Abstrakti
A novel homogeneous assay system QTR-FRET (Quencher modulated Time-Resolved Förster Resonance Energy Transfer) combining quenching resonance energy transfer (QRET) and time-resolved Förster resonance energy transfer (TR-FRET) was developed to reduce background signal in the conventional energy transfer applications. The TR-FRET functionality is often limited by the lanthanide donor background signal leading to the use of low donor concentration. QTR-FRET reduces this background by introducing soluble quencher molecule, and in this work the concept functionality was proven and compared to previously introduced QRET and TR-FRET technologies. Comparison was performed with three different Eu3+-chelates exhibiting different luminescent lifetime and stability. The side-by-side comparison of the three signaling systems and Eu3+-chelates was demonstrated in a model assay with Eu3+-chelate conjugated biotin and streptavidin (SA) or Cy5-SA conjugate. Comparison of the methodologies showed increased signal-to-background ratios when comparing QTR-FRET to TR-FRET, especially at high Eu3+-biotin concentrations. Quenching the non-bound Eu3+-biotin improved the assay performance, which suggests that an improved assay performance can be attained with the QTR-FRET method. QTR-FRET is expected to be especially useful for Eu3+-labeled ligands with low affinity or assays requiring high Eu3+-ligand concentration. The QTR-FRET indicated potential for multi-analyte approaches separately utilizing the direct QRET-type Eu3+-chelate signal and energy transfer signal readout in a single-well. This potential was hypothesized with Avi-KRAS nucleotide exchange assay as a second biologically relevant model system.
| Alkuperäiskieli | Englanti |
|---|---|
| Sivut | 93-101 |
| Sivumäärä | 9 |
| Julkaisu | Analytica Chimica Acta |
| Vuosikerta | 1092 |
| DOI - pysyväislinkit | |
| Tila | Julkaistu - 19 syysk. 2019 |
| OKM-julkaisutyyppi | A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä |
Rahoitus
This work is supported by the Academy of Finland, Finland (Project IDs: 296225 and 296093 ) and Moikoisten Syöväntutkimussäätiö, Finland . We thank Jonas Kapp from University of Zurich, Switzerland and Dr. William Gillette from Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, MD, USA for providing us the Avi-KRAS and SOS cat proteins. Appendix A
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