<p>Here, we report on the self-assembly and protein-responsive properties of new bioconjugated fork-like mesogens at aqueous/liquid-crystalline (LC) interfaces. A series of biotin-conjugated fork-like mesogens with different spacer lengths has been designed and synthesized. Self-assembly of these molecules at aqueous/LC interfaces leads to the formation of 2D biofunctional LC materials bearing a specific binding moiety. Protein-responsive ordering transitions of the LC interfaces are induced by mixing biotin-conjugated and biotin-free fork-like mesogens, which results in changes in optical appearance. In addition, the protein-responsive properties are affected by the spacer lengths of the biotin-conjugated fork-like mesogens. These results demonstrate that tuning the density and rigidity of bioconjugated fork-like mesogens at aqueous/LC interfaces is an effective strategy for achieving protein-responsive functions. The relationships between the response properties and chemical structures of monolayers of these molecules formed at air/water interfaces are examined to obtain insights into self-assembly at aquatic interfaces. The results of the present study provide guidance for the design of aquatic functional LC materials with tunable protein responsiveness.</p>

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Self-assembly and protein-responsive properties of biotin-conjugated fork-like mesogens at aqueous/liquid-crystalline interfaces

  • Junya Uchida,
  • Mina Hasome,
  • Jumpei Inomata,
  • Rie Makiura,
  • Nicholas L. Abbott,
  • Takashi Kato

摘要

Here, we report on the self-assembly and protein-responsive properties of new bioconjugated fork-like mesogens at aqueous/liquid-crystalline (LC) interfaces. A series of biotin-conjugated fork-like mesogens with different spacer lengths has been designed and synthesized. Self-assembly of these molecules at aqueous/LC interfaces leads to the formation of 2D biofunctional LC materials bearing a specific binding moiety. Protein-responsive ordering transitions of the LC interfaces are induced by mixing biotin-conjugated and biotin-free fork-like mesogens, which results in changes in optical appearance. In addition, the protein-responsive properties are affected by the spacer lengths of the biotin-conjugated fork-like mesogens. These results demonstrate that tuning the density and rigidity of bioconjugated fork-like mesogens at aqueous/LC interfaces is an effective strategy for achieving protein-responsive functions. The relationships between the response properties and chemical structures of monolayers of these molecules formed at air/water interfaces are examined to obtain insights into self-assembly at aquatic interfaces. The results of the present study provide guidance for the design of aquatic functional LC materials with tunable protein responsiveness.