G.A. Krestov Institute of Solution Chemistry of Russian Academy of Sciences, 153045 Ivanovo, Russia.
Structural Bioinformatics and High Performance Computing Research Group (BIO-HPC), Universidad Católica de Murcia (UCAM), 30107 Guadalupe, Spain.
Int J Mol Sci. 2020 Nov 30;21(23):9102. doi: 10.3390/ijms21239102.
The selectivity of encapsulation of leflunomide and teriflunomide by native α-, β- and γ-cyclodextrins was investigated through H NMR and molecular modeling. Thermodynamic analysis revealed the main driving forces involved in the binding. For α-cyclodextrin, the partial encapsulation was obtained while deep penetration was characterized for the other two cyclodextrins, where the remaining polar fragment of the molecule is located outside the macrocyclic cavity. The interactions via hydrogen bonding are responsible for high negative enthalpy and entropy changes accompanying the complexation of cyclodextrins with teriflunomide. These results were in agreement with the molecular modeling calculations, which provide a clearer picture of the involved interactions at the atomic level.
通过核磁共振（1H NMR）和分子模拟研究了 native α-、β-和 γ-环糊精对来氟米特和特立氟胺的包合选择性。热力学分析揭示了结合过程中涉及的主要驱动力。对于 α-环糊精，得到了部分包合；而对于另外两种环糊精，则是深穿透，分子的剩余极性片段位于大环腔之外。氢键相互作用是导致环糊精与特立氟胺络合时焓变和熵变呈负值的主要原因。这些结果与分子模拟计算一致，分子模拟计算在原子水平上更清楚地描绘了涉及的相互作用。
