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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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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:允许修改表面的Ca〜(2+)能够与羟基磷灰石的表面上坐标的水分子的数量适当的热处理(HA)的纳米颗粒包围的无定形层。尽管在未处理和处理的HA之间的第一水合程度随之显著差异,吸附的BSA的用作模型蛋白质的量,基本上保持不变和吸附的蛋白质的天然结构被保留(由中间-IR ATR所指示的)。近红外光谱证明该吸附的蛋白质应在通过带电酸性残基H_2O分子的位移与表面的Ca〜(2+)的直接接触。与先前的研究一致认为,证明表面的异质性的Ca〜(2+)在路易斯酸性方面离子时,将其建议BSA的这种纳米羟基磷灰石吸附应的局部结构的某些特征被排除表面的Ca〜(2+)位点,当时的暴露阳离子位点和所述第一水合层的相关特征的总数。

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