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铜离子配位和亚胺键协同构筑的高强耐酸模块化蛋白纤维

Modular Protein Fibers with Outstanding High-Strength and Acid-Resistance Performance Mediated by Copper Ion Binding and Imine Networking.

机构信息

State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, China, 130022.

School of Applied Chemistry and Engineering, University of Science and Technology of China, Hefei, China, 230026.

出版信息

Adv Mater. 2024 Jun;36(24):e2400544. doi: 10.1002/adma.202400544. Epub 2024 Mar 1.

DOI:10.1002/adma.202400544
PMID:38390909
Abstract

Engineered protein fibers are promising biomaterials with diverse applications due to their tunable protein structure and outstanding mechanical properties. However, it remains challenging at the molecular level to achieve satisfied mechanical properties and environmental tolerance simultaneously, especially under extreme acid conditions. Herein, the construction of artificial fibers comprising chimeric proteins made of rigid amyloid peptide and flexible cationic elastin-like protein (ELP) module is reported. The amyloid peptide readily assembles into highly organized β-sheet structures that can be further strengthened by the coordination of Cu, while the flexible ELP module allows the formation of imine-based crosslinking networks. These double networks synergistically enhance the mechanical properties of the fibers, leading to a high tensile strength and toughness, overwhelming many reported recombinant spidroin fibers. Notably, the coordination of Cu with serine residues could stabilize β-sheet structures in the fibers under acidic conditions, which makes the fibers robust against acid, thus enabling their successful utilization in gastric perforation suturing. This work highlights the customization of double networks at the molecular level to create tailored high-performance protein fibers for various application scenarios.

摘要

工程蛋白纤维是一种很有前途的生物材料,由于其可调节的蛋白质结构和出色的机械性能,具有多种应用。然而,在分子水平上同时实现令人满意的机械性能和环境耐受性仍然具有挑战性,特别是在极端酸性条件下。在此,报道了一种由刚性淀粉样肽和柔性阳离子弹性蛋白样蛋白(ELP)模块组成的嵌合蛋白的人工纤维的构建。淀粉样肽易于组装成高度有序的β-折叠结构,而 Cu 的配位可以进一步增强其结构,同时柔性的 ELP 模块允许形成亚胺基交联网络。这些双重网络协同增强了纤维的机械性能,导致其具有高拉伸强度和韧性,超过了许多报道的重组蜘蛛丝纤维。值得注意的是,丝氨酸残基与 Cu 的配位可以在酸性条件下稳定纤维中的β-折叠结构,使纤维具有耐酸能力,从而能够成功用于胃穿孔缝合。这项工作突出了在分子水平上定制双重网络以创建用于各种应用场景的定制化高性能蛋白纤维的重要性。

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