Luminescent Lanthanide-Functionalized Gold Nanoparticles: Exploiting the Interaction with Bovine Serum Albumin for Potential Sensing Applications
Luminescent Lanthanide-Functionalized Gold Nanoparticles: Exploiting the Interaction with Bovine Serum Albumin for Potential Sensing Applications
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DOI：
10.1021/nn201992z
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发表时间：
2011-09-01
期刊：
影响因子：
17.1
通讯作者：
Gunnlaugsson, Thorfinnur
中科院分区：
文献类型：
--
作者：
Comby, Steve;Gunnlaugsson, Thorfinnur
随着发光表面功能化金纳米颗粒在生物医学领域成为潜在的强大分析工具，了解这种系统与蛋白质的相互作用变得至关重要。在本研究中，研究了发光水溶性金纳米颗粒（AuNP-1）的相互作用。研究了Eu-nta)与牛血清白蛋白（BSA）通过C-12烷基硫醇间隔剂连接在金表面的Eu（III）环配合物与萘-二酮天线自组装而得。在生理pH下，监测天线和蛋白质的紫外可见吸收和荧光光谱的变化，以及由此产生的自组装的时间分辨Eu（III）中心发射，作为BSA浓度的函数。结果表明，加入BSA后，unp表面自组装产生的Eu（III）辐射几乎完全被淬灭。结合常数测定清楚地表明，增敏天线没有移位，猝灭是天线与BSA相互作用的结果。对nta-BSA体系进行了详细的光谱研究，更好地了解了这种相互作用的强度及其对蛋白质二级结构的影响。最后，在每个系统上收集的信息导致应用AuNP-1。通过nta-BSA相互作用的扰动，Eu-nta-BSA用于药物的发光检测。使用布洛芬和华法林的竞争性滴定表明，nta位于BSA的结合位点II，而华法林作为一种位点I的药物，并不会干扰II位点布洛芬的检测。
As luminescent surface-functionalized gold nanoparticles emerged as potential powerful analytical tools in the biomedical fields, understanding the interaction of such systems with proteins has become crucial. In the present study, the interaction of luminescent water-soluble gold nanoparticles (AuNP-1 . Eu-nta), obtained through the self-assembly of a naphthalene beta-diketone antenna with a Eu(III) cyclen complex tethered to the gold surface via a C-12 alkyl thiol spacer, with bovine serum albumin (BSA) was investigated. The changes In the UV-visible absorption and fluorescence spectra of both the antenna and protein, as well as in the time-resolved Eu(III)-centered emission, of the resulting self-assembly were monitored, at physiological pH, as a function of the BSA concentration. We demonstrate that the Eu(III) emission arising from the self-assembly on the AuNP surface Is almost completely quenched upon addition of BSA. Binding constant determination clearly showed that the sensitizing antenna was not displaced and that the quenching was the result of the Interaction between the antenna and BSA. Detailed spectroscopic studies performed on the nta-BSA system brought a better insight in the strength of such interaction as well as its effect on the protein secondary structure. Finally, the information gathered on each system resulted in applying AuNP-1 . Eu-nta-BSA for the luminescent detection of drugs via the perturbation of the nta-BSA Interaction. Competitive titrations using ibuprofen and warfarin showed that nta was located in the binding site II of BSA and that the presence of warfarin, a site I drug, did not interfere with the detection of site II ibuprofen.