Extrinsic Fluorescent Dyes as Tools for Protein Characterization

By A. Hawe, M. Sutter, W. Jiskoot. Pharmaceutical Research, 2008

1,133 citations recorded by the source corpus.

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.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c3d2afed45ff1b811c50d13292d8493045badffa

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In Materials Chemistry

1. Hanns-Christian Mahler
2. S. Kiese
3. W. Friess
4. U. Grauschopf

In Molecular Biology

1. Hanns-Christian Mahler
2. S. Kiese
3. W. Friess
4. U. Grauschopf

Citations in the corpus

• Protein aggregation: pathways, induction factors and analysis. (2009, background): “Previously, the use of dyes to measure extrinsic fluorescence has also been reported as a means to analyze protein aggregation.(202) Environment sensitive fluorescent dyes such as Nile red, Congo red, Thioflavin T are considered being useful to detect aggregated proteins through microscopic or spect”