| Literature DB >> 26642428 |
A Sheila Holmes-Smith1, Jacob Crisp1, Firasat Hussain2, Greta R Patzke3, Graham Hungerford4.
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.Entities:
Keywords: LRET; europium; protein; terbium; time-resolved luminescence
Mesh:
Substances:
Year: 2015 PMID: 26642428 DOI: 10.1002/cphc.201500954
Source DB: PubMed Journal: Chemphyschem ISSN: 1439-4235 Impact factor: 3.102