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Use of Lanthanide-Containing Polyoxometalates to Sensitise the Emission of Fluorescent Labelled Serum Albumin


Holmes-Smith, A Sheila; Crisp, Jacob; Hussain, Firasat; Patzke, Greta R; Hungerford, Graham (2016). Use of Lanthanide-Containing Polyoxometalates to Sensitise the Emission of Fluorescent Labelled Serum Albumin. ChemPhysChem, 17(3):418-424.

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.

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.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:2016
Deposited On:12 Jan 2016 15:32
Last Modified:05 Apr 2016 19:53
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:1439-4235
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1002/cphc.201500954

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