Resonance localized surface plasmon spectroscopy: Sensing substrate and inhibitor binding to cytochrome P450
Resonance localized surface plasmon spectroscopy: Sensing substrate and inhibitor binding to cytochrome P450
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DOI：
10.1021/jp801719c
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发表时间：
2008-08-28
影响因子：
3.7
通讯作者：
Van Duyne, Richard P.
中科院分区：
文献类型：
--
作者：
Zhao, Jing;Das, Aditi;Van Duyne, Richard P.
开发了一种基于共振局域表面等离子体光谱的传感方法，用于与血红素蛋白结合的低分子量底物和抑制剂分子。细胞色素 P450 蛋白在可见光波长区域具有 Soret 和 Q 吸收带。 P450 的分子共振与功能化银纳米粒子的局域表面等离子体共振 (LSPR) 之间的耦合导致高度依赖于波长的 LSPR 响应。底物（例如樟脑）或抑制剂（例如咪唑）分子与细胞色素 P450 的结合导致细胞色素 P450 的吸收带分别向更短或更长的波长移动。通过监测纳米传感器的局域表面等离子共振 (LSPR)，樟脑/咪唑与表面经过细胞色素 P450 蛋白修饰的纳米粒子结合，导致 LSPR 发生波长依赖性蓝/红移。樟脑或咪唑引起的 LSPR 偏移的幅度与在溶液中 P450 中观察到的 Soret 带波长偏移一致。
A sensing method based on resonance localized surface plasmon spectroscopy was developed for low molecular weight substrate and inhibitor molecules binding to heme proteins. Cytochrome P450 proteins have Soret and Q absorption bands in the visible wavelength region. The coupling between the molecular resonance of P450 and the localized surface plasmon resonance (LSPR) of functionalized silver nanoparticles leads to a highly wavelength-dependent LSPR response. Binding of substrate (e.g., camphor) or inhibitor (e.g., imidazole) molecules to a cytochrome P450 causes the absorption band of cytochrome P450 shift to shorter or longer wavelengths, respectively. By monitoring the localized surface plasmon resonance (LSPR) of the nanosensors, the binding of camphor/imidazole to a nanoparticle whose surface is modified with cytochrome P450 protein leads to a wavelength-dependent blue/red shift in the LSPR. The magnitude of the LSPR shift induced by camphor or imidazole is consistent with the Soret band wavelength shift observed in P450 in solution.