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红外光谱分析确定了由氧化纳米颗粒对白蛋白的二次结构变化

Masakazu Umezawa^1,2, Ryodai Itano², Naoya Sakaguchi²

¹Department of Medical and Robotic Engineering Design, Faculty of Advanced Engineering, Tokyo University of Science, Tokyo, Japan.

Frontiers in toxicology

|October 11, 2023

概括

氧化纳米粒子影响牛血清白蛋白结构,促进在正电荷表面形成β片. 了解这些相互作用是纳米材料安全生物医学应用的关键.

科学领域:

纳米材料科学科学纳米材料科学
生物化学生物化学
表面化学表面化学

背景情况:

氧化 (CeO2) 纳米颗粒具有抗氧化特性,表明生物医学潜力.
观察到与无机纳米颗粒相互作用时的蛋白质构成变化,但对其理解不佳.
研究这些纳米粒子-蛋白质相互作用对于安全的临床转化至关重要.

研究的目的:

通过与表面修饰的氧化 (CeO2) 纳米粒子相互作用,研究牛血清白蛋白 (BSA) 的二次结构变化.
阐明纳米粒子表面修饰在决定蛋白质结构改变中的作用.
了解用于生物医学应用的纳米粒子-蛋白质相互作用的基本原则.

主要方法:

通过同质沉合成240nm CeO2纳米粒子.
使用多巴胺和3,4-二基酸 (DHCA) 的CeO2纳米颗粒的表面修饰.
使用福里埃变换红外光谱 (FTIR) 分析BSA二次结构变化.

主要成果:

CeO2纳米粒子诱导了BSA二次结构的变化.
在CeO2纳米颗粒的存在下,观察到BSA中β片形成的增加.
这种效应在胺基修饰 (正电荷) CeO2纳米粒子上尤其明显.

结论:

带正电荷的CeO2纳米粒子促进了BSAβ片的形成,这可能是由于局部度和静电相互作用.
纳米颗粒的表面特性显著影响蛋白质结构.
对纳米粒子-蛋白相互作用机制的进一步研究对于氧化纳米粒子的安全生物医学使用至关重要.

关键词:

专辑蛋白 (albumin) 是一种红外光谱测量中的红外光谱.纳米毒理学的纳米毒理学蛋白质构成的结构.蛋白质冠状病毒冠状病毒在β-sheet上使用.

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