Department of Applied Chemistry, China Agricultural University, Beijing 100193, China.
Molecules. 2012 Feb 17;17(2):2000-14. doi: 10.3390/molecules17022000.
A novel type of 2-(un)substituted phenyl-2,3-dihydroquinazolin-4(1H)-one (DQL) derivatives were designed and synthesized to study the impact of halogen substituents on interactions between DQL and human serum albumin (HSA) by comparison methodology. The interactions between DQL and HSA were studied by fluorescence spectroscopy. The intrinsic fluorescence of human serum albumin was quenched by DQL through a static quenching mechanism. Site marker competitive experiments showed that DQL bound to HSA in site II (subdomain IIIA). The binding constants, the numbers of binding sites and the thermodynamic parameters were measured too. The results indicated that the interactions were spontaneous, mainly through hydrophobic forces, and the substitution by halogen atoms in the benzene ring could increase the interactions between DQL and HSA. Furthermore, the binding affinity was enhanced gradually with the increasing of halogen atomic number.
设计并合成了一类新型的 2-(未)取代苯基-2,3-二氢喹唑啉-4(1H)-酮(DQL)衍生物，通过比较方法研究了卤素取代基对 DQL 与人体血清白蛋白(HSA)相互作用的影响。通过荧光光谱法研究了 DQL 与 HSA 之间的相互作用。DQL 通过静态猝灭机制使人体血清白蛋白的内源性荧光猝灭。位点标记竞争实验表明，DQL 结合在 HSA 的 II 位(亚域 IIIA)。还测量了结合常数、结合位点数和热力学参数。结果表明，相互作用是自发的，主要通过疏水作用力，苯环上卤素原子的取代可以增加 DQL 与 HSA 之间的相互作用。此外，随着卤素原子数的增加，结合亲和力逐渐增强。
