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Bovine hemoglobin adsorption onto modified silica nanoparticles: Multi-spectroscopic measurements based on kinetics and protein conformation.
International Journal of Biological Macromolecules ( IF 8.2 ) Pub Date : 2020-03-27 , DOI: 10.1016/j.ijbiomac.2020.03.211
Haiyan Yang 1 , Changchun Hao 1 , Zhezhu Nan 1 , Runguang Sun 1
Affiliation  

Herein, the effects of bovine hemoglobin (BHb) binding to hydrophilic silica nanoparticles (SN1) and hydrophobic silica nanoparticles (SN2) were explored under physiological conditions. SEM and XRD were used to characterize silica nanoparticles (SNs). Zeta potential and DLS confirmed the formation of protein corona (PC), and SN2 showed more increase in their size after PC formation comparing with SN1. The adsorption isotherms were fitted well by the Freundlich model, and the kinetics tended to follow pseudo-second-order kinetics. Then, the second structure of BHb has been analyzed by UV-vis and FT-IR spectroscopy, which implied the impact of SN2 on the secondary structure of BHb was greater than that of SN1 on BHb. Moreover, fluorescence spectroscopy and Raman spectroscopy showed that SNs may induce heme degradation to form fluorescent heme product, resulting in increased fluorescence intensity. This investigation will be significant in exploring the toxicity profile of SNs for their in vivo.

中文翻译:

牛血红蛋白吸附到改性二氧化硅纳米颗粒上:基于动力学和蛋白质构象的多光谱测量。

在此,在生理条件下研究了牛血红蛋白(BHb)与亲水性二氧化硅纳米颗粒(SN1)和疏水性二氧化硅纳米颗粒(SN2)结合的作用。SEM和XRD用于表征二氧化硅纳米颗粒(SN)。Zeta电位和DLS证实了蛋白质电晕(PC)的形成,与SN1相比,SN2在PC形成后显示出更大的尺寸增加。吸附等温线通过Freundlich模型拟合得很好,动力学趋于遵循伪二级动力学。然后,通过UV-vis和FT-IR光谱分析了BHb的二级结构,这表明SN2对BHb的二级结构的影响大于SN1对BHb的二级结构的影响。此外,荧光光谱和拉曼光谱显示,SN可能诱导血红素降解,形成荧光血红素产物,导致荧光强度增加。这项研究对于探索SNs在体内的毒性特征将具有重要意义。
更新日期:2020-03-28
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