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A supramolecular system that strictly follows the binding mechanism of conformational selection

Author

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  • Liu-Pan Yang

    (Southern University of Science and Technology)

  • Li Zhang

    (Southern University of Science and Technology)

  • Mao Quan

    (Southern University of Science and Technology)

  • Jas S. Ward

    (University of Jyvaskyla)

  • Yan-Long Ma

    (Southern University of Science and Technology)

  • Hang Zhou

    (Southern University of Science and Technology)

  • Kari Rissanen

    (University of Jyvaskyla)

  • Wei Jiang

    (Southern University of Science and Technology)

Abstract

Induced fit and conformational selection are two dominant binding mechanisms in biology. Although induced fit has been widely accepted by supramolecular chemists, conformational selection is rarely studied with synthetic systems. In the present research, we report a macrocyclic host whose binding mechanism is unambiguously assigned to conformational selection. The kinetic and thermodynamic aspects of this system are studied in great detail. It reveals that the kinetic equation commonly used for conformational selection is strictly followed here. In addition, two mathematical models are developed to determine the association constants of the same guest to the two host conformations. A “conformational selectivity factor” is defined to quantify the fidelity of conformational selection. Many details about the kinetic and thermodynamic aspects of conformational selection are revealed by this synthetic system. The conclusion and the mathematical models reported here should be helpful in understanding complex molecular recognition in both biological and synthetic systems.

Suggested Citation

  • Liu-Pan Yang & Li Zhang & Mao Quan & Jas S. Ward & Yan-Long Ma & Hang Zhou & Kari Rissanen & Wei Jiang, 2020. "A supramolecular system that strictly follows the binding mechanism of conformational selection," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16534-9
    DOI: 10.1038/s41467-020-16534-9
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    Cited by:

    1. Adam C. Oken & Nicolas E. Lisi & Ismayn A. Ditter & Haoyuan Shi & Nadia A. Nechiporuk & Steven E. Mansoor, 2024. "Cryo-EM structures of the human P2X1 receptor reveal subtype-specific architecture and antagonism by supramolecular ligand-binding," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Xin Sun & Jin-Ku Bai & Yu-Dong Yang & Ke-Lin Zhu & Jia-Qi Liang & Xin-Yue Wang & Jun-Feng Xiang & Xiang Hao & Tong-Ling Liang & Ai-Jiao Guan & Ning-Ning Wu & Han-Yuan Gong, 2024. "Controlled interconversion of macrocyclic atropisomers via defined intermediates," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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