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通过分析骨涎蛋白和牙本质基质蛋白的功能域, 设计合成了一种非胶原蛋白模拟多肽E8DS (EEEEEEEEDSESSEEDR), 引入胶原蛋白仿生矿化体系, 共同调控磷酸钙晶体的矿化过程。圆二色谱和红外光谱分析结果表明, 多肽E8DS可与钙离子和胶原分子通过静电作用相结合。使用稳态凝胶系统对多肽E8DS的分析结果表明,
E8DS具有很强的调控钙磷盐矿化的能力。多肽的加入有助于胶原纤维的分子组装, 增加了形核位点, 促进了磷酸钙在胶原纤维表面矿化, 使胶原纤维的矿化程度明显提高。

Peptides with sequence (EEEEEEEEDSpESpSp$EEDR) were synthesized to mimic the biomineralization function of non-collagenous protein over the type I collagens. The results show that the peptide can be bound to Ca$^{2+}$and type I collagen by electrostatic interactions. Moreover, synthetic peptide is conducive to calcium ions binding and promotes the nucleation and formation of minerals on the surface of collagen fibrils. Designed peptides also presented a function of accelerating type I collagen fibrillogenesis and the formation of fibrils bundle or network.

参考文献

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[4] G.He, A.George, Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro, Journal of Biological Chemistry, 279(12), 11649(2004)

2 R.Fujisawa, Y.Nodasaka, Y.Kuboki, Further characterization of interaction between bone sialoprotein (BSP) and collagen, Calcified Tissue International, 56(2), 140(1995)

3 C.E.Tye, G.K.Hunter, H.A.Goldberg, Identification of the type I collagen-binding domain of bone sialoprotein and characterization of the mechanism of interaction, Journal of Biological Chemistry, 280(14), 13487(2005)

4 J.J.Hao, A.Ramachandran, A.George, Temporal and spatial localization of the dentin matrix proteins during dentin biomineralization, Journal of Histochemistry &
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