals 2020, 10, 1131; doi:10.3390/cryst10121131 www.mdpi.com/journal/crystals
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