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首页> 外文期刊>The journal of physical chemistry, C. Nanomaterials and interfaces >Kinetics of Metal-Affinity Driven Self-Assembly between Proteins or Peptides and CdSe-ZnS Quantum Dots
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Kinetics of Metal-Affinity Driven Self-Assembly between Proteins or Peptides and CdSe-ZnS Quantum Dots

机译：蛋白质或多肽与CdSe-ZnS量子点之间金属亲和力驱动的自组装动力学

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摘要

We present a molecular characterization of metal-affinity driven self-assembly between CdSe-ZnS core-shell quantum dots (QDs) and a series of proteins and peptides appended with various length polyhistidine tags. In particular, we investigated the kinetics of self-assembly between surface-immobilized QDs and proteins/peptides under flow conditions, as well as between freely diffusing QDs and proteins/peptides (solution phase). In the first configuration, QDs were immobilized onto functionalized substrates and then exposed to dye-labeled peptides/proteins. Using evanescent wave excitation, we assessed self-assembly by monitoring the time-dependent changes in the dye fluorescence. In solution, the kinetics of self-assembly was monitored via energy transfer between QDs and dye-labeled proteins/peptides. These measurements allowed determination of the kinetic parameters, including the association and dissociation rates (kon and koff) and the apparent binding constant (Kd). We find that self-assembly is rapid with an equilibrium constant Kd-1 1 nM for solution self-assembly, confirming that metal-affinity interactions provide QD bioconjugates that are functional and stable.
机译：我们提出了金属亲和力驱动的CdSe-ZnS核壳量子点（QDs）和一系列蛋白质和多肽与各种长度的多组氨酸标签之间的自组装的分子表征。特别是，我们研究了流动条件下表面固定的QD与蛋白质/肽之间以及自由扩散的QD与蛋白质/肽（溶液相）之间自组装的动力学。在第一种配置中，将QD固定在功能化的底物上，然后暴露于染料标记的肽/蛋白质。使用e逝波激发，我们通过监测染料荧光的时间依赖性变化来评估自组装。在溶液中，通过QD与染料标记的蛋白质/肽之间的能量转移来监测自组装的动力学。这些测量允许确定动力学参数，包括缔合和解离速率（kon和koff）和表观结合常数（Kd）。我们发现自组装是快速的，溶液自组装的平衡常数为Kd-1 1 nM，这证实了金属亲和力相互作用提供了功能稳定的QD生物共轭物。

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