Protocol for evaluating drug-protein interactions based on fluorescence spectroscopy

Investigating the interactions between ligands, such as drugs, and proteins is essential to understand their functions and effects. This fluorescence spectroscopy protocol details how to analyze the effects of drugs on protein structure, including steps for solution preparation, fluorescence spectra...

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Veröffentlicht in:STAR protocols 2024-12, Vol.5 (4), p.103429, Article 103429
Hauptverfasser: Jalali, Elaheh, Sargolzaei, Javad
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Sprache:eng
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Zusammenfassung:Investigating the interactions between ligands, such as drugs, and proteins is essential to understand their functions and effects. This fluorescence spectroscopy protocol details how to analyze the effects of drugs on protein structure, including steps for solution preparation, fluorescence spectra collection, and results analysis. It is applicable to studying drug-protein interactions, binding affinity, and thermodynamic parameters as well as performing further studies on drug design. For complete details on the use and execution of this protocol, please refer to Jalali et al.1 and Sargolzaei et al.2 [Display omitted] •Instructions for examining drug-protein interaction with fluorescence spectroscopy•Guidance on analyzing binding sites on a protein for a specific drug•Steps for calculating thermodynamic parameters in drug-protein interaction Publisher’s note: Undertaking any experimental protocol requires adherence to local institutional guidelines for laboratory safety and ethics. Investigating the interactions between ligands, such as drugs, and proteins is essential to understand their functions and effects. This fluorescence spectroscopy protocol details how to analyze the effects of drugs on protein structure, including steps for solution preparation, fluorescence spectra collection, and results analysis. It is applicable to studying drug-protein interactions, binding affinity, and thermodynamic parameters as well as performing further studies on drug design.
ISSN:2666-1667
2666-1667
DOI:10.1016/j.xpro.2024.103429