多级有序矿化胶原纤维的仿生构建-材料学专业论文.docxVIP

暨南大 暨南大学硕士学位论文 II II Abstract Natural bone is composed of mineralized collagen fiber with hierarchical structure. The development of mineralized collagen was supposed to “be tuned by organic matrix” according to the present studies. However, there is no authoritative theory about the principle of mineralization about bone, and the process also is difficult to mimick in vitro. Research on the biomimetic construction of mineralized collagen systematically will benefit to grasp the mechanism of biomineralization, also benefit to the development of the repairing material and regeneration material of bone. In the study, the orderly template for mineralization self-assembled with self-made type I collagen from rat-tail was to establish. Self-made EMPs (Enamel Matrix Proteins) from pig, DMP1 (Dentin Matrix Protein 1), PAA (PolyAcrylic Acid), TPP (Tripolyphosphate) and β-GP (Beta-glycerophosphate) were used as inducing factors, and SBF (Simulated Body Fluid ) and PBS ( Phosphate Buffer Solution)-CaCl2 solution worked as biomimetic solution. The experiments of biomimetic construct were carried out under 37.5℃. POM, AFM, FSEM were used to observe the microstructure of the products and XRD characterized the phase species. Under the tune of PAA, a hierarchical structure from nanoscale to micro-scale composed by the ordered mineralized collgen fiber was obtained, also together with qusia-bone period ribbon construct in the collagen fiber. The mineralized collagen fibres kept highly ordered structure with unified size even in the microscale level, which verified the mechanism of PILP (Polymer Inducing Liquid Process) on bone formation in some degree. TPP and β-GP had strong ability to inducing the formation of nucleator in the biomimetic solution, while its ability to tuning collagen mineralization was suffered to limited. So, when TPP and β-GP worked as inducing factors, mineralized collgen composite fibre still can keep its ordered structure in nanosacle level. Be