首页> 外文期刊>Journal of Bionanoscience >Characterizing the Binding Interaction Between Titanium (IV) Oxide Nanoparticles and Human Serum Albumin: Spectroscopic and Molecular Docking Methods
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Characterizing the Binding Interaction Between Titanium (IV) Oxide Nanoparticles and Human Serum Albumin: Spectroscopic and Molecular Docking Methods

机译:表征钛(IV)氧化物纳米颗粒与人血清白蛋白:光谱和分子对接方法之间的结合相互作用

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摘要

Herein, we have reported the binding interaction between Human Serum Albumin and the titanium dioxide nanoparticles in vitro. Characterization of the nanoparticles physicochemical and morphological properties was done with X-ray Diffraction, Fourier Transform Infra Red, Ramanspectroscopic and microscopic methods. XRD and FT-Raman studies have confirmed the anatase phase of the nanoparticles. Surface active functional groups have been identified from FTIR studies. SEMEDAX has figured out the spherical shape of the particles with their metallic constituents. Hyperchromiceffect observed against the absorbance and the quenching behavior of the nanoparticles on the intrinsic fluorescence of the HSA has confirmed the complex formation to exist via static mechanism. Circular Dichroism studies have dictated the loss in the secondary structures. Docking studiesshowed the binding mode of TNPs-HSA complex system.
机译:在此,我们已经报道了人血清白蛋白和二氧化钛纳米颗粒之间的结合相互作用在体外,含有钛酰胺纳米颗粒。 用X射线衍射,傅里叶变换红外线,ramanspectroscopic和微观方法进行纳米颗粒物理化学和形态学性质的表征。 XRD和FT-Raman研究证实了纳米颗粒的锐钛矿相。 已经从FTIR研究中鉴定了表面活性官能团。 Semredax已经用金属成分计算出颗粒的球形形状。 对吸光度观察的超高速特写以及纳米颗粒对HSA内在荧光的猝灭行为已经证实了通过静态机制存在的复杂形成。 循环二中间主义研究已经决定了二级结构的损失。 对接研究TNPS-HSA复杂系统的绑定模式。

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