Holmes-Smith A Sheila, Crisp Jacob, Hussain Firasat, Patzke Greta R, Hungerford Graham
School of Engineering and Built Environment, Glasgow Caledonian University, Cowcaddens Road, Glasgow, G4 0BA, UK.
Department of Chemistry, University of Delhi, Delhi -, 110007, India.
Chemphyschem. 2016 Feb 3;17(3):418-24. doi: 10.1002/cphc.201500954. Epub 2015 Dec 23.
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.
监测生物分子间的相互作用至关重要,而能量转移的应用是阐明纳米级相互作用的主要技术。镧系化合物是用于生物样品的有前景的发光探针,因为它们的发射寿命比任何天然自发荧光都长。多金属氧酸盐(POMs)是结合镧系元素的有趣结构基序,具有低毒性且尺寸适合生物应用。在此,我们使用含有铽或铕的同构POMs,并通过激发镧系元素经由LRET(发光共振能量转移)使蛋白质上的荧光标签敏化,来评估它们与血清白蛋白的相互作用。时间分辨测量表明,POM - 蛋白质系统的能量转移效率超过90%。铽 - POM的结果相对直接,而具有同构铕 - POM的结果因蛋白质对水环境的屏蔽作用而变得复杂。