自组装 19F NMR/MRI 纳米探针的蛋白质检测机制的系统研究，以实现合理设计和提高灵敏度,Journal of the American Chemical Society

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自组装 19F NMR/MRI 纳米探针的蛋白质检测机制的系统研究，以实现合理设计和提高灵敏度
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2011-08-03 , DOI: 10.1021/ja203996c
Yousuke Takaoka ₁ , Keishi Kiminami ₁ , Keigo Mizusawa ₁ , Kazuya Matsuo ₁ , Michiko Narazaki ₂ , Tetsuya Matsuda ₂ , Itaru Hamachi _{1,

3}

Affiliation

(19)F NMR/MRI 探针由于其高灵敏度且在活体中没有背景信号，因此有望成为选择性传感生物活性剂的有力工具。我们最近报道了一种使用蛋白质配体束缚自组装 (19) F 探针检测特定蛋白质的独特超分子策略。该方法基于纳米探针的识别驱动拆卸，其诱导了 (19)F NMR/MRI 的清晰开启信号。在本研究中，我们对探针的结构和性质之间的关系进行了系统研究，以详细阐明这种开启（19）F NMR 传感的机制。新合成的 (19) F 探针在响应目标蛋白时表现出三种不同的行为：关闭/开启、始终开启和始终关闭模式。我们清楚地证明了蛋白质反应的这些差异可以用探针聚集体稳定性的差异来解释，并且聚集体的“中等稳定性”在蛋白质检测中产生了理想的开启响应。我们还通过改变探针的疏水性/亲水性平衡成功地控制了聚合稳定性。对检测机制的详细理解使我们能够合理设计具有更高灵敏度的开启（19）F NMR 探针，为（19）F MRI 中的目标蛋白提供更高的图像强度。我们还通过改变探针的疏水性/亲水性平衡成功地控制了聚合稳定性。对检测机制的详细了解使我们能够合理设计具有更高灵敏度的开启（19）F NMR 探针，为（19）F MRI 中的目标蛋白提供更高的图像强度。我们还通过改变探针的疏水性/亲水性平衡成功地控制了聚合稳定性。对检测机制的详细了解使我们能够合理设计具有更高灵敏度的开启（19）F NMR 探针，为（19）F MRI 中的目标蛋白提供更高的图像强度。

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Systematic Study of Protein Detection Mechanism of Self-Assembling19F NMR/MRI Nanoprobes toward Rational Design and Improved Sensitivity

(19)F NMR/MRI probe is expected to be a powerful tool for selective sensing of biologically active agents owing to its high sensitivity and no background signals in live bodies. We have recently reported a unique supramolecular strategy for specific protein detection using a protein ligand-tethered self-assembling (19)F probe. This method is based on a recognition-driven disassembly of the nanoprobes, which induced a clear turn-on signal of (19)F NMR/MRI. In the present study, we conducted a systematic investigation of the relationship between structure and properties of the probe to elucidate the mechanism of this turn-on (19)F NMR sensing in detail. Newly synthesized (19)F probes showed three distinct behaviors in response to the target protein: off/on, always-on, and always-off modes. We clearly demonstrated that these differences in protein response could be explained by differences in the stability of the probe aggregates and that "moderate stability" of the aggregates produced an ideal turn-on response in protein detection. We also successfully controlled the aggregate stability by changing the hydrophobicity/hydrophilicity balance of the probes. The detailed understanding of the detection mechanism allowed us to rationally design a turn-on (19)F NMR probe with improved sensitivity, giving a higher image intensity for the target protein in (19)F MRI.

更新日期：2011-08-03

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