作者：Yan Xu, Yongchun Liu, Xinyi Hu, Rongrong Qin, Hao Su, Juling Li, Peng Yang*
关键字：Protein nanofilm, Thiol-disulfide exchange reaction, Chemoselectivity, Encapsulation and release, Active proteins
论文来源：期刊
具体来源：Angewandte Chemie International Edition
发表时间：2020年

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 virtually arbitrary substrate remain key challenges in chemistry and materials science. Here, we implicate the potential of the thiol-disulfide exchange reaction in the synthesis of a macroscopic 2D ultrathin proteinaceous film with the potential for scaled-up fabrication and on-demand encapsulation/release of functional molecules. The synthesis success is determined by the chemoselectivity and site-specificity of the reaction between the Cys6-Cys127 disulfide bond of native lysozyme and cysteine, as supported by the superior redox potential of the Cys6-Cys127 disulfide bond over that of other disulfide bonds in native lysozyme and other unreactive proteins. The partially unfolded lysozyme-cysteine conjugate monomers are formed by this strategy, which then further aggregate at the air/water or solid/liquid interface to form an ultralarge 2D nanofilm (e.g., 900 cm2) with ~100% optical transparency. On the basis of amyloid-like aggregation inside the nanofilm, this material presents robust adhesion onto a virtually arbitrary substrate and on-demand controllability to mediate the encapsulation and release of small, mid-sized and large molecules without significant activity loss upon the surface immobilization of active proteins. Our approach provides an important application for the thiol-disulfide exchange reaction in the biocompatible large-scale preparation of 2D proteinaceous nanofilms and coatings with the capability of tunable functional molecular block encapsulation and release.

Angew. Chem. Int. Ed. DOI: 10.1002/anie.201912848 and 10.1002/ange.201912848, Just Accepted.