Protein-structure-dependent spectral shifts of near-infrared photoluminescence from locally functionalized single-walled carbon nanotubes based on avidin-biotin interactions
Protein-structure-dependent spectral shifts of near-infrared photoluminescence from locally functionalized single-walled carbon nanotubes based on avidin-biotin interactions
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DOI：
10.1039/d2nr01440h
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发表时间：
2022-08-03
期刊：
影响因子：
6.7
通讯作者：
Shiraki，Tomohiro
中科院分区：
文献类型：
--
作者：
Niidome，Yoshiaki;Wakabayashi，Rie;Shiraki，Tomohiro
单壁碳纳米管 (SWCNT) 在近红外 (NIR) 区域（>900 nm）发射光致发光 (PL)。为了增强其 PL 特性，通过局部化学功能化进行缺陷掺杂已被开发出来。局部功能化的 SWCNT (lf-SWCNT) 发射源自缺陷掺杂位点的激子的红移且明亮的 E11* PL。在这里，我们观察到通过 lf-SWCNT 掺杂位点的亲和素-生物素相互作用，蛋白质吸附引起的 E11* PL 能量变化。我们确定亲和素衍生物的结构差异显着影响能量转移。首先，基于重氮化学合成 lf-SWCNT 束缚生物素基团 (lf-SWCNT-b)，然后进行后修饰。研究了 lf-SWCNTs-b 对不同微环境的响应性，并建立了 E11* PL 能量变化与周围溶剂的感应极性参数之间的相关性。中性抗生物素蛋白吸附到 lf-SWCNT-b 上会导致生物素掺杂位点周围的感应极性参数增加，导致 E11* PL 峰红移。与添加中性抗生物素蛋白的情况相比，当引入抗生物素蛋白和链霉抗生物素蛋白时，lf-SWCNTs-b 的 E11* PL 偏移行为发生显着变化。这是由于引入的抗生物素蛋白衍生物的结构特征不同，在生物素掺杂位点形成了不同的微环境。此外，我们使用制造的薄膜装置成功增强了 lf-SWCNTs-b 的检测信号（>三倍），用于链霉亲和素检测。因此，lf-SWCNT 在基于 NIR PL 的先进蛋白质检测/识别设备中的应用展现出巨大的前景。
Single-walled carbon nanotubes (SWCNTs) emit photoluminescence (PL) in the near-infrared (NIR) region (>900 nm). To enhance their PL properties, defect doping via local chemical functionalization has been developed. The locally functionalized SWCNTs (lf-SWCNTs) emit red-shifted and bright E11* PL originating from the excitons localized at the defect-doped sites. Here, we observe the E11* PL energy shifts induced by protein adsorption via the avidin–biotin interactions at the doped sites of lf-SWCNTs. We establish that the difference in the structures of the avidin derivatives notably influences the energy shifts. First, lf-SWCNT-tethering biotin groups (lf-SWCNTs-b) are synthesized based on diazonium chemistry, followed by post-modification. The responsiveness of the lf-SWCNTs-b to different microenvironments is investigated, and a correlation between the E11* PL energy shift and the induction-polarity parameters of surrounding solvents is established. The adsorption of neutravidin onto the lf-SWCNTs-b induces an increase in the induction-polarity parameters around the biotin-doped sites, resulting in the red-shift of the E11* PL peak. The E11* PL shift behaviors of the lf-SWCNTs-b change noticeably when avidin and streptavidin are introduced compared to the case with neutravidin. This is due to the different microenvironments formed at the biotin-doped sites, attributed to the difference in the structural features of the introduced avidin derivatives. Moreover, we successfully enhance the detection signals of lf-SWCNTs-b (>three fold) for streptavidin detection using a fabricated film device. Therefore, lf-SWCNTs exhibit significant promise for application in advanced protein detection/recognition devices based on NIR PL.