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曲通 X-100 和牛血清白蛋白混合物的相分离:多元醇的性质和组成对相关物理化学参数的影响。

Phase separation of triton X-100 and bovine serum albumin mixture: Impacts of nature and composition of polyols on associated physicochemical parameters.

机构信息

Department of Chemistry, Jahangirnagar University, Savar, Dhaka 1342, Bangladesh.

Department of Chemistry, Dhaka University of Engineering & Technology, Gazipur 1707, Bangladesh.

出版信息

Int J Biol Macromol. 2024 Nov;279(Pt 4):135298. doi: 10.1016/j.ijbiomac.2024.135298. Epub 2024 Sep 5.

Abstract

Bovine serum albumin (BSA) is widely used in tissue engineering and pharmaceutical research. It is readily available as a byproduct of the cattle industry, and collected from blood. In this study, we conducted a physicochemical investigation of the phase separation in a mixture of Triton X-100 (TX-100) and BSA, influenced by various polyols, using the well-established cloud point (CP) determination method. The addition of polyols resulted in a significant reduction in CP values for the TX-100 + BSA mixture. The magnitudes of CP in the experimental system were highly varied with different polyols and followed the order of: [Formula: see text] Under identical conditions, the system exhibited maximum solubility in the xylose solution and minimum solubility in the maltose solution. The positive ΔG values were acquired in all working medium imply the nonspontaneity of phase transition in the TX-100 + BSA system. At lower polyol contents, the negative values of standard enthalpy (∆H) and standard entropy (∆S) changes were observed, suggesting that electrostatic forces dominated as the driving force for clouding. At highest employed polyols concentration in some case, the positive values for ∆H and ∆S were achieved, which indicated that hydrophobic interactions likely dominate the phase partitioning of the amphiphile and protein mixture. Additionally, entropy-enthalpy compensation parameters were calculated and analyzed with a rational approach. Molecular docking analysis further demonstrated the presence of hydrogen bonds and hydrophobic interactions between TX-100 and BSA.

摘要

牛血清白蛋白(BSA)广泛应用于组织工程和药物研究领域。它是从牛产业的副产品中提取的,通常从血液中收集。在这项研究中,我们采用已建立的浊点(CP)测定方法,研究了不同多元醇对 Triton X-100(TX-100)和 BSA 混合物相分离的物理化学性质。多元醇的加入导致 TX-100+BSA 混合物的 CP 值显著降低。实验体系的 CP 值大小随不同多元醇而变化很大,遵循以下顺序:[公式:见正文]在相同条件下,体系在木糖溶液中表现出最大的溶解度,在麦芽糖溶液中表现出最小的溶解度。所有工作介质中均获得正值 ΔG,表明 TX-100+BSA 体系的相转变是非自发的。在较低的多元醇含量下,观察到标准焓(∆H)和标准熵(∆S)变化的负值,表明静电力是浊点的主要驱动力。在某些情况下,当使用最高浓度的多元醇时,∆H 和 ∆S 呈现正值,这表明疏水相互作用可能主导两亲物和蛋白质混合物的相分配。此外,还通过合理的方法计算和分析了熵焓补偿参数。分子对接分析进一步证实了 TX-100 和 BSA 之间存在氢键和疏水相互作用。

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