In Situ Absorption and Fluorescence Microspectroscopy Investigation of the Molecular Incorporation Process into Single Nanoporous Protein Crystals

In Situ Absorption and Fluorescence Microspectroscopy Investigation of the Molecular Incorporation Process into Single Nanoporous Protein Crystals
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原位吸收和荧光显微光谱研究分子掺入单个纳米孔蛋白质晶体的过程

DOI:
10.1021/acsomega.0c01038
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发表时间:
2020
期刊:
影响因子:
4.1
通讯作者:
and Mitsuru Ishikawa
and Mitsuru Ishikawa
中科院分区:
化学3区
文献类型:
--
作者:
Takayuki Uwada;Kohei Kouno;and Mitsuru Ishikawa

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蛋白质晶体表现出独特的三维结构,其中包含有序的纳米多孔溶剂通道,提供了化学异质环境。本文利用荧光染料(包括吖啶黄 G、罗丹明 6G 和曙红 Y)演示了各种分子掺入天然鸡蛋清溶菌酶晶体的溶剂通道中。该过程基于单晶水平的吸收和荧光显微光谱进行了评估。分子加载过程清晰地可视化为时间的函数,并且确定蛋白质晶体可以充当纳米多孔材料。研究发现,掺入过程强烈依赖于分子电荷,导致异质分子聚集,这表明从纳米多孔材料的角度来看蛋白质晶体存在主客体相互作用。
Protein crystals exhibit distinct three-dimensional structures, which contain well-ordered nanoporous solvent channels, providing a chemically heterogeneous environment. In this paper, the incorporation of various molecules into the solvent channels of native hen egg-white lysozyme crystals was demonstrated using fluorescent dyes, including acridine yellow G, rhodamine 6G, and eosin Y. The process was evaluated on the basis of absorption and fluorescence microspectroscopy at a single-crystal level. The molecular loading process was clearly visualized as a function of time, and it was determined that the protein crystals could act as nanoporous materials. It was found that the incorporation process is strongly dependent on the molecular charge, leading to heterogeneous molecular aggregation, which suggests host–guest interaction of protein crystals from the viewpoint of nanoporous materials.
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发表时间: 2005-06-02
影响因子: 3.3
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