We use cookies to ensure that we give you the best experience on our website. By continuing to browse this repository, you give consent for essential cookies to be used. You can read more about our Privacy and Cookie Policy.

Durham Research Online
You are in:

Induced europium circularly polarised luminescence monitors reversible drug binding to native α1-acid glycoprotein.

Jennings, L. and Waters, R.S. and Pal, R. and Parker, D. (2017) 'Induced europium circularly polarised luminescence monitors reversible drug binding to native α1-acid glycoprotein.', ChemMedChem., 12 (3). pp. 271-277.


Alpha-1-acid glycoprotein (α1-AGP) is an important blood plasma glycoprotein. Following an acute-phase reaction such as stress, inflammation, burn, or infection, the bloodstream concentration of α1-AGP can increase up to 400 % of its normal concentration. A wide range of drugs is known to bind α1-AGP. Increased binding of pharmacologically active compounds to α1-AGP moderates their clinical effect by decreasing the amount of unbound drug in the bloodstream. This has important clinical ramifications for such applications as the duration of anesthesia and in determining dosage for drug therapy. In this study, the competitive binding to α1-AGP of a dynamically racemic europium(III) complex with seven pharmacologically active drugs absorbing in the range λ 250–290 nm was monitored by following changes in europium total emission and in induced circularly polarized luminescence (CPL). Binding affinities corresponding to Kd values in the range 0.5–100 μm were measured, in good agreement with published data.

Item Type:Article
Full text:(AM) Accepted Manuscript
Download PDF
Publisher Web site:
Publisher statement:This is the peer reviewed version of the following article: L. Jennings, R. S. Waters, R. Pal, D. Parker, ChemMedChem 2017, 12(3), 271-277, which has been published in final form at This article may be used for non-commercial purposes in accordance With Wiley-VCH Terms and Conditions for self-archiving.
Date accepted:15 December 2016
Date deposited:03 March 2017
Date of first online publication:09 January 2017
Date first made open access:09 January 2018

Save or Share this output

Look up in GoogleScholar