College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, China.
J Biomol Struct Dyn. 2024 Aug;42(12):6108-6118. doi: 10.1080/07391102.2023.2232027. Epub 2023 Jul 4.
Bovine serum albumin (BSA), a model protein was used to evaluate the binding behavior of nisoldipine and human serum albumin by a series of experiments and in this article. The outcomes suggested that nisoldipine and BSA formed the nisoldipine-BSA complex with a molar ratio of 1:1, caused the fluorescence quenching of BSA, which quenching mechanism was attributable to static quenching. The binding constant of the nisoldipine-BSA complex was (1.3-3.0) × 10 M at 298-310 K, indicating that nisoldipine on BSA protein had a moderate affinity. During the complexation of nisoldipine with BSA, nisoldipine can spontaneously insert into the site II (subdomain III A) of BSA and the distance of energy transfer from donor group in protein to acceptor group in nisoldipine was 3.21 nm, which led to the change in the hydrophobicity of the microenvironment surrounding Trp residues and in the secondary structure of BSA. Additionally, the findings also confirmed that the hydrogen bond and van der Waals force were responsible for forming the nisoldipine-BSA complex and the complexation process was a spontaneous exothermic process.Communicated by Ramaswamy H. Sarma.
牛血清白蛋白（BSA）是一种模型蛋白，用于通过一系列实验评估硝苯地平与人血清白蛋白的结合行为。结果表明，硝苯地平和 BSA 形成了摩尔比为 1:1 的硝苯地平-BSA 复合物，导致 BSA 的荧光猝灭，猝灭机制归因于静态猝灭。在 298-310 K 下，硝苯地平-BSA 复合物的结合常数为（1.3-3.0）×10^M，表明硝苯地平对 BSA 蛋白具有中等亲和力。在硝苯地平与 BSA 的结合过程中，硝苯地平可以自发插入 BSA 的 II 位（亚域 III A），并且供体基团在蛋白质与硝苯地平的受体基团之间的能量转移距离为 3.21nm，这导致了色氨酸残基周围微环境的疏水性和 BSA 二级结构的变化。此外，研究结果还证实，氢键和范德华力是形成硝苯地平-BSA 复合物的原因，并且复合物的形成过程是一个自发的放热过程。由 Ramaswamy H. Sarma 交流。
