2,2′-Bithiophene as sensor tag for ligand-protein binding assays based on Förster resonance energy transfer

Ligand-protein binding assays based on intrinsic protein fluorescence are straightforward, inexpensive methods to study ligand-protein interactions. However, their applicability is limited to ligands that can interfere with protein emission. In this Note, we describe the applicability of 2,2′-bithio...

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Hauptverfasser: Behnam, Mira A. M. (VerfasserIn) , Basché, Thomas (VerfasserIn) , Klein, Christian D. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 1 December 2023
In: Analytical biochemistry
Year: 2023, Jahrgang: 682, Pages: 1-7
ISSN:1096-0309
DOI:10.1016/j.ab.2023.115335
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.ab.2023.115335
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0003269723003007
Volltext
Verfasserangaben:Mira A.M. Behnam, Thomas Basché, Christian D.P. Klein
Beschreibung
Zusammenfassung:Ligand-protein binding assays based on intrinsic protein fluorescence are straightforward, inexpensive methods to study ligand-protein interactions. However, their applicability is limited to ligands that can interfere with protein emission. In this Note, we describe the applicability of 2,2′-bithiophene as a FRET-based sensor tag, that can be incorporated into high-affinity ligands to generate target-specific compounds able to quench protein fluorescence upon binding. The generated ligands were assessed in different assay designs. Considerations to account for possible sources of interference with the assay readout are addressed, besides interpretation of the obtained results.
Beschreibung:Gesehen am 17.01.2024
Beschreibung:Online Resource
ISSN:1096-0309
DOI:10.1016/j.ab.2023.115335