Ercelen Sebnem, Klymchenko Andrey S, Demchenko Alexander P
TUBITAK Research Institute for Genetic Engineering and Biotechnology, 41470 Gebze-Kocaeli, Turkey.
FEBS Lett. 2003 Mar 13;538(1-3):25-8. doi: 10.1016/s0014-5793(03)00116-9.
We report on strong, highly specific and stochiometric binding to bovine serum albumin of novel fluorescence probe FA, 2-(6-diethylaminobenzo[b]furan-2-yl)-3-hydroxychromone, that exhibits a very characteristic two-band fluorescence spectrum. Both absorption band and two fluorescence bands of FA are very sensitive to non-covalent interactions in the immediate environment of the probe. Multiparametric analysis of this spectroscopic information allows us to conclude that the binding site is characterized by very low polarity, high extent of screening from aqueous environment and unusually high electronic polarizability. The latter suggests the proximal location of probe FA to the aromatic amino acid residues in the binding site. The new probe can be proposed for the study of interaction of ligands and drugs of different nature with serum albumins.
我们报道了新型荧光探针FA（2-(6-二乙氨基苯并[b]呋喃-2-基)-3-羟基色酮）与牛血清白蛋白之间存在强的、高度特异性的化学计量结合，该探针呈现出非常独特的双波段荧光光谱。FA的吸收带和两个荧光带对探针紧邻环境中的非共价相互作用都非常敏感。对这些光谱信息进行多参数分析使我们能够得出结论，结合位点的特征是极性非常低、从水性环境中的屏蔽程度高以及电子极化率异常高。后者表明探针FA在结合位点中靠近芳香族氨基酸残基。可以提出将这种新探针用于研究不同性质的配体和药物与血清白蛋白的相互作用。
