Carr Rachel, Puckrin Robert, McMahon Brian K, Pal Robert, Parker David, Pålsson Lars-Olof
Department of Chemistry, Durham University, South Road, Durham DH1 3LE, UK.
Methods Appl Fluoresc. 2014 Apr 10;2(2):024007. doi: 10.1088/2050-6120/2/2/024007.
A circularly polarized luminescence (CPL) spectrometer has been built and used to study the binding interaction of lactate and four different proteins with racemic Eu and Tb 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 Tb CPL also characterizes the binding interaction of alpha-1-acid glycoprotein with a dissociation constant, K, of 2.5 μM.
已构建了一台圆偏振发光（CPL）光谱仪，并用于研究乳酸与四种不同蛋白质在水溶液中与外消旋铕和铽配合物的结合相互作用。乳酸结合产生强烈的诱导CPL光谱，观察到的发射不对称因子随对映体组成呈线性变化。特别强烈的诱导铽CPL也表征了α-1-酸性糖蛋白的结合相互作用，其解离常数K为2.5 μM。
