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Real-time monitoring of hydrophobic aggregation reveals a critical role of cooperativity in hydrophobic effect

Author

Listed:
  • Liguo Jiang

    (Institute for Advanced Study, The Hong Kong University of Science and Technology
    The Hong Kong University of Science and Technology
    HKUST-Shenzhen Research Institute)

  • Siqin Cao

    (The Hong Kong University of Science and Technology
    HKUST-Shenzhen Research Institute)

  • Peter Pak-Hang Cheung

    (The Hong Kong University of Science and Technology)

  • Xiaoyan Zheng

    (The Hong Kong University of Science and Technology)

  • Chris Wai Tung Leung

    (The Hong Kong University of Science and Technology)

  • Qian Peng

    (Key Laboratory of Organic Solids, Institute of Chemistry, Chinese Academy of Sciences)

  • Zhigang Shuai

    (Tsinghua University)

  • Ben Zhong Tang

    (The Hong Kong University of Science and Technology
    HKUST-Shenzhen Research Institute
    The Hong Kong University of Science and Technology
    Hong Kong Branch of Chinese National Engineering Research Center for Tissue Restoration & Reconstruction, The Hong Kong University of Science and Technology)

  • Shuhuai Yao

    (HKUST-Shenzhen Research Institute
    Hong Kong Branch of Chinese National Engineering Research Center for Tissue Restoration & Reconstruction, The Hong Kong University of Science and Technology
    The Hong Kong University of Science and Technology)

  • Xuhui Huang

    (The Hong Kong University of Science and Technology
    HKUST-Shenzhen Research Institute
    Hong Kong Branch of Chinese National Engineering Research Center for Tissue Restoration & Reconstruction, The Hong Kong University of Science and Technology)

Abstract

The hydrophobic interaction drives nonpolar solutes to aggregate in aqueous solution, and hence plays a critical role in many fundamental processes in nature. An important property intrinsic to hydrophobic interaction is its cooperative nature, which is originated from the collective motions of water hydrogen bond networks surrounding hydrophobic solutes. This property is widely believed to enhance the formation of hydrophobic core in proteins. However, cooperativity in hydrophobic interactions has not been successfully characterized by experiments. Here, we quantify cooperativity in hydrophobic interactions by real-time monitoring the aggregation of hydrophobic solute (hexaphenylsilole, HPS) in a microfluidic mixer. We show that association of a HPS molecule to its aggregate in water occurs at sub-microsecond, and the free energy change is −5.8 to −13.6 kcal mol−1. Most strikingly, we discover that cooperativity constitutes up to 40% of this free energy. Our results provide quantitative evidence for the critical role of cooperativity in hydrophobic interactions.

Suggested Citation

  • Liguo Jiang & Siqin Cao & Peter Pak-Hang Cheung & Xiaoyan Zheng & Chris Wai Tung Leung & Qian Peng & Zhigang Shuai & Ben Zhong Tang & Shuhuai Yao & Xuhui Huang, 2017. "Real-time monitoring of hydrophobic aggregation reveals a critical role of cooperativity in hydrophobic effect," Nature Communications, Nature, vol. 8(1), pages 1-8, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15639
    DOI: 10.1038/ncomms15639
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