Adsorption of amelogenin onto self-assembled and fluoroapatite surfaces.
Adsorption of amelogenin onto self-assembled and fluoroapatite surfaces.
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DOI：
10.1021/jp804548x
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发表时间：
2009-02-19
期刊：
影响因子：
--
通讯作者：
Shaw WJ
中科院分区：
文献类型：
--
作者：
Tarasevich BJ;Lea S;Bernt W;Engelhard M;Shaw WJ
蛋白质在表面的相互作用对于生物矿化过程以及生物材料的发展和功能具有重要意义。釉原蛋白是一种独特的生物矿化蛋白，因为它可以自组装形成称为“纳米球”的超分子结构，即直径为20 - 60 nm的单体球形聚集体。虽然在溶液中已经观察到纳米球的四级结构，但吸附到表面上的牙釉原蛋白的四级结构也引起了极大的兴趣，因为表面结构对其功能至关重要。我们报告的自组装单分子膜（SAM）与COOH和CH 3端基功能和单晶氟磷灰石（FAP）的釉原蛋白的吸附研究。动态光散射（DLS）实验表明，溶液中含有纳米球和纳米球的聚集体。通过零椭圆偏振仪、X射线光电子能谱（XPS）和外反射傅里叶变换红外光谱（ERFTIR）证明了蛋白质在各种基底上的吸附。虽然在溶液中只观察到纳米球，椭圆偏振法和原子力显微镜（AFM）表明，蛋白质吸附物的结构比原来的纳米球小得多，从单体到小的低聚物的大小。甲烷吸附促进到CH 3表面，和小的低聚物吸附促进到COOH和FAP基板。在某些情况下，原始纳米球的残余物作为多层吸附在下面的亚纳米球层的顶部。虽然小的结构可能存在于溶液中，即使它们没有被DLS检测到，我们还提出，釉原蛋白可能吸附的“脱落”或拆卸的亚结构从纳米球到基板上。这项工作表明，釉原蛋白可能有一系列可能的四级结构，与表面相互作用。
The interactions of proteins at surfaces are of great importance to biomineralizaton processes and to the development and function of biomaterials. Amelogenin is a unique biomineralization protein because it self-assembles to form supramolecular structures called “nanospheres”, spherical aggregates of monomers that are 20−60 nm in diameter. Although the nanosphere quaternary structure has been observed in solution, the quaternary structure of amelogenin adsorbed onto surfaces is also of great interest because the surface structure is critical to its function. We report studies of the adsorption of the amelogenin onto self-assembled monolayers (SAMs) with COOH and CH3 end group functionality and single crystal fluoroapatite (FAP). Dynamic light scattering (DLS) experiments showed that the solutions contained nanospheres and aggregates of nanospheres. Protein adsorption onto the various substrates was evidenced by null ellipsometry, X-ray photoelectron spectroscopy (XPS), and external reflectance Fourier transform infrared spectroscopy (ERFTIR). Although only nanospheres were observed in solution, ellipsometry and atomic force microscopy (AFM) indicated that the protein adsorbates were much smaller structures than the original nanospheres, from monomers to small oligomers in size. Monomer adsorption was promoted onto the CH3 surfaces, and small oligomer adsorption was promoted onto the COOH and FAP substrates. In some cases, remnants of the original nanospheres adsorbed as multilayers on top of the underlying subnanosphere layers. Although the small structures may be present in solution even though they are not detected by DLS, we also propose that amelogenin may adsorb by the “shedding” or disassembling of substructures from the nanospheres onto the substrates. This work suggests that amelogenin may have a range of possible quaternary structures that interact with surfaces.
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影响因子：
3.9
作者：
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3
作者：
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