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电子转移蛋白天青蛋白-金纳米颗粒体系的光学研究

Optical investigation of the electron transfer protein azurin-gold nanoparticle system.

作者信息

Delfino Ines, Cannistraro Salvatore

机构信息

Biophysics and Nanoscience Centre, CNISM, Facoltà di Scienze, Università della Tuscia, Viterbo, Italy.

出版信息

Biophys Chem. 2009 Jan;139(1):1-7. doi: 10.1016/j.bpc.2008.09.016. Epub 2008 Sep 30.

Abstract

The hybrid system obtained by conjugating the protein azurin, which is a very stable and well-described protein showing a unique interplay among its electron transfer and optical properties, with 20-nm sized gold nanoparticles has been investigated. Binding of azurin molecules to gold nanoparticle surface results in the red shift of the nanoparticle resonance plasmon band and in the quenching of the azurin single tryptophan fluorescence signal. These findings together with the estimate of the hydrodynamic radius of the composite, obtained by means of Dynamic Light Scattering, are consistent with the formation of a monolayer of protein molecules, with preserved natural folding, on nanoparticle surface. The fluorescence quenching of azurin bound molecules is explained by an energy transfer from protein to metal surface and it is discussed in terms of the involvement of the Az electron transfer route in the interaction of the protein with the nanoparticle.

摘要

对通过将蛋白质天青蛋白(一种非常稳定且描述详尽的蛋白质,其电子转移和光学性质之间呈现独特的相互作用)与20纳米大小的金纳米颗粒共轭而获得的混合系统进行了研究。天青蛋白分子与金纳米颗粒表面的结合导致纳米颗粒共振等离子体带的红移以及天青蛋白单个色氨酸荧光信号的猝灭。这些发现连同通过动态光散射获得的复合材料流体力学半径的估计结果,与在纳米颗粒表面形成具有保留的天然折叠的蛋白质分子单层是一致的。结合的天青蛋白分子的荧光猝灭是通过从蛋白质到金属表面的能量转移来解释的,并且根据Az电子转移途径在蛋白质与纳米颗粒相互作用中的参与情况进行了讨论。

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