Calcium oxalate crystallization in the presence of amphiphilic phosphoproteins
作者： Yan Liu , Huiyuan Mao , Xifang Liu , Longjiao Qiao , Rong Guo
DOI: 10.1039/C4CE00772G
关键词:
摘要: To gain more insight into protein structure–function relationships that govern biomineralization is an exciting and challenging task. The influence of casein on the crystallization calcium oxalate has been investigated in order to determine roles amphiphilicity phosphate groups proteins morphology phase control crystals. crystals obtained were characterized by scanning electron microscopy, Fourier-transform infrared spectroscopy, X-ray powder diffraction, thermal gravimetric analysis. results show monohydrate (COM) was absence proteins, while dihydrate (COD) presence casein. Casein can be assumed take a key role during dumbbell-shaped COD formation where it serves as effective stabilizing agent for assembles nanorods dumbbell COD. Compared controls containing hydrolysate or bovine serum albumin (BSA), effect arises from electrostatic attraction between well carbonate (especially former) ions assembling mainly comes hydrophobic interaction molecules bound nanorod surfaces. In addition, inhibits process significantly. Our studies may contribute understanding specific amphiphilic phosphoproteins process.
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