Unraveling the origin of chirality from plasmonic nanoparticle-protein complexes
Unraveling the origin of chirality from plasmonic nanoparticle-protein complexes
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DOI：
10.1126/science.aax5415
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发表时间：
2019-09-27
期刊：
影响因子：
56.9
通讯作者：
Link, Stephan
中科院分区：
文献类型：
--
作者：
Zhang, Qingfeng;Hernandez, Taylor;Link, Stephan
等离子激元耦合圆二色谱通过分子手性与表面等离子体的耦合，为生物分子构象的超灵敏检测提供了一种很有前途的方法。没有手性分子存在的手性纳米粒子组装体也具有很大的光学活性。我们应用单粒子圆差分散射光谱结合电子成像和模拟来识别手性蛋白质引起的等离子体聚集体的结构手性和等离子体耦合圆二色谱。我们证明，手性聚集体和非手性组装的颗粒间隙中的少数几个蛋白质都对系综信号负责。但单一的纳米颗粒并不起作用。我们进一步发现，该蛋白质具有两种作用：将手性转移到手性和非手性等离子体底物上。它还负责纳米棒的手性三维组装。了解这些潜在的因素为检测单个生物分子的手性铺平了道路。
Plasmon-coupled circular dichroism has emerged as a promising approach for ultrasensitive detection of biomolecular conformations through coupling between molecular chirality and surface plasmons. Chiral nanoparticle assemblies without chiral molecules present also have large optical activities. We apply single-particle circular differential scattering spectroscopy coupled with electron imaging and simulations to identify both structural chirality of plasmonic aggregates and plasmon-coupled circular dichroism induced by chiral proteins. We establish that both chiral aggregates and just a few proteins in interparticle gaps of achiral assemblies are responsible for the ensemble signal. but single nanoparticles do not contribute. We furthermore find that the protein plays two roles: It transfers chirality to both chiral and achiral plasmonic substrates. and it is also responsible for the chiral three-dimensional assembly of nanorods. Understanding these underlying factors paves the way toward sensing the chirality of single biomolecules.