Chakraborty Bishwayan, Santra Asmit, Tah Debangana, Goswami Koushik, Jana Anupam, Girigoswami Agnishwar, Bose Debosreeta
Department of Chemistry, Amity Institute of Applied Sciences, Amity University Kolkata, 700135, India.
Amity Institute of Biotechnology, Amity University Kolkata, 700135, India.
Biophys Chem. 2025 Jul;322:107435. doi: 10.1016/j.bpc.2025.107435. Epub 2025 Mar 13.
In the present article, we have tried to theoretically analyze the structure-function relationship of a novel imidazo pyrimidine derivative, IPD, and decipher its interactions with two serum proteins, BSA and HSA, spectroscopically. IPD is almost non-fluorescent in a polar environment, but its fluorescence enhancement is significant in non-polar mediums like proteins. Steady-state fluorometric investigations indicate a strong binding interaction between the probe, IPD, and serum proteins, with HSA being more strongly bound to IPD. This stronger binding affinity of the IPD-HSA complex than compared to the IPD-BSA complex was corroborated through denaturation and quenching studies, too. In silico molecular docking interactions also reveal a similar stronger binding affinity in HSA than BSA. This is attributed to the probe residing in a more hydrophobic region in HSA; thus, the π and alkyl interactions are stronger in HSA than in BSA.
在本文中，我们试图从理论上分析一种新型咪唑并嘧啶衍生物（IPD）的结构-功能关系，并通过光谱学方法解析其与两种血清蛋白，即牛血清白蛋白（BSA）和人血清白蛋白（HSA）的相互作用。IPD在极性环境中几乎无荧光，但在诸如蛋白质等非极性介质中其荧光增强显著。稳态荧光研究表明，探针IPD与血清蛋白之间存在强烈的结合相互作用，其中HSA与IPD的结合更强。通过变性和猝灭研究也证实了IPD-HSA复合物比IPD-BSA复合物具有更强的结合亲和力。计算机模拟分子对接相互作用也显示HSA中存在比BSA更强的结合亲和力。这归因于探针位于HSA中更疏水的区域；因此，HSA中π和烷基相互作用比BSA中更强。
