Quantitative characterization of non-specific interaction of two globular proteins with Dextran T70 in a binary mixture

IF 2.2 4区生物学 Q3 BIOPHYSICS

European Biophysics Journal Pub Date : 2024-10-25 DOI:10.1007/s00249-024-01727-7

Adedayo A. Fodeke

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Abstract

In a bid to quantify the contribution of molecular structure to non-specific interactions leading to functionally important structural changes in cellular processes, the self-interaction of dextran-T70 (DT70) and its interaction with each of bovine serum albumin (BSA) and ovomucoid trypsin inhibitor (OVO) were studied at pH 7.4 between 5 and 37 °C. The dependences of the apparent molecular weight of each of BSA, OVO and DT70 on the concentration of DT70 were independent of temperature. The activity coefficient of the interaction of each species on DT70 concentration was also independent of temperature. The change in activity coefficient was however dependent on the molecular structure and size of the interacting species. The energy of insertion of each macromolecule in DT70 increased in the order DT70 > BSA > OVO. These findings show that although the enthalpic contribution is negligible, the extent of the entropic contribution to the macromolecular activity coefficient of interaction is chiefly the consequence of the exclusion volume of the interacting macromolecules.

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二元混合物中两种球状蛋白质与右旋糖酐 T70 非特异性相互作用的定量表征。

为了量化分子结构对导致细胞过程中重要功能结构变化的非特异性相互作用的贡献，我们研究了葡聚糖-T70（DT70）的自身相互作用以及它与牛血清白蛋白（BSA）和卵磷脂胰蛋白酶抑制剂（OVO）在 5 至 37 °C、pH 值为 7.4 的条件下的相互作用。BSA、OVO 和 DT70 的表观分子量与 DT70 的浓度无关。每种物质相互作用的活性系数对 DT70 浓度的影响也与温度无关。不过，活性系数的变化取决于相互作用物种的分子结构和大小。每种大分子在 DT70 中的插入能按照 DT70 > BSA > OVO 的顺序增加。这些发现表明，虽然焓贡献可以忽略不计，但熵对相互作用的大分子活性系数的贡献程度主要取决于相互作用的大分子的排阻体积。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

European Biophysics Journal 生物-生物物理

CiteScore

4.30

自引率

0.00%

发文量

审稿时长

6-12 weeks

期刊介绍： The journal publishes papers in the field of biophysics, which is defined as the study of biological phenomena by using physical methods and concepts. Original papers, reviews and Biophysics letters are published. The primary goal of this journal is to advance the understanding of biological structure and function by application of the principles of physical science, and by presenting the work in a biophysical context. Papers employing a distinctively biophysical approach at all levels of biological organisation will be considered, as will both experimental and theoretical studies. The criteria for acceptance are scientific content, originality and relevance to biological systems of current interest and importance. Principal areas of interest include: - Structure and dynamics of biological macromolecules - Membrane biophysics and ion channels - Cell biophysics and organisation - Macromolecular assemblies - Biophysical methods and instrumentation - Advanced microscopics - System dynamics.