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Published on: October 2, 2016
CH-π Interactions Elucidated at the Single-Molecule Level
Qianyuan Ren1,2, Wenying Hao2,3, Lixia Wang4
1College of Food and Bioengineering, Xihua University, Chengdu 610039, China.
None:
CH-π interactions represent a weak yet significant molecular force that is prevalent in diverse biological and chemical systems. Despite compelling evidence supporting the existence of CH-π interactions, experimentally measuring these weak interactions remains challenging due to the coexistence of numerous stronger noncovalent interactions. Here, we construct a refined system to accurately compare the strength of CH-π interactions between phenylalanine derivatives and aliphatic amino acids through molecular exchange processes inside a protein nanopore. Based on a quantitative comparison of binding strengths, we found that CH-π interactions are primarily governed by dispersive attraction, and a more acidic C-H bond results in stronger CH-π interactions, both of which are consistent with the literature. Most importantly, we resolved the long-standing debate regarding the deuterium isotope effect on CH-π interactions and confirmed that deuterium forms weaker CD-π interactions compared to protic CH-π interactions.
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