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The Synthesis of a 2D Ultra‐Large Protein Supramolecular Nanofilm by Chemoselective Thiol–Disulfide Exchange and its Emergent Functions
Author(s) -
Xu Yan,
Liu Yongchun,
Hu Xinyi,
Qin Rongrong,
Su Hao,
Li Juling,
Yang Peng
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201912848
Subject(s) - thiol , monomer , molecule , supramolecular chemistry , chemistry , nanotechnology , disulfide bond , cysteine , fabrication , lysozyme , materials science , combinatorial chemistry , polymer , organic chemistry , enzyme , medicine , biochemistry , alternative medicine , pathology
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.