College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, China.
J Biomol Struct Dyn. 2020 Feb;38(3):744-755. doi: 10.1080/07391102.2019.1587515. Epub 2019 Mar 11.
The binding affinity between ritonavir (RTV) and model transport protein, BSA was assessed through multi-spectroscopic approaches and computer simulation. The findings revealed RTV statically quenched the fluorescence of BSA and formed the 1:1 RTV-BSA complex with the binding constant () of 1.06 × 10 ∼ 5.08 × 10 M under the studied temperatures (298 ∼ 310 K). During the interaction of RTV with BSA, the hydrogen bonds and van der Waals forces acted as predominant function while the hydrophobicity played an assistant function. Molecular modeling further verified the result obtained from the competitive binding experiments, RTV preferentially fit into in the sub-domain IIIA of BSA. The perturbation in the secondary structures of BSA upon acting with RTV was observed from IR results, whereas synchronous and 3D fluorescence spectral findings unraveled the slight change in the hydrophobicity surrounding Tyr and Trp residues.Communicated by Ramaswamy H. Sarma.
通过多种光谱方法和计算机模拟评估了利托那韦（RTV）与模型转运蛋白 BSA 之间的结合亲和力。研究结果表明，RTV 静态猝灭了 BSA 的荧光，并在研究温度（298~310 K）下形成了 1:1 的 RTV-BSA 复合物，结合常数（）为 1.06×10∼5.08×10 M。在 RTV 与 BSA 的相互作用过程中，氢键和范德华力起主要作用，疏水力起辅助作用。分子模拟进一步验证了竞争性结合实验的结果，RTV 优先结合 BSA 的 IIIA 亚结构域。从红外结果可以观察到 RTV 作用下 BSA 二级结构的扰动，而同步和三维荧光光谱结果揭示了色氨酸和色氨酸残基周围疏水性的微小变化。由 Ramaswamy H. Sarma 传达。
