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

Abstract 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.

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Publication Details

Journal
Polymer Journal
Published
2026-07-24
DOI
https://doi.org/10.1038/s41428-026-01230-0
Primary Topic
Liquid Crystal Research Advancements
Type
article
Field-Weighted Citation Impact
0.00

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article

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

Takashi Kato, Junya Uchida, Rie Makiura, Mina Hasome et al.
Polymer Journal
Liquid Crystal Research Advancements
article

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

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

Abstract

Abstract 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.

Polymer Journal
Shinshu University (JP), Osaka Prefecture University (JP), Okayama University (JP), Cornell University (US), The University of Tokyo (JP)
Japan Society for the Promotion of Science
Openalex Percentile: Top 22%
Liquid Crystal Research Advancements
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Self-assembly and protein-responsive properties of biotin-conjugated fork-like mesogens at aqueous/liquid-crystalline interfaces — Takashi Kato, Junya Uchida, et al. · Polymer Journal (2026) | TGRS Research Map | TGRS