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通过金属薄膜中的双纳米孔孔径的光透射来观察单个蛋白质结合。

Observing single protein binding by optical transmission through a double nanohole aperture in a metal film.

作者信息

Al Balushi Ahmed A, Zehtabi-Oskuie Ana, Gordon Reuven

机构信息

Department of Electrical and Computer Engineering, University of Victoria, Victoria, BC, V8W3P6, Canada.

出版信息

Biomed Opt Express. 2013 Aug 1;4(9):1504-11. doi: 10.1364/BOE.4.001504. eCollection 2013.

DOI:10.1364/BOE.4.001504
PMID:24049672
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3771822/
Abstract

We experimentally demonstrate protein binding at the single particle level. A double nanohole (DNH) optical trap was used to hold onto a 20 nm biotin-coated polystyrene (PS) particle which subsequently is bound to streptavidin. Biotin-streptavidin binding has been detected by an increase in the optical transmission through the DNH. Similar optical transmission behavior was not observed when streptavidin binding sites where blocked by mixing streptavidin with excess biotin. Furthermore, interaction of non-functionalized PS particles with streptavidin did not induce a change in the optical transmission through the DNH. These results are promising as the DNH trap can make an excellent single molecule resolution sensor which would enable studying biomolecular interactions and dynamics at a single particle/molecule level.

摘要

我们通过实验证明了单颗粒水平上的蛋白质结合。使用双纳米孔(DNH)光阱捕获一个20纳米生物素包被的聚苯乙烯(PS)颗粒,该颗粒随后与链霉亲和素结合。通过DNH的光透射增加已检测到生物素-链霉亲和素结合。当链霉亲和素结合位点被链霉亲和素与过量生物素混合阻断时,未观察到类似的光透射行为。此外,未功能化的PS颗粒与链霉亲和素的相互作用未引起通过DNH的光透射变化。这些结果很有前景,因为DNH阱可以成为一个出色的单分子分辨率传感器,能够在单颗粒/分子水平上研究生物分子相互作用和动力学。

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本文引用的文献

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