期刊
JOURNAL OF PHYSICAL CHEMISTRY C
卷 112, 期 9, 页码 3300-3307出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp710541j
关键词
-
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据