Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.
Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland; Leibniz-Institut für Lebensmittel-Systembiologie an der Technischen Universität München, 85354 Freising, Germany.
Int J Biol Macromol. 2024 May;266(Pt 2):131134. doi: 10.1016/j.ijbiomac.2024.131134. Epub 2024 Mar 25.
In this article, the binding interactions between bovine serum albumin (BSA) and three 1-alkylsulfonates, namely sodium 1-dodecanesulfonate, sodium 1-decanesulfonate, and sodium 1-octanesulfonate, have been thoroughly investigated. The study employed various experimental techniques such as isothermal titration calorimetry (ITC), steady-state fluorescence spectroscopy (SF), circular dichroism spectroscopy (CD), and molecular dynamics-based simulations. The objective was to understand the influence of the alkyl chain length of the investigated ligands on several aspects, including the strength of the interaction, the stoichiometry of the resulting complexes, the number of BSA binding sites, and the underlying mechanisms of binding. Notably, the study also demonstrated that sodium dodecyl sulfate (S12S) can serve as an effective site marker for BSA when studying ligands with similar structural and topological features. These findings may have significant implications for enhancing our understanding of the interactions between small amphiphilic molecules and proteins.
本文深入研究了牛血清白蛋白（BSA）与三种 1-烷基磺酸盐（1-十二烷磺酸钠、1-癸烷磺酸钠和 1-辛烷磺酸钠）之间的结合相互作用。该研究采用了多种实验技术，如等温热力学滴定（ITC）、稳态荧光光谱（SF）、圆二色光谱（CD）和基于分子动力学的模拟。目的是了解所研究配体的烷基链长度对多个方面的影响，包括相互作用的强度、生成复合物的化学计量比、BSA 结合位点的数量以及结合的潜在机制。值得注意的是，该研究还表明，当研究具有相似结构和拓扑特征的配体时，十二烷基硫酸钠（S12S）可以作为 BSA 的有效位点标记。这些发现可能对增强我们对小分子两亲性分子与蛋白质之间相互作用的理解具有重要意义。
