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.
|Number of pages||7|
|Journal||ChemPhysChem : a European Journal of Chemical Physics and Physical Chemistry|
|Early online date||7 Dec 2015|
|Publication status||Published - 3 Feb 2016|
- time-resolved luminescence