Biomolecular Complexation on the "Wrong Side": A Case Study of the Influence of Salts and Sugars on the Interactions between Bovine Serum Albumin and Sodium Polystyrene Sulfonate.
Biomolecular Complexation on the "Wrong Side": A Case Study of the Influence of Salts and Sugars on the Interactions between Bovine Serum Albumin and Sodium Polystyrene Sulfonate.
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DOI：
10.1021/acs.biomac.2c00933
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发表时间：
2022-10-10
影响因子：
6.2
通讯作者：
Lukšič M
中科院分区：
文献类型：
--
作者：
Simončič M;Hritz J;Lukšič M
在蛋白质纯化、药物递送、食品工业和涉及蛋白质-水络合的生物技术应用中，共溶质和溶液条件的适当选择起着至关重要的作用。甚至在蛋白质等离子点的所谓“错误侧”上发生（生物）大分子络合的开始，其中蛋白质和蛋白质都是净带电的。为了深入了解盐（NaCl、NaBr和NaI）和糖（蔗糖和三氯蔗糖）在蛋白质-BSA复合中的调节作用，采用等温滴定量热法、荧光光谱法、圆二色谱法和热力学模型相结合的方法研究了pH = 8.0时牛血清白蛋白（BSA）和聚苯乙烯磺酸钠（NaPSS）之间的相互作用. BSA-NaPSS络合通过两个结合过程进行（首先，形成聚合物内复合物，然后形成互聚物复合物），这两个过程都是由NaPSS的带负电荷的磺酸基（− SO 3-）和BSA表面上带正电荷的补丁之间的有利静电相互作用驱动的。两个这样的积极补丁被确定，每个负责两个结合过程之一。盐的存在下筛选两个大分子之间的短程吸引力和长程排斥静电相互作用，导致两个结合过程的总离子强度上的结合亲和力的非单调依赖性。此外，还观察到了明显的阴离子特异性效应（NaCl < NaBr < NaI）。糖的效果不太明显：蔗糖对络合没有影响，但其氯化类似物，三氯蔗糖，促进它稍微由于BSA和NaPSS之间的长距离排斥静电相互作用的筛选。虽然短程非静电相互作用在文献中经常提到的BSA或NaPSS，我们发现，在“错误的一面”的络合的主要驱动力是静电相互作用。
In the protein purification, drug delivery, food industry, and biotechnological applications involving protein–polyelectrolyte complexation, proper selection of co-solutes and solution conditions plays a crucial role. The onset of (bio)macromolecular complexation occurs even on the so-called “wrong side” of the protein isoionic point where both the protein and the polyelectrolyte are net like-charged. To gain mechanistic insights into the modulatory role of salts (NaCl, NaBr, and NaI) and sugars (sucrose and sucralose) in protein–polyelectrolyte complexation under such conditions, interaction between bovine serum albumin (BSA) and sodium polystyrene sulfonate (NaPSS) at pH = 8.0 was studied by a combination of isothermal titration calorimetry, fluorescence spectroscopy, circular dichroism, and thermodynamic modeling. The BSA–NaPSS complexation proceeds by two binding processes (first, formation of intrapolymer complexes and then formation of interpolymer complexes), both driven by favorable electrostatic interactions between the negatively charged sulfonic groups (−SO3–) of NaPSS and positively charged patches on the BSA surface. Two such positive patches were identified, each responsible for one of the two binding processes. The presence of salts screened both short-range attractive and long-range repulsive electrostatic interactions between both macromolecules, resulting in a nonmonotonic dependence of the binding affinity on the total ionic strength for both binding processes. In addition, distinct anion-specific effects were observed (NaCl < NaBr < NaI). The effect of sugars was less pronounced: sucrose had no effect on the complexation, but its chlorinated analogue, sucralose, promoted it slightly due to the screening of long-range repulsive electrostatic interactions between BSA and NaPSS. Although short-range non-electrostatic interactions are frequently mentioned in the literature in relation to BSA or NaPSS, we found that the main driving force of complexation on the “wrong side” are electrostatic interactions.
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