Yin Hang, Cheng Qian, Rosas Roselyne, Viel Stéphane, Monnier Valerie, Charles Laurence, Siri Didier, Gigmes Didier, Yemloul Mehdi, Wang Ruibing, Kermagoret Anthony, Bardelang David
State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau Taipa, Macau, China.
Aix Marseille Univ, CNRS, Centrale Marseille, FSCM, Spectropole, Marseille, France.
Angew Chem Int Ed Engl. 2025 May 26;64(22):e202420880. doi: 10.1002/anie.202420880. Epub 2025 Apr 4.
Allosteric stiffening of a portion of a protein surface is a strategy used in nature to regulate protein oligomerization and provide crucial functions for cells. However, a similar strategy to selectively control part of a compound dynamics remains elusive. Here we show that cucurbit[n]uril (CB[n]) macrocycles can bind almost all portions of a tetratopic guest molecule, stiffening the different parts of the guest to different extents. "Host-guest" interactions were found to be instrumental in selectively "freezing" guest molecular motions. The combination of H-NMR (1D, 2D), DOSY, VT-NMR, isothermal titration calorimetry (ITC), mass spectrometry and molecular modelling enabled to highlight the crucial role of cucurbit[8]uril (CB[8]) binding in the selective hardening of relevant portions of the guest molecule. Beyond implications for bioinspired systems mimicking control of a system dynamic to create a new function, this approach has relevance for improving room temperature phosphorescence, and could also be used to allosterically control organocatalysis in water.
蛋白质表面一部分的变构硬化是自然界中用于调节蛋白质寡聚化并为细胞提供关键功能的一种策略。然而，一种类似的选择性控制化合物动力学部分的策略仍然难以捉摸。在这里，我们表明葫芦[n]脲（CB[n]）大环可以结合四配位客体分子的几乎所有部分，使客体的不同部分以不同程度变硬。发现“主客体”相互作用有助于选择性地“冻结”客体分子运动。1D、2D H-NMR、DOSY、VT-NMR、等温滴定量热法（ITC）、质谱和分子建模的结合能够突出葫芦[8]脲（CB[8]）结合在客体分子相关部分选择性硬化中的关键作用。除了对模仿系统动力学控制以创造新功能的仿生系统有影响外，这种方法与改善室温磷光有关，也可用于变构控制水中的有机催化。
