Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly. Issue 4 (4th December 2019)
- Record Type:
- Journal Article
- Title:
- Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly. Issue 4 (4th December 2019)
- Main Title:
- Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly
- Authors:
- Zhong, Qi‐Zhi
Richardson, Joseph J.
Li, Shiyao
Zhang, Wenjie
Ju, Yi
Li, Jianhua
Pan, Shuaijun
Chen, Jingqu
Caruso, Frank - Abstract:
- 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). Abstract : The toolbox of metal–phenolic networks is expanded by enzyme‐mediated assembly, where a range of monophenols are converted into catechol‐containing molecules and cross‐linked by metal ions. This strategy preserves functionality of the monophenol precursors, while conferring benefits ofAbstract: 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). Abstract : The toolbox of metal–phenolic networks is expanded by enzyme‐mediated assembly, where a range of monophenols are converted into catechol‐containing molecules and cross‐linked by metal ions. This strategy preserves functionality of the monophenol precursors, while conferring benefits of catechol‐containing molecules (e.g., universal adhesion) to the networks. … (more)
- Is Part Of:
- Angewandte Chemie international edition. Volume 59:Issue 4(2020)
- Journal:
- Angewandte Chemie international edition
- Issue:
- Volume 59:Issue 4(2020)
- Issue Display:
- Volume 59, Issue 4 (2020)
- Year:
- 2020
- Volume:
- 59
- Issue:
- 4
- Issue Sort Value:
- 2020-0059-0004-0000
- Page Start:
- 1711
- Page End:
- 1717
- Publication Date:
- 2019-12-04
- Subjects:
- metal–organic films -- polyphenols -- self-assembly -- surface modification -- thin films
Chemistry -- Periodicals
540 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1521-3773 ↗
http://www.interscience.wiley.com/jpages/1433-7851 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/anie.201913509 ↗
- Languages:
- English
- ISSNs:
- 1433-7851
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0902.000500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 20865.xml