Measuring Protein Structure and Stability of Protein-Nanoparticle Systems with Synchrotron Radiation Circular Dichroism
Measuring Protein Structure and Stability of Protein-Nanoparticle Systems with Synchrotron Radiation Circular Dichroism
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DOI：
10.1021/nl202909s
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发表时间：
2011-10-01
期刊：
影响因子：
10.8
通讯作者：
Calzolai, Luigi
中科院分区：
文献类型：
--
作者：
Laera, Stefania;Ceccone, Giacomo;Calzolai, Luigi
我们测量了纳米分子浓度下蛋白质与纳米颗粒相互作用时的结构和稳定性的变化。使用同步辐射圆二色谱(SRCD)，我们测量了人血清白蛋白与银纳米颗粒相互作用时的热展开降低6摄氏度，而与金的相互作用不发生这种情况。SRCD的使用可以测量蛋白质-纳米颗粒相互作用的关键参数，并将为纳米毒理学提供关键生物蛋白质相对稳定性的实验数据。
We measure the structural and stability changes of proteins at nanomolar concentration upon interaction with nanoparticles. Using synchrotron radiation circular dichroism (SRCD), we measure a decrease of 6 degrees C in the thermal unfolding of human serum albumin upon interaction with silver nanoparticles while this does not happen with gold. The use of SRCD allows measuring critical parameters on protein-nanoparticle interactions, and it will provide experimental data on the relative stability of key biological proteins for nanotoxicology.