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Protein Adsorption On Nanohydroxyapatites: Spectroscopic Investigations At Molecular Level

机译:纳米羟基磷灰石上的蛋白质吸附:分子水平的光谱研究。

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摘要

Proper thermal treatments allowed to modify the number of surface Ca~(2+) able to coordinate water molecules on the surface of hydroxyapatite (HA) nanoparticles surrounded by an amorphous layer. Despite the consequent significant difference in the first hydration level between untreated and treated HA, the amount of adsorbed BSA, used as a model protein, remained essentially unchanged and the native structure of adsorbed protein was retained (as indicated by mid-IR ATR). Near-IR spectroscopy evidenced that adsorbed proteins should be in direct contact with surface Ca~(2+) through a displacement of H_2O molecules by charged acidic residues. In agreement with a previous study that evidenced the heterogeneity of surface Ca~(2+) ions in terms of Lewis acidity, it was then proposed that the adsorption of BSA on such nano-HA should be ruled by some feature of the local structure of surface Ca~(2+) sites, prevailing on the total number of cationic sites exposed and the related features of the first hydration layer.
机译:适当的热处理可以改变能够协调无定形层包围的羟基磷灰石(HA)纳米颗粒表面水分子的Ca〜(2+)数量。尽管未处理的HA和处理的HA之间在第一水合水平上存在显着差异,但是用作模型蛋白的BSA的吸附量基本上保持不变,并且吸附的蛋白的天然结构得以保留(如中红外ATR所示)。近红外光谱表明,吸附的蛋白质应通过带电酸性残基置换H_2O分子而直接与表面Ca〜(2+)直接接触。与先前的研究证明路易斯酸度方面的表面Ca〜(2+)离子具有非均质性的观点相一致,然后提出了BSA在此类纳米HA上的吸附应受其局部结构特征的支配。表面Ca〜(2+)位点,占暴露的阳离子位点总数和第一水化层的相关特征。

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