Abstract
Monitoring the interaction of biomolecules is important, and the use of energy transfer is a principal technique in elucidating nanoscale interactions. Lanthanide compounds are promising luminescent probes for biological samples as their emission is longer-lived than any native autofluorescence. Polyoxometalates (POMs) are interesting structural motifs to incorporate lanthanides, offering low toxicity and a size pertinent for biological applications. Here, we employ iso-structured POMs containing either terbium or europium and assess their interaction with serum albumin by sensitisation of a fluorescent tag on the protein via LRET (luminescence resonance energy transfer) by exciting the lanthanide. Time-resolved measurements showed energy transfer with an efficiency of over 90% for the POM–protein systems. The Tb–POM results were relatively straightforward, while those with the iso-structured Eu–POM were complicated by the effect of protein shielding from the aqueous environment.
Original language | English |
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Pages (from-to) | 418–424 |
Number of pages | 7 |
Journal | ChemPhysChem : a European Journal of Chemical Physics and Physical Chemistry |
Volume | 17 |
Issue number | 3 |
Early online date | 7 Dec 2015 |
DOIs | |
Publication status | Published - 3 Feb 2016 |
Keywords
- europium
- LRET
- protein
- terbiuim
- time-resolved luminescence
ASJC Scopus subject areas
- Chemistry(all)
- Physics and Astronomy(all)