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Enzymatic polymerization of enantiomeric L−3,4-dihydroxyphenylalanine into films with enhanced rigidity and stability

Author

Listed:
  • Yuhe Shen

    (Tianjin University)

  • Rongxin Su

    (Tianjin University
    Tianjin Key Laboratory of Membrane Science and Desalination Technology
    Collaborative Innovation Center of Chemical Science and Engineering (Tianjin))

  • Dongzhao Hao

    (Tianjin University)

  • Xiaojian Xu

    (Tianjin University)

  • Meital Reches

    (Institute of Chemistry, the Hebrew University)

  • Jiwei Min

    (Tianjin University)

  • Heng Chang

    (Tianjin University)

  • Tao Yu

    (Tianjin University)

  • Qing Li

    (Tianjin University)

  • Xiaoyu Zhang

    (Tianjin University of Traditional Chinese Medicine)

  • Yuefei Wang

    (Tianjin University of Traditional Chinese Medicine
    Haihe Laboratory of Modern Chinese Medicine)

  • Yuefei Wang

    (Tianjin University
    Tianjin Key Laboratory of Membrane Science and Desalination Technology
    Soochow University)

  • Wei Qi

    (Tianjin University
    Tianjin Key Laboratory of Membrane Science and Desalination Technology
    Collaborative Innovation Center of Chemical Science and Engineering (Tianjin))

Abstract

L−3,4-dihydroxyphenylalanine is an important molecule in the adhesion of mussels, and as an oxidative precursor of natural melanin, it plays an important role in living system. Here, we investigate the effect of the molecular chirality of 3,4-dihydroxyphenylalanine on the properties of the self-assembled films by tyrosinase-induced oxidative polymerization. The kinetics and morphology of pure enantiomers are completely altered upon their co-assembly, allowing the fabrication of layer-to-layer stacked nanostructures and films with improved structural and thermal stability. The different molecular arrangements and self-assembly mechanisms of the L+D-racemic mixtures, whose oxidation products have increased binding energy, resulting in stronger intermolecular forces, which significantly increases the elastic modulus. This study provides a simple pathway for the fabrication of biomimetic polymeric materials with enhanced physicochemical properties by controlling the chirality of monomers.

Suggested Citation

  • Yuhe Shen & Rongxin Su & Dongzhao Hao & Xiaojian Xu & Meital Reches & Jiwei Min & Heng Chang & Tao Yu & Qing Li & Xiaoyu Zhang & Yuefei Wang & Yuefei Wang & Wei Qi, 2023. "Enzymatic polymerization of enantiomeric L−3,4-dihydroxyphenylalanine into films with enhanced rigidity and stability," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38845-3
    DOI: 10.1038/s41467-023-38845-3
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    References listed on IDEAS

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