The temperature-dependence of host-guest binding thermodynamics: experimental and simulation studies.
The temperature-dependence of host-guest binding thermodynamics: experimental and simulation studies.
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DOI：
10.1039/d3sc01975f
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发表时间：
2023-11-01
期刊：
影响因子：
8.4
通讯作者：
Biedermann, Frank
中科院分区：
文献类型：
--
作者：
Grimm, Laura M.;Setiadi, Jeffry;Tkachenko, Boryslav;Schreiner, Peter R.;Gilson, Michael K.;Biedermann, Frank
主客体结合的热力学参数可以用来描述、理解和预测水体系中的分子识别事件。然而，即使对于这些相对简单的分子，解释结合热力学仍然具有挑战性，因为它们是由直接和溶剂介导的主客体相互作用决定的。在这一贡献中，我们通过实验和计算研究了一系列近刚性、电中性主客体系统的结合热力学，重点研究了水对结合的贡献，并报道了随温度变化的热力学结合贡献ΔGB(T)，ΔHB(T)，ΔSB(T)和ΔCP，b。结合等温滴定热量测量和分子动力学(MD)模拟，我们深入了解了大环主瓜环[n]尿素(CBN，n=7-8)和β-环糊精(β-CD)与一系列客体分子的结合力。我们发现，在这里研究的所有系统以及文献中的主客体系统的结合热容(ΔCp，b)都是负的变化，这表明在更高的温度下结合的热能驱动力增加。我们将这些趋势归因于溶剂化效应，因为水的溶剂性质随着温度的升高而恶化。由于经典疏水效应和非经典疏水效应的符号和大小不同，热容变化对结合的贡献不同，热容变化似乎是水中主客体络合物形成的统一和更一般的特征。这项工作对理解蛋白质-配体相互作用和水环境中的其他复杂体系具有重要意义。通过等温滴定量热和分子动力学模拟，我们证明了热容量负变化(ΔCp，b)是经典疏水效应和非经典疏水效应的统一特征。
The thermodynamic parameters of host–guest binding can be used to describe, understand, and predict molecular recognition events in aqueous systems. However, interpreting binding thermodynamics remains challenging, even for these relatively simple molecules, as they are determined by both direct and solvent-mediated host–guest interactions. In this contribution, we focus on the contributions of water to binding by studying binding thermodynamics, both experimentally and computationally, for a series of nearly rigid, electrically neutral host–guest systems and report the temperature-dependent thermodynamic binding contributions ΔGb(T), ΔHb(T), ΔSb(T), and ΔCp,b. Combining isothermal titration calorimetry (ITC) measurements with molecular dynamics (MD) simulations, we provide insight into the binding forces at play for the macrocyclic hosts cucurbit[n]uril (CBn, n = 7–8) and β-cyclodextrin (β-CD) with a range of guest molecules. We find consistently negative changes in heat capacity on binding (ΔCp,b) for all systems studied herein – as well as for literature host–guest systems – indicating increased enthalpic driving forces for binding at higher temperatures. We ascribe these trends to solvation effects, as the solvent properties of water deteriorate as temperature rises. Unlike the entropic and enthalpic contributions to binding, with their differing signs and magnitudes for the classical and non-classical hydrophobic effect, heat capacity changes appear to be a unifying and more general feature of host–guest complex formation in water. This work has implications for understanding protein–ligand interactions and other complex systems in aqueous environments. Through isothermal titration calorimetry (ITC) and molecular dynamics (MD) simulations, we demonstrate that negative changes in heat capacity (ΔCp,b) are a unifying feature for both the classical and non-classical hydrophobic effect.
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影响因子：
5.7
作者：
de Oliveira, Denilson Mendes;Ben-Amotz, Dor
通讯作者：
Ben-Amotz, Dor
影响因子：
8.4
作者：
Sun H;Hunter CA;Llamas EM
通讯作者：
Llamas EM
影响因子：
3.5
作者：
Amezcua M;El Khoury L;Mobley DL
通讯作者：
Mobley DL
影响因子：
16.6
作者：
Ellermann, Manuel;Jakob-Roetne, Roland;Diederich, Francois
通讯作者：
Diederich, Francois
DOI：
10.1002/anie.201804597
发表时间：
2018-10-22
期刊：
Angewandte Chemie (International ed. in English)
影响因子：
--
作者：
Assaf KI;Nau WM
通讯作者：
Nau WM