Department of Pharmacy, Yantaishan Hospital Affiliated to Binzhou Medical University, Yantai, China.
Department of Anesthesiology, Yantaishan Hospital Affiliated to Binzhou Medical University, Yantai, China.
Luminescence. 2024 Sep;39(9):e4879. doi: 10.1002/bio.4879.
The binding mechanism of molecular interaction between bicalutamide and human serum albumin (HSA) in a pH 7.4 phosphate buffer was studied using various spectroscopic techniques in combination with molecular modeling. Fluorescence data revealed that the fluorescence quenching of HSA by bicalutamide was a static quenching procedure. The binding constants and number of binding sites were evaluated at different temperatures. The thermodynamic parameters, ΔH and ΔS, were calculated to be 4.30 × 10 J·mol and 245 J·mol·K, respectively, suggesting that the binding of bicalutamide to HSA was driven mainly by hydrophobic interactions and hydrogen bonds. The displacement studies indicated neither Sudlow's site I nor II but subdomain IB as the main binding site for bicalutamide on HSA. The binding distance between bicalutamide and HSA was determined to be 3.54 nm based on the Förster theory. Analysis of circular dichroism, synchronous, and 3D fluorescence spectra demonstrated that HSA conformation was slightly altered in the presence of bicalutamide.
采用多种光谱技术结合分子模拟方法研究了比卡鲁胺与人血清白蛋白（HSA）在 pH 7.4 磷酸盐缓冲液中的分子相互作用的结合机制。荧光数据表明，比卡鲁胺对 HSA 的荧光猝灭是一个静态猝灭过程。在不同温度下评估了结合常数和结合位点数。计算热力学参数ΔH 和 ΔS 分别为 4.30×10 J·mol 和 245 J·mol·K，表明比卡鲁胺与 HSA 的结合主要是由疏水相互作用和氢键驱动的。置换研究表明，比卡鲁胺在 HSA 上的主要结合位点既不是 Sudlow 的位点 I 也不是 II，而是亚域 IB。根据福斯特理论，确定比卡鲁胺与 HSA 之间的结合距离为 3.54nm。圆二色性、同步和 3D 荧光光谱分析表明，HSA 构象在存在比卡鲁胺时略有改变。
