Detection of protein coatings on nanoparticles surfaces by ToF‐SIMS and advanced electron microscopy
Detection of protein coatings on nanoparticles surfaces by ToF‐SIMS and advanced electron microscopy
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利用 ToF-SIMS 和先进电子显微镜检测纳米粒子表面的蛋白质涂层
DOI：
10.1002/sia.5287
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发表时间：
2013
影响因子：
1.7
通讯作者：
H. Wiesmann
中科院分区：
文献类型：
--
作者：
J. Neunzehn;F. Draude;U. Golla‐Schindler;H. Arlinghaus;H. Wiesmann
在这项研究中，利用飞行时间二次离子质谱（ToF - SIMS）和先进的电子显微镜（扫描电子显微镜（SEM）、扫描透射电子显微镜（STEM）和透射电子显微镜（TEM））来检测和分析金纳米颗粒（NP）上不同的纳米级蛋白质涂层。NP包被I型胶原蛋白和纤维连接蛋白以及这些蛋白的不同组合。这两种主要的蛋白在人类细胞组织和组织形成中被ToF‐SIMS通过典型的氨基酸质量峰检测鉴定。此外，通过透射电镜和扫描电镜研究了蛋白质包被颗粒的结构、表面蛋白质层厚度以及NP在不同蛋白质溶液中的反应。在这项研究中，证明了不同蛋白质诱导颗粒团聚的分化。本研究的调查是特异性靶向研究项目CellNanoTox(项目编号：NMP4‐CT‐2006‐032731)由欧盟委员会根据第六届欧盟研究和技术发展框架计划资助。版权所有©2013 John Wiley & Sons， Ltd
In this study, time‐of‐flight secondary ion mass spectrometry (ToF‐SIMS) and advanced electron microscopy (scanning electron microscopy (SEM), scanning transmission electron microscopy (STEM) and transmission electron microscopy (TEM)) were applied to detect and analyse different nano‐scaled protein coatings on gold nanoparticles (NP). The NP were coated with collagen type I and fibronectin as well as different combinations of these proteins. These two main proteins in human cell organization and tissue formation were identified with the aid of ToF‐SIMS by typical amino acid mass peak detection. In addition, the protein‐coated particles were investigated by TEM and SEM to get information about the protein structure, the protein layer thickness on the particle surfaces and the reaction of NP in different protein solutions. In this study, a differentiation of diverse protein induced particle agglomeration was proven. The investigations of this study were part of the Specific Targeted Research Project CellNanoTox (project no. NMP4‐CT‐2006‐032731) funded by the European Commission under the 6th EU Framework Programme for Research and Technological Development. Copyright © 2013 John Wiley & Sons, Ltd.
影响因子：
5.5
作者：
Han, Gang;Ghosh, Partha;Rotello, Vincent M.
通讯作者：
Rotello, Vincent M.