Extrinsic fluorescent dyes as tools for protein characterization

被引：966

作者：

Hawe, Andrea ^{[1
]}

Sutter, Marc ^{[1
]}

Jiskoot, Wim ^{[1
]}

机构：

[1] Leiden Univ, Leiden Amsterdam Ctr Drug Res, Div Drug Delivery Technol, NL-2300 RA Leiden, Netherlands

来源：

PHARMACEUTICAL RESEARCH | 2008年 / 25卷 / 07期

关键词：

extrinsic fluorescent dyes; fluorescence spectroscopy; protein aggregation; protein characterization; protein folding;

D O I：

10.1007/s11095-007-9516-9

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, e.g. to characterize folding intermediates, measure surface hydrophobicity, and detect aggregation or fibrillation. The main underlying mechanisms, which explain the fluorescence properties of many extrinsic dyes, are solvent relaxation processes and (twisted) intramolecular charge transfer reactions, which are affected by the environment and by interactions of the dyes with proteins. In recent time, the use of extrinsic fluorescent dyes such as ANS, Bis-ANS, Nile Red, Thioflavin T and others has increased, because of their versatility, sensitivity and suitability for high-throughput screening. The intention of this review is to give an overview of available extrinsic dyes, explain their spectral properties, and show illustrative examples of their various applications in protein characterization.

引用

页码：1487 / 1499

页数：13

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[11] Folding pathway of the pyridoxal 5′-phosphate C-S lyase MalY from Escherichia coli [J].