Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 7, Pages 2850-2859Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201912848
Keywords
aggregation; encapsulation; proteins; redox chemistry; thin films
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Funding
- National Natural Science Foundation of China [51903147, 51673112, 21875132]
- 111 Project [B14041]
- Distinguished Young Scholars in Shaanxi Province of China [2018JC-018]
- Fundamental Research Funds For the Central Universities [GK201801003, 2017CBY004]
- Open Project of the State Key Laboratory of Supramolecular Structure and Materials [sklssm2019032]
- Natural Science Basic Research Plan in Shaanxi Province of China [2019JQ-162]
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The design and scalable synthesis of robust 2D biological ultrathin films with a tunable structure and function and the ability to be easily transferred to a range of substrates remain key challenges in chemistry and materials science. Herein, we report the use of the thiol-disulfide exchange reaction in the synthesis of a macroscopic 2D ultrathin proteinaceous film with the potential for large-scale fabrication and on-demand encapsulation/release of functional molecules. The reaction between the Cys6-Cys127 disulfide bond of lysozyme and cysteine is chemo- and site-selective. The partially unfolded lysozyme-cysteine monomers aggregate at the air/water or solid/liquid interface to form an ultra-large 2D nanofilm (900 cm(2)) with about 100 % optical transparency. This material adheres to a wide range of substrates and encapsulates and releases a range of molecules without significantly affecting activity.
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