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首页> 外文期刊>Biochemistry >Spatially and Temporally Controlled Biomineralization Is Facilitated by Interaction between Self-Assembled Dentin Matrix Protein 1 and Calcium Phosphate Nuclei in Solution
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Spatially and Temporally Controlled Biomineralization Is Facilitated by Interaction between Self-Assembled Dentin Matrix Protein 1 and Calcium Phosphate Nuclei in Solution

机译：自组装的牙本质基质蛋白1和溶液中磷酸钙核之间的相互作用促进了时空控制的生物矿化

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Bone and dentin biomineralization are well-regulated processes mediated by extracellular matrix proteins.It is widely believed that specific matrix proteins in these tissues modulate nucleation of apatite nanoparticles and their growth into micrometer-sized crystals via molecular recognition at the protein-mineral interface.However,this assumption has been supported only circumstantially,and the exact mechanism remains unknown.Dentin matrix protein 1(DMP1)is an acidic matrix protein,present in the mineralized matrix of bone and dentin.In this study,we have demonstrated using synchrotron small-angle X-ray scattering that DMP1 in solution can undergo oligomerization and temporarily stabilize the newly formed calcium phosphate nanoparticle precursors by sequestering them and preventing their further aggregation and precipitation.The solution structure represents the first low-resolution structural information for DMP1.Atomic force microscopy and transmission electron microscopy studies further confirmed that the nascent calcium phosphate nuclei formed in solution were assembled into ordered protein-mineral complexes with the aid of oligomerized DMP1,recombinant and native.This study reveals a novel mechanism by which DMP1 might facilitate initiation of mineral nucleation at specific sites during bone and dentin mineralization and prevent spontaneous calcium phosphate precipitation in areas in which mineralization is not desirable.
机译：骨和牙本质的生物矿化作用是由细胞外基质蛋白介导的调节良好的过程，人们普遍认为，这些组织中的特定基质蛋白通过蛋白-矿物质界面上的分子识别来调节磷灰石纳米颗粒的成核并使其生长成微米级的晶体。 Dentin基质蛋白1（DMP1）是一种酸性基质蛋白，存在于骨骼和牙本质的矿化基质中。在本研究中，我们证明了使用同步加速器小分子角度X射线散射表明溶液中的DMP1可以低聚并通过螯合它们并防止其进一步聚集和沉淀来暂时稳定新形成的磷酸钙纳米颗粒前体。溶液结构代表了DMP1的第一个低分辨率结构信息。和透射电子显微镜的研究rther证实，在低聚的DMP1（重组的和天然的）的帮助下，溶液中形成的新生磷酸钙核被组装成有序的蛋白质-矿物复合物。这项研究揭示了一种新的机制，DMP1可以通过这种机制促进骨骼中特定部位的矿物成核的启动牙本质矿化，并防止在不需要矿化的区域自发沉淀磷酸钙。

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