Abstract
A circularly polarized luminescence (CPL) spectrometer has been built and used to study the binding interaction of lactate and four different proteins with racemic EuIII and TbIII complexes in aqueous solution. Lactate binding gives rise to strong induced CPL spectra, and the observed emission dissymmetry factors vary linearly with enantiomeric composition. Particularly strong induced TbIII CPL also characterizes the binding interaction of alpha-1-acid glycoprotein with a dissociation constant, Kd, of 2.5 μM.
Highlights
The use of circularly polarised light in optical spectroscopy is most commonly found in circular dichroism spectroscopy
The emission was fed through a photoelastic modulator (PEM) (Hinds Series II/FS42AA) and through a linear sheet polariser (Comar)
[18] Such behaviour contrasts with examples in the extensive series of complexes based on heptadentate cyclen-derived ligands of lower steric demand, where - hydroxy acids form a 5–ring chelate, involving one carboxylate oxygen and the alcohol OH group, as revealed by crystallographic and NMR analyses. [1921]
Summary
The use of circularly polarised light in optical spectroscopy is most commonly found in circular dichroism spectroscopy Using this technique, the character of the electronic ground state can be elucidated providing an understanding of the molecular conformations of chiral systems. [1,2] CPL spectroscopy is inherently much more sensitive than CD This is due to the fact that the excited state behaviour can be modulated by a number of factors, such as polarity and medium effects or static or dynamic quenching. With CPL it is possible to achieve selective excitation and detection of the sensing emissive complex which ensures a unique signal free from background interference This is of obvious utility when attempting to detect chiral species in vivo. A promising class of chiral emissive probes is based on functionalised lanthanide (LnIII)
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