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Collagen modulating crystallization of apatite in a biomimetic gel system

机译:在仿生凝胶系统中胶原蛋白调节磷灰石的结晶

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Apatite crystals were formed at 37 °C in a biomimetic gel system with the presence and absence of collagen under pH 6.5, 7.0 and 7.5 respectively. X-ray diffraction, transmission electron microscope and selected area electron diffraction pattern were applied to characterize the crystals. The results indicated that collagen modulate crystallization of apatite both in composition and morphology. With the absence of collagen, the obtained crystals were ribbon-shaped octacalcium phosphate (OCP) at pH 6.5, the mixture of OCP and nanosize rod-shaped hydroxyapatite (HAP) at pH 7.0 and 7.5 respectively. OCP would be a precursor of HAP with the absence of collagen. With the presence of collagen, collagen acted more effectively in controlling crystallization of HAP than pH did in the system. Ribbon-shaped HAP was the main phase at pH 6.5, kept a very thin structure at pH 7.0 while the needle-shaped HAP with several nanometers in diameter was obtained at pH 7.5. It was discussed amorphous calcium phosphate would be an intermediate phase of HAP with the presence of collagen. Such understanding of collagen and pH control on biomineralization gives new insights on the controlled synthesis of apatite.
机译:在仿生凝胶系统中,于37°C形成磷灰石晶体,分别在pH 6.5、7.0和7.5下存在和不存在胶原蛋白。应用X射线衍射,透射电子显微镜和选定区域的电子衍射图谱表征晶体。结果表明胶原蛋白在组成和形态上均能调节磷灰石的结晶。在没有胶原的情况下,获得的晶体为pH 6.5的带状磷酸八钙(OCP),OCP和pH 7.0和7.5的纳米棒状羟基磷灰石(HAP)的混合物。如果没有胶原蛋白,OCP将是HAP的前体。在存在胶原蛋白的情况下,与系统中的pH值相比,胶原蛋白在控制HAP结晶方面更有效。带状HAP是pH 6.5的主要相,在pH 7.0时保持非常薄的结构,而在pH 7.5时获得了直径为几纳米的针状HAP。已经讨论了无定形磷酸钙将是存在胶原的HAP的中间相。对生物矿化过程中胶原蛋白和pH控制的这种理解为磷灰石的受控合成提供了新的见解。

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