Synthesis of biopolymer intercalated inorganic-layered materials: Intercalation of collagen peptide and soybean peptide into Zn–Al layered double hydroxide and layered zinc hydroxide

Synthesis of biopolymer intercalated inorganic-layered materials: Intercalation of collagen peptide and soybean peptide into Zn–Al layered double hydroxide and layered zinc hydroxide
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DOI:
10.1016/j.jpcs.2007.10.077
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发表时间:
2008-05
影响因子:
4
通讯作者:
A. Yasutake;S. Aisawa;Satoshi Takahashi;Hidetoshi Hirahara;E. Narita
A. Yasutake;S. Aisawa;Satoshi Takahashi;Hidetoshi Hirahara;E. Narita
中科院分区:
材料科学3区
文献类型:
--
作者:
A. Yasutake;S. Aisawa;Satoshi Takahashi;Hidetoshi Hirahara;E. Narita

文献摘要

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为了开发新型的生物相容性有机/无机纳米杂化材料,采用共沉淀法将胶原肽(CP)和大豆肽(SP)分别嵌入到Zn-Al层状双氢氧化物(LDH)和层状氢氧化锌(LZH)中。用元素分析、X射线粉末衍射、拉曼光谱、热分析和透射电镜对固体产物进行了表征。根据XRD图谱和拉曼光谱,发现固体产物显示出具有层状结构的宽衍射峰,并且掺入了肽。CP/LDH和SP/LDH具有膨胀的LDH结构,d 003 =2- 3 nm,证实两种肽以无序排列插入LDH层间空间。与肽/LDH相比,CP/LZH具有有序的层状结构。CP 1000/LZH和CP 2000/LZH的d值分别为3.0nm和4.4nm,支持CP有序地插入LZH层间空间。这些结果证实了插入肽的取向依赖于肽的氨基酸组成。
In order to develop a new type biocompatible organic/inorganic nanohybrid material, we have been investigated an intercalation of collagen peptides (CP) and soybean peptide (SP) into Zn–Al layered double hydroxide (LDH) and layered zinc hydroxide (LZH) by coprecipitation reaction. The solid products have been characterized by element chemical analysis, powder X-ray diffraction (XRD), Raman spectroscopy, thermal analysis and transmission electron microscopy. According to the XRD patterns and Raman spectra, the solid products were found to show broad diffraction peaks with layered structures and to incorporate peptide. The CP/LDH and SP/LDH has the expanding LDH structure, d003=2–3nm, confirming that both peptides were intercalated into the LDH interlayer space with a disordered arrangement. The CP/LZH has an ordered layered structure in comparison with the peptide/LDH. The d-values are 3.0nm for the CP1000/LZH and 4.4nm for the CP2000/LZH, supporting that CP was orderly intercalated into the LZH interlayer space. These results confirmed that the orientation of the intercalated peptide depends on amino acid composition of peptide.