Protein binding by functionalized multiwalled carbon nanotubes is governed by the surface chemistry of both parties and the nanotube diameter
Protein binding by functionalized multiwalled carbon nanotubes is governed by the surface chemistry of both parties and the nanotube diameter
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DOI：
10.1021/jp710541j
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发表时间：
2008-03-06
影响因子：
3.7
通讯作者：
Yan, Bing
中科院分区：
文献类型：
--
作者：
Mu, Qingxin;Liu, Wei;Yan, Bing
纳米颗粒的蛋白质结合倾向决定了它们的体内毒性和它们被人类防御系统调理和清除的命运。在这项工作中，蛋白质结合机制的原始和功能化的多壁碳纳米管（f-MWNTs）进行了研究，通过改变f-MWNTs的直径，纳米管表面化学，和蛋白质使用稳态和时间分辨荧光，和圆二色性（CD）光谱。与具有较小直径（类似于10 nm）的那些相比，具有较大直径（类似于40 nm）的f-MWNT通常表现出更强的蛋白结合，这表明纳米颗粒的曲率在确定蛋白结合亲和力中起关键作用。负电荷或空间特性的f-MWNTs增强结合的一些蛋白质，但不是其他的，这表明纳米管和蛋白质的静电和立体化学性质支配纳米管/蛋白质结合。蛋白质荧光寿命没有改变的结合，而强度淬灭，表明通过复合物形成的静态淬灭。CD研究进一步证实了结合诱导的构象变化。
The protein binding propensity of nanoparticles determines their in vivo toxicity and their fate to be opsonized and cleared by human defense systems. In this work, protein-binding mechanisms of pristine and functionalized multiwalled carbon nanotubes (f-MWNTs) were investigated by varying f-MWNTs' diameters, nanotube surface chemistry, and proteins using steady-state and time-resolved fluorescence, and circular dichroism (CD) spectroscopies. The f-MWNTs with a larger diameter (similar to 40 nm) generally exhibited stronger protein binding compared to those with a smaller diameter (similar to 10 nm), demonstrating that the curvature of nanoparticles plays a key role in determining the protein binding affinity. Negative charges or steric properties on f-MWNTs enhanced binding for some proteins but not others, indicating that the electrostatic and stereochemical nature of both nanotubes and proteins govern nanotube/protein binding. Protein fluorescence lifetime was not altered by the binding while the intensity was quenched indicating a static quenching through complex formation. The binding-induced conformational changes were further confirmed by CD studies.