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Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly
Author(s) -
Zhong QiZhi,
Richardson Joseph J.,
Li Shiyao,
Zhang Wenjie,
Ju Yi,
Li Jianhua,
Pan Shuaijun,
Chen Jingqu,
Caruso Frank
Publication year - 2020
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201913509
Subject(s) - catechol , molecule , tyrosinase , combinatorial chemistry , catalysis , small molecule , chemistry , nanotechnology , covalent bond , materials science , artificial enzyme , enzyme , organic chemistry , biochemistry
Abstract Functional coatings are of considerable interest because of their fundamental implications for interfacial assembly and promise for numerous applications. Universally adherent materials have recently emerged as versatile functional coatings; however, such coatings are generally limited to catechol, ( ortho ‐diphenol)‐containing molecules, as building blocks. Here, we report a facile, biofriendly enzyme‐mediated strategy for assembling a wide range of molecules (e.g., 14 representative molecules in this study) that do not natively have catechol moieties, including small molecules, peptides, and proteins, on various surfaces, while preserving the molecule's inherent function, such as catalysis (≈80 % retention of enzymatic activity for trypsin). Assembly is achieved by in situ conversion of monophenols into catechols via tyrosinase, where films form on surfaces via covalent and coordination cross‐linking. The resulting coatings are robust, functional (e.g., in protective coatings, biological imaging, and enzymatic catalysis), and versatile for diverse secondary surface‐confined reactions (e.g., biomineralization, metal ion chelation, and N ‐hydroxysuccinimide conjugation).