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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >How does cholinium cation surpass tetraethylammonium cation in amino acid-based ionic liquids for thermal and structural stability of serum albumins?
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How does cholinium cation surpass tetraethylammonium cation in amino acid-based ionic liquids for thermal and structural stability of serum albumins?

机译：Cholinium阳离子如何超越氨基酸基离子液体中的四乙基铵阳离子，用于血清蛋白的热和结构稳定性？

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摘要

In this study, we report how similarly two serum albumins (bovine serum albumin (BSA) and human serum albumin (HSA)) respond in the presence of different concentration of aromatic amino acid based ionic liquids (AAILs), which are cholinium tryptophan [CHO][Trp]lL and tetraethylammonium tryptophan [TEA][Trp]lL Extended results of thermodynamic stability indicate the extent to which both serum albumins differ in their thermal stability despite having structural similarity in presence of AAILs. To efficiently quantify the results, biomolecular interactions studies were carried out between serum albumins and AAILs with the help of differential scanning calorimetry (DSC), dynamic light scattering (DLS) and various spectroscopic techniques. DSC results illustrated that both AAILs are increasing the thermal stability of BSA and HSA, as per transition temperature (T-m) values, BSA (65.51 to 72.46 degrees C) and HSA (65.46 to 75.97 degrees C) have more thermal stability in the presence [CHO][Trp]lL as compare to [TEA][Trp]lL, BSA (65.51 to 69.75 degrees C) and HSA (65.46 to 72.08 degrees C). Secondary structure results obtained using Dichroweb software and selcon calculations. Furthermore, to illustrate the specific binding of AAIL's cations or anions with the binding sites of BSA and HSA, the molecular docking studies were also performed using Molegro trail version v 6.0. (C) 2020 Elsevier B.V. All rights reserved.
机译：在这项研究中，我们报告了两种血清白蛋白（牛血清白蛋白（BSA）和人血清白蛋白（HSA））在不同浓度的芳族氨基酸的离子液体（薯类）存在下，这是胆碱色氨酸的[cho [Trp] L1和四乙基铵色氨酸[TERP] [TRP] LL的热力学稳定性的延长结果表明，尽管在存在八种存在的结构相似之处，但血清白化素蛋白在其热稳定性方面不同的程度。为了有效地量化结果，借助于差示扫描量热法（DSC），动态光散射（DLS）和各种光谱技术，在血清蛋白质和氧气之间进行生物分子相互作用研究。 DSC的结果示出，这两个AAILs正在增加BSA和HSA的热稳定性，如每过渡温度（Tm）的值，BSA（65.51到72.46℃）和HSA（65.46到75.97℃）具有在存在更多的热稳定性[ CHO] [TRP] LL与茶[TRP] LL，BSA（65.51至69.75摄氏度）和HSA（65.46至72.08度）进行比较。二级结构结果使用Dichroweb软件和selcon计算获得。此外，为了说明AAIL的阳离子或阴离子与BSA和HSA的结合位点的特异性结合，也使用MOLEGRO TRAIL VSPRES V 6.0进行分子对接研究。 （c）2020 Elsevier B.v.保留所有权利。

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