a Department of Chemistry , Istanbul Medeniyet University , 34700 Istanbul , Turkey.
b Department of Chemistry , Gaziantep University , 27310 Gaziantep , Turkey.
J Biomol Struct Dyn. 2018 Sep;36(12):3114-3121. doi: 10.1080/07391102.2017.1380536. Epub 2017 Oct 3.
The interaction mechanisms of two ethidium derivatives, 3,8-dibenzoylamino-5-ethyl-6-phenylphenantridinium chloride (E2) and 3,8-diphenylacetylamino-5-ethyl-6-phenylphenantridinium chloride (E3) with serum albumins (BSA and HSA) have been investigated by a combined experimental and computational approach. Fluorescence quenching and UV-vis results revealed that the interaction of derivatives with albumins resulted in formation of ground-state complexes and the obtained Stern-Volmer quenching constants designate the presence of a static component in the quenching mechanisms. Thermodynamic parameters (ΔH and ΔS values) point out the ionic interactions play the major role in E2-BSA, E2-HSA and E3-HSA complexes. The van der Waals interactions are dominant forces in E3-BSA complex. Moreover, the obtained results in this study were supported with computational analyzes which have same tendency.
采用实验与计算相结合的方法研究了两种吖啶衍生物，3,8-二苯甲酰氨基-5-乙基-6-苯基菲啶鎓氯化物（E2）和 3,8-二苯乙酰氨基-5-乙基-6-苯基菲啶鎓氯化物（E3）与血清白蛋白（BSA 和 HSA）的相互作用机制。荧光猝灭和紫外-可见结果表明，衍生物与白蛋白的相互作用导致形成基态复合物，所得 Stern-Volmer 猝灭常数表明猝灭机制中存在静态成分。热力学参数（ΔH 和 ΔS 值）表明离子相互作用在 E2-BSA、E2-HSA 和 E3-HSA 复合物中起主要作用。范德华相互作用是 E3-BSA 复合物中的主要作用力。此外，本研究的结果得到了具有相同趋势的计算分析的支持。
